entry
stringlengths 6
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stringlengths 5
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| protein_name
stringlengths 3
2.44k
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stringlengths 2
35.2k
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stringlengths 7
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O35633
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VIAAT_MOUSE
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Vesicular inhibitory amino acid transporter (Solute carrier family 32 member 1) (Vesicular GABA and glycine transporter) (Vesicular GABA transporter) (mVGAT) (mVIAAT)
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MATLLRSKLTNVATSVSNKSQAKVSGMFARMGFQAATDEEAVGFAHCDDLDFEHRQGLQMDILKSEGEPCGDEGAEAPVEGDIHYQRGGAPLPPSGSKDQAVGAGGEFGGHDKPKITAWEAGWNVTNAIQGMFVLGLPYAILHGGYLGLFLIIFAAVVCCYTGKILIACLYEENEDGEVVRVRDSYVAIANACCAPRFPTLGGRVVNVAQIIELVMTCILYVVVSGNLMYNSFPGLPVSQKSWSIIATAVLLPCAFLKNLKAVSKFSLLCTLAHFVINILVIAYCLSRARDWAWEKVKFYIDVKKFPISIGIIVFSYTSQIFLPSLEGNMQQPSEFHCMMNWTHIAACVLKGLFALVAYLTWADETKEVITDNLPGSIRAVVNLFLVAKALLSYPLPFFAAVEVLEKSLFQEGSRAFFPACYGGDGRLKSWGLTLRCALVVFTLLMAIYVPHFALLMGLTGSLTGAGLCFLLPSLFHLRLLWRKLLWHQVFFDVAIFVIGGICSVSGFVHSLEGLIEAYRTNAED
|
Antiporter that exchanges vesicular protons for cytosolic 4-aminobutanoate or to a lesser extend glycine, thus allowing their secretion from nerve terminals. The transport is equally dependent on the chemical and electrical components of the proton gradient. May also transport beta-alanine (By similarity). Acidification of GABAergic synaptic vesicles is a prerequisite for 4-aminobutanoate uptake.
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O35638
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STAG2_MOUSE
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Cohesin subunit SA-2 (SCC3 homolog 2) (Stromal antigen 2)
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MIAAPEIPTDFNLLQESETHFSSDTDFEDIEGKNQKQGKGKTCKKGKKGPAEKGKSGNGGGKPPSGSNRMNGHHQQNGVENMMLFEVVKMGKSAMQSVVDDWIESYKHDRDIALLDLINFFIQCSGCKGVVTAEMFRHMQNSEIIRKMTEEFDEDSGDYPLTMAGPQWKKFKSSFCEFIGVLVRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSINMDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNAIFKGVFVHRYRDAIAEIRAICIEEIGIWMKMYSDAFLNDSYLKYVGWTMHDKQGEVRLKCLTALQGLYYNKELNSKLELFTSRFKDRIVSMTLDKEYDVAVQAIKLLTLVLQSSEEVLTAEDCENVYHLVYSAHRPVAVAAGEFLYKKLFSRRDPEEDGLMKRRGRQGPNANLVKTLVFFFLESELHEHAAYLVDSMWDCATELLKDWECMNSLLLEEPLSGEEALTDRQESALIEIMLCTIRQAAECHPPVGRGTGKRVLTAKEKKTQLDDRTRITELFAVALPQLLAKYSVDAEKVTNLLQLPQYFDLEIYTTGRLEKHLDALLRQIRNIVEKHTDTDVLEACSKTYHALCNEEFTIFNRVDISRSQLIDELADKFNRLLEDFLQEGEEPDEDDAYQVLSTLKRITAFHNAHDLSKWDLFACNYKLLKTGIENGDMPEQIVIHALQCAHYVILWQLAKITESTSTKEDLLRLKKQMRVFCQICQHYLTNVNTTVKEQAFTILCDILMIFSHQIMSGGRDMLEPLVYTPDSSLQSELLSFILDHVFIEQDDDSNSADGQQEDEASKIEALHKRRNLLAAFCKLIVYTVVEMNTAADIFKQYMKYYNDYGDIIKETMSKTRQIDKIQCAKTLILSLQQLFNEMIQENGYNFDRSSSTFSGIKELARRFALTFGLDQLKTREAIAMLHKDGIEFAFKEPNPQGESHPPLNLAFLDILSEFSSKLLRQDKRTVYVYLEKFMTFQMSLRREDVWLPLMSYRNSLLAGGDDDTMSVISGMSSRGSTVRSKKSKPSTGKRKVVEGMQLALPEESSSSDSMWLSREQTLHTPVMMQTPQLTSTIMREPKRLRPEDSFMSVYPMQAEHHQTPLDYNRRGTSLMEDDEEPIVEDVMMSSEGRIEDLNEGMDFDTMDIDLPPSKNRRERTELKPDFFDPASIMDESVLGVSMF
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Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis (By similarity).
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O35639
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ANXA3_MOUSE
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Annexin A3 (35-alpha calcimedin) (Annexin III) (Annexin-3) (Lipocortin III) (Placental anticoagulant protein III) (PAP-III)
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MASIWVGPRGTIKDYPGFSPSVDAEAIRKAIRGLGTDEKTLINILTERSNAQRQLIVKQYQAAYEQELKDDLKGDLSGHFEHVMVALVTAPALFDAKQLKKSMKGTGTDEDALIEILTTRSSRQMKEISQAYYTVYKKSLGDDISSETSGDFRKALLTLADGRRDESLKVDEHLAKKDAQILYNAGENKWGTDEDKFTEVLCLRSFPQLKLTFDEYRNISQKDIEDSIKGELSGHFEDLLLAIVHCARNTPAFLAERLHQALKGAGTDEFTLNRIMVSRSEIDLLDIRHEFKKHYGYSLYSAIQSDTSGDYRTVLLKICGEDD
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Inhibitor of phospholipase A2, also possesses anti-coagulant properties.
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O35643
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AP1B1_MOUSE
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AP-1 complex subunit beta-1 (Adaptor protein complex AP-1 subunit beta-1) (Adaptor-related protein complex 1 subunit beta-1) (Beta-1-adaptin) (Beta-adaptin 1) (Clathrin assembly protein complex 1 beta large chain) (Golgi adaptor HA1/AP1 adaptin beta subunit)
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MTDSKYFTTTKKGEIFELKAELNSDKKEKKKEAVKKVIASMTVGKDVSALFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNTFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQLVEDQGFLDTLKDLISDSNPMVVANAVAALSEIAESHPSSNLLDLNPQSINKLLTALNECTEWGQIFILDCLANYMPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFMEMLSKDLDYYATLLKKLAPPLVTLLSAEPELQYVALRNINLIVQKRPEILKHEMKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIKDIFRKYPNKYESVIATLCENLDSLDEPEARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLQLLTAIVKLFLKKPTETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVAAKEVVLAEKPLISEETDLIEPTLLDELICYIGTLASVYHKPPNAFVEGGRGVVHKSLPPRTASSESTESPETAPAGAPAGDQPDVIPAQGDLLGDLLNLDLGPPVSGPPLAASSVQMGAVDLLGGGLDSLIGDSNFGAPSASVAAAPAPARLGAPISSGLSDLFDLTSGVGTLSGSYVAPKAVWLPAMKAKGLEISGTFTRQAGSISMDLQLTNKALQVMTDFAIQFNRNSFGLAPAAPLQVHVPLSPNQTVEISLPLNTVGSVLKMEPLNNLQVAVKNNIDVFYFSTLYPLHVLFVEDGKMDRQMFLATWKDIANENEAQFQIRDCPLNTEAASNKLQSSNIFTVAKRNVEGQDMLYQSLKLTNGIWVLAELRIQPGNPSFTLSLKCRAPEVSQHVYQAYETILKN
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Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
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O35646
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CAN6_MOUSE
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Calpain-6
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MGPPLKLFKNQKYQELKQECMKDGRLFCDPTFLPENDSLFFNRLLPGKVVWKRPQDISDDPHLIVGNISNHQLIQGRLGNKAMISAFSCLAVQESHWTKAIPNHKDQEWDPRKPEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLGCYEALDGLTITDIIMDFTGTLAEIIDMQKGRYTDLVEEKYKLFGELYKTFTKGGLICCSIESPSQEEQEVETDWGLLKGYTYTMTDIRKLRLGERLVEVFSTEKLYMVRLRNPLGRQEWSGPWSEISEEWQQLTVTDRKNLGLVMSDDGEFWMSLEDFCHNFHKLNVCRNVNNPVFGRKELESVVGCWTVDDDPLMNRSGGCYNNRDTFLQNPQYIFTVPEDGHKVIMSLQQKDLRTYRRMGRPDNYIIGFELFKVEMNRRFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGSYVLVPTMFQHGRTSEFLLRIFSEVPVQLRELTLDMPKMSCWNLARGYPKVVTQITVHSAEGLEKKYANETVNPYLIIKCGKEEVRSPVQKNTVHAIFDTQAIFYRRTTDIPIIIQVWNSRKFCDQFLGQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLTEL
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Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues.
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O35648
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CETN3_MOUSE
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Centrin-3
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MSLALRGELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDQAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFIAIMTGDI
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Plays a fundamental role in microtubule-organizing center structure and function. As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores.
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O35652
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LHX8_MOUSE
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LIM/homeobox protein Lhx8 (LIM homeobox protein 8) (L3) (LIM/homeobox protein Lhx7) (LIM homeobox protein 7)
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MYWKSDQMFVCKLEGKEVPELAVPREKCPGLMSEECGRPAALAAGRTRKGAGEEGLVNPEGAGDEDSCSSSAPLSPSSSPQSMASGSVCPPGKCVCSSCGLEIVDKYLLKVNDLCWHVRCLSCSVCRTSLGRHTSCYIKDKDIFCKLDYFRRYGTRCSRCGRHIHSTDWVRRAKGNVYHLACFACFSCKRQLSTGEEFALVEEKVLCRVHFDCMLDNLKREVENGNGISVEGALLTEQDVNHPKPAKRARTSFTADQLQVMQAQFAQDNNPDAQTLQKLAERTGLSRRVIQVWFQNCRARHKKHVSPNHSSSAPVTAVPSSRLSPPMLEEMAYSAYVPQDGTMLTALHSYMDAHQQLLDSSPCYPIQ
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Transcription factor involved in differentiation of certain neurons and mesenchymal cells.
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O35655
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PPE1_MOUSE
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Serine/threonine-protein phosphatase with EF-hands 1 (PPEF-1) (EC 3.1.3.16) (DRES10) (Protein phosphatase with EF calcium-binding domain) (PPEF)
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MGCGTSSKKGNKSKKVIKAALVIQNWYRRYRARLRVRQHYALAIFQSIEYSDEQGQMQLSSFFSFMLENYTKTNNEDSALVTRIFDNTRRESQIKDRDDFLGLIEVPDSYDGPRLQFPLTFTDIHILLQAFKQQQILHAHYVLEVLFEARKVLKQMPNFSHVKTFPAKEITICGDLHGKLDDLMLIFYKNGLPSENNPYVFNGDFVDRGNNSMEILMILLVCFLVYPSDLHLNRGNHEDFMMNLRYGFTKEILQKYKLHGRKILQVLEEVYTWLPIGTIIDNEILVIHGGISESTDLNTLHQLQRNKMKSVLMPPVLGNQETGEKRNKSASNYVEPRKVEPDKTPSEDLTKQEWEQIVDILWSDPRGKKGCYPNTSRGGGCYFGPDVTSKVLSKNQLKMLIRSHECKPDGYEVSHDGKVITVFSASNYYEEGSNRGAYIRLSYGTMPQFFQYQVTSTSCLNPLHQRMNAMESSAFKILKEKMISRKTDLINAFELRDHSRSGRISLAEWAFSMENILGLNLPWRSLSSHLVTIDSSGSVDYMSSFDDIRIEKPTKDMKSNLTETMYRYRSDLKIIFNIIDSDQSGLISMDEFRTMWKLFNAHYKAHIDDSQIDELASIVDFNKDGNIDFNEFLKAFYVVHKYDKPGTSLA
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May have a role in the recovery or adaptation response of photoreceptors. May have a role in diverse sensory neurons and in development.
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O35657
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NEUR1_MOUSE
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Sialidase-1 (EC 3.2.1.18) (G9 sialidase) (Lysosomal sialidase) (N-acetyl-alpha-neuraminidase 1)
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MVGADPTRPRGPLSYWAGRRGQGLAAIFLLLVSAAESEARAEDDFSLVQPLVTMEQLLWVSGKQIGSVDTFRIPLITATPRGTLLAFAEARKKSASDEGAKFIAMRRSTDQGSTWSSTAFIVDDGEASDGLNLGAVVNDVDTGIVFLIYTLCAHKVNCQVASTMLVWSKDDGISWSPPRNLSVDIGTEMFAPGPGSGIQKQREPGKGRLIVCGHGTLERDGVFCLLSDDHGASWHYGTGVSGIPFGQPKHDHDFNPDECQPYELPDGSVIINARNQNNYHCRCRIVLRSYDACDTLRPRDVTFDPELVDPVVAAGALATSSGIVFFSNPAHPEFRVNLTLRWSFSNGTSWQKERVQVWPGPSGYSSLTALENSTDGKKQPPQLFVLYEKGLNRYTESISMVKISVYGTL
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Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage.
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O35658
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C1QBP_MOUSE
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Complement component 1 Q subcomponent-binding protein, mitochondrial (GC1q-R protein) (Glycoprotein gC1qBP) (C1qBP)
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MLPLLRCVPRSLGAASGLRTAIPAQPLRHLLQPAPRPCLRPFGLLSVRAGSARRSGLLQPPVPCACGCGALHTEGDKAFVEFLTDEIKEEKKIQKHKSLPKMSGDWELEVNGTEAKLLRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKAEEQEPERTSTPNFVVEVTKTDGKKTLVLDCHYPEDEIGHEDEAESDIFSIKEVSFQATGDSEWRDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKNQ
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Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q specifically binds to the globular 'heads' of C1q thus inhibiting C1 may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense.
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O35659
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GLP1R_MOUSE
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Glucagon-like peptide 1 receptor (GLP-1 receptor) (GLP-1-R) (GLP-1R)
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MASTPSLLRLALLLLGAVGRAGPRPQGTTVSLSETVQKWREYRRQCQRFLTEAPLLATGLFCNRTFDDYACWPDGPPGSFVNVSCPWYLPWASSVLQGHVYRFCTAEGLWLHKDNSSLPWRDLSECEESKRGERNFPEEQLLSLYIIYTVGYALSFSALVIASAILVGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLGCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVFSEQRIFKLYLSIGWGVPLLFVIPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVNFLIFIRVICIVVSKLKANLMCKTDIKCRLAKSTLTLIPLLGTHEVIFAFVMDEHARGTLRFIKLFTELSFTSFQGLMVAILYCFVNNEVQMEFRKCWERWRLEHLNIQRDCSMKPLKCPTSSVSSGATVGSSVYAATCQSSYS
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G-protein coupled receptor for glucagon-like peptide 1 (GLP-1). Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels (By similarity). Plays a role in regulating insulin secretion in response to GLP-1.
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O35664
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INAR2_MOUSE
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Interferon alpha/beta receptor 2 (IFN-R-2) (IFN-alpha/beta receptor 2) (Type I interferon receptor 2)
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MRSRCTVSAVGLLSLCLVVSASLETITPSAFDGYPDEPCTINITIRNSRLILSWELENKSGPPANYTLWYTVMSKDENLTKVKNCSDTTKSSCDVTDKWLEGMESYVVAIVIVHRGDLTVCRCSDYIVPANAPLEPPEFEIVGFTDHINVTMEFPPVTSKIIQEKMKTTPFVIKEQIGDSVRKKHEPKVNNVTGNFTFVLRDLLPKTNYCVSLYFDDDPAIKSPLKCIVLQPGQESGLSESAIVGITTSCLVVMVFVSTIVMLKRIGYICLKDNLPNVLNFRHFLTWIIPERSPSEAIDRLEIIPTNKKKRLWNYDYEDGSDSDEEVPTASVTGYTMHGLTGKPLQQTSDTSASPEDPLHEEDSGAEESDEAGAGAGAEPELPTEAGAGPSEDPTGPYERRKSVLEDSFPREDNSSMDEPGDNIIFNVNLNSVFLRVLHDEDASETLSLEEDTILLDEGPQRTESDLRIAGGDRTQPPLPSLPSQDLWTEDGSSEKSDTSDSDADVGDGYIMR
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Together with IFNAR1, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response. Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another. The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (STAT1, STAT2 and STAT). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes.
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O35668
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HAP1_MOUSE
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Huntingtin-associated protein 1 (HAP-1)
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MRPKEQVQSGAGDGTGSGDPAAGTPTTQPAVGPAPEPSAEPKPAPAQGTGSGQKSGSRTKTGSFCRSMIIGDSDAPWTRYVFQGPYGPRATGLGTGKAEGIWKTPAAYIGRRPGVSGPERAAFIRELQEALCPNPPPTKKITEDDVKVMLYLLEEKERDLNTAARIGQSLVKQNSVLMEENNKLETMLGSAREEILHLRKQVNLRDDLLQLYSDSDDDDDEEDEEDEEEGEEEEREGQRDQDQQHDHPYGAPKPHPKAETAHRCPQLETLQQKLRLLEEENDHLREEASHLDNLEDEEQMLILECVEQFSEASQQMAELSEVLVLRLEGYERQQKEITQLQAEITKLQQRCQSYGAQTEKLQQMLASEKGIHSESLRAGSYMQDYGSRPRDRQEDGKSHRQRSSMPAGSVTHYGYSVPLDALPSFPETLAEELRTSLRKFITDPAYFMERRDTHCREGRKKEQRAMPPPPAQDLKPPEDFEAPEELVPEEELGAIEEVGTAEDGQAEENEQASEETEAWEEVEPEVDETTRMNVVVSALEASGLGPSHLDMKYVLQQLSNWQDAHSKRQQKQKVVPKDSPTPQQQTNMGGGILEQQPRVPTQDSQRLEEDRATHSPSAREEEGPSGAT
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Originally identified as neuronal protein that specifically associates with HTT/huntingtin and the binding is enhanced by an expanded polyglutamine repeat within HTT possibly affecting HAP1 interaction properties. Both HTT and HAP1 are involved in intracellular trafficking and HAP1 is proposed to link HTT to motor proteins and/or transport cargos. Seems to play a role in vesicular transport within neurons and axons such as from early endosomes to late endocytic compartments and to promote neurite outgrowth. The vesicular transport function via association with microtubule-dependent transporters can be attenuated by association with mutant HTT. Involved in the axonal transport of BDNF and its activity-dependent secretion the function seems to involve HTT, DCTN1 and a complex with SORT1. Involved in APP trafficking and seems to facilitate APP anterograde transport and membrane insertion thereby possibly reducing processing into amyloid beta. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptors to synapses the function is dependent on kinesin motor protein KIF5 and is disrupted by HTT with expanded polyglutamine repeat. Involved in regulation of autophagosome motility by promoting efficient retrograde axonal transport. Seems to be involved in regulation of membrane receptor recycling and degradation, and respective signal transduction, including GABA(A) receptors, tyrosine kinase receptors, EGFR, IP3 receptor and androgen receptor. Among others suggested to be involved in control of feeding behavior (involving hypothalamic GABA(A) receptors), cerebellar and brainstem development (involving AHI1 and NTRK1/TrkA), postnatal neurogenesis (involving hypothalamic NTRK2/TrkB regulating the number of Npyr1-expressing cells), and ITPR1/InsP3R1-mediated Ca(2+) release (involving HTT and possibly the effect of mutant HTT). Via association with DCTN1/dynactin p150-glued and HTT/huntingtin involved in cytoplasmic retention of REST in neurons. May be involved in ciliogenesiss however, reports are conflicting: PubMed:21985783 reports that Hap1 is required for ciliogenesis in primary cortical neurons and proposes that HTT interacts with PCM1 through HAP1 PubMed:23532844 reports that mice with disrupted Hap1 display normal cilium formation and function. Involved in regulation of exocytosis. Isoform A but not isoform B seems to be involved in formation of cytoplasmic inclusion bodies (STBs). In case of anomalous expression of TBP, can sequester a subset of TBP into STBs sequestration is enhanced by an expanded polyglutamine repeat within TBP.
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O35671
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ITBP1_MOUSE
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Integrin beta-1-binding protein 1 (Bodenin)
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MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNSNLDTCAEFRIKYVGAIEKLAVSEGKSLEGPLDLINYIDVAQQDGKLPFVPLEEEFILGVSKYGIKVSTTDQHGVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSDKS
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Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter.
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O35674
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ADA19_MOUSE
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Disintegrin and metalloproteinase domain-containing protein 19 (ADAM 19) (EC 3.4.24.-) (Meltrin-beta)
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MPGRAGVARFCLLALALQLHWPLAACEPGWTTRGSQEGSPPLQHELIIPQWRTSESPGRGKHPLRAELRVMAEGRELILDLEKNEHLFAPAYTETCYTASGNPQTSTLKSEDHCFYHGTVRDVDESSVTLSTCRGIRGLIIVRSNLSYIIEPVPNSDSQHRIYRSEHLTLPPGNCGFEHSGPTSKDWALQFTHQTKKQPRRMKREDLHSMKYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRKLLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHCCSASAADGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMPDTRTLYGGRRCGNGYLEDGEECDCGEEEECKNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYYQMDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKGLNGQYRKCSPRDAKCGKIQCQSTQARPLESNAVSIDTTITLNGRRIHCRGTHVYRGPEEEEGEGDMLDPGLVMTGTKCGHNHICFEGQCRNTSFFETEGCGKKCNGHGVCNNNKNCHCFPGWSPPFCNTPGDGGSVDSGPLPPKSVGPVIAGVFSALFVLAVLVLLCHCYRQSHKLGKPSALPFKLRHQFSCPFRVSQSGGTGHANPTFKLQTPQGKRKVTNTPESLRKPSHPPPRPPPDYLRVESPPAPLPAHLNRAAGSSPEAGARIERKESARRPPPSRPMPPAPNCLLSQDFSRPRPPQKALPANPVPGQRTGPRSGGTSLLQPPTSGPQPPRPPAVPVPKLPEYRSQRVGAIISSKI
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Participates in the proteolytic processing of beta-type neuregulin isoforms which are involved in neurogenesis and synaptogenesis, suggesting a regulatory role in glial cell. Also cleaves alpha-2 macroglobulin. May be involved in osteoblast differentiation and/or osteoblast activity in bone (By similarity). {ECO:0000250, ECO:0000269|PubMed:11116142}.
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O35678
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MGLL_MOUSE
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Monoglyceride lipase (MGL) (EC 3.1.1.23) (Monoacylglycerol lipase) (MAGL)
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MPEASSPRRTPQNVPYQDLPHLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRIAAAGAGCPP
|
Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain. Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (By similarity).
|
O35681
|
SYT3_MOUSE
|
Synaptotagmin-3 (Synaptotagmin III) (SytIII)
|
MSGDYEDDLCRRALILVSDLCARVRDADTNDRCQEFNELRIRGYPRGPDADISVSLLSVIVTFCGIVLLGVSLFVSWKLCWVPWRDKGGSAVGGGPLRKDLAPGVGLAGLVGGGGHHLGASLGGHPLLGGPHHHGHTAHHPPFAELLEPGGLGGSEPPEPSYLDMDSYPEAAVASVVAAGVKPSQTSPELPSEGGTGSGLLLLPPSGGGLPSAQSHQQVTSLAPTTRYPALPRPLTQQTLTTQADPSTEERPPALPLPLPGGEEKAKLIGQIKPELYQGTGPGGRRGGGSGEAGAPCGRISFALRYLYGSDHLVVRILQALDLPAKDSNGFSDPYVKIYLLPDRKKKFQTKVHRKTLNPIFNETFQFSVPLAELAQRKLHFSVYDFDRFSRHDLIGQVVLDNLLELAEQPPDRPLWRDILEGGSEKADLGELNFSLCYLPTAGRLTVTIIKASNLKAMDLTGFSDPYVKASLISEGRRLKKRKTSIKKNTLNPTYNEALVFDVAPESVENVGLSIAVVDYDCIGHNEVIGVCRVGPEAADPHGREHWAEMLANPRKPVEHWHQLVEEKTLSSFTKGGKGLSEKENSE
|
Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain. Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes both actions contribute to triggering exocytosis. Plays a role in dendrite formation by melanocytes.
|
O35685
|
NUDC_MOUSE
|
Nuclear migration protein nudC (Nuclear distribution protein C homolog) (Silica-induced gene 92 protein) (SIG-92)
|
MGGEQEEERFDGMLLAMAQQHEGGVQELVNTFFSFLRRKTDFFIGGEEGMAEKLITQTFNHHNQLAQKARREKRARQETERREKAERAARLAKEAKAETPGPQIKELTDEEAERLQLEIDQKKDAEDQEAQLKNGSLDSPGKQDAEDEEDEEDEKDKGKLKPNLGNGADLPNYRWTQTLAELDLAVPFRVSFRLKGKDVVVDIQRRHLRVGLKGQPPVVDGELYNEVKVEESSWLIEDGKVVTVHLEKINKMEWWNRLVTSDPEINTKKINPENSKLSDLDSETRSMVEKMMYDQRQKSMGLPTSDEQKKQEILKKFMDQHPEMDFSKAKFN
|
Plays a role in neurogenesis and neuronal migration. Necessary for correct formation of mitotic spindles and chromosome separation during mitosis (By similarity). Necessary for cytokinesis and cell proliferation (By similarity).
|
O35696
|
SIA8B_MOUSE
|
Alpha-2,8-sialyltransferase 8B (EC 2.4.99.-) (Polysialic acid synthase) (Sialyltransferase 8B) (SIAT8-B) (Sialyltransferase St8Sia II) (ST8SiaII) (Sialyltransferase X) (STX)
|
MQLQFRSWMLAALTLLVVFLIFADISEIEEEIGNSGGRGTIRSAVNSLHSKSNRAEVVINGSSPPAVADRSNESLKHNIQPASSKWRHNQTLSLRIRKQILKFLDAEKDISVLKGTLKPGDIIHYIFDRDSTMNVSQNLYELLPRTSPLKNKHFQTCAIVGNSGVLLNSGCGQEIDTHSFVIRCNLAPVQEYARDVGLKTDLVTMNPSVIQRAFEDLVNATWREKLLQRLHGLNGSILWIPAFMARGGKERVEWVNALILKHHVNVRTAYPSLRLLHAVRGYWLTNKVHIKRPTTGLLMYTLATRFCNQIYLYGFWPFPLDQNQNPVKYHYYDSLKYGYTSQASPHTMPLEFKALKSLHEQGALKLTVGQCDGAT
|
May transfer sialic acid through alpha-2,8-linkages to the alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked oligosaccharides of glycoproteins and may be involved in PSA (polysialic acid) expression.
|
O35701
|
MATN3_MOUSE
|
Matrilin-3
|
MLLSAPLRHLPGLLLLLWPLLLLPSLAAPGRLARASVRRLGTRVPGGSPGHLSALATSTRAPYSGGRGAGVCKSRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTGTMSGLAIQTAMEEAFTVEAGARGPMSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASKPLEEHVFYVETYGVIEKLSARFQETFCALDQCMLGTHQCQHVCVSDGDGKHHCECSQGYTLNADGKTCSAIDKCALSTHGCEQICVNDRNGSYHCECYGGYALNADRRTCAALDKCASGTHGCQHICVNDGAGSHHCECFEGYTLNADKKTCSVRNKCALGTHGCQHICVSDGAVAYHCDCFPGYTLNDDKKTCSDIEEARSLISIEDACGCGATLAFQEKVSSHLQKLNTKLDNILKKLKVTEYGQVHR
|
Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks.
|
O35704
|
SPTC1_MOUSE
|
Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1)
|
MATVAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSKNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVSGLKVVGESLSPALHLQLEESTGSREKDVKLLQAIVDQCMDKGIALTQARYLDKEEKCLPPPSIRVVVTVEQTEEELQRAASTIREAAQAVLL
|
Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates. The SPTLC1-SPTLC2-SPTSSB complex displays a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme has the ability to use a broader range of acyl-CoAs (By similarity). Required for adipocyte cell viability and metabolic homeostasis.
|
O35710
|
NOCT_MOUSE
|
Nocturnin (EC 3.1.3.108) (Carbon catabolite repression 4-like protein)
|
MYQSPRRLCSALLLRDAPGLRRTLVPGPRRTLAPPVLGSRPKSPQLQAAAASGAARSRPRTVSSMGNGTSRLYSALAKTVNSSAAAQHPEYLVSTDPEHLEPIDPKELLEECRAVLHTRPPRYQRDFVDLRTDCSSSHSPIRVMQWNILAQALGEGKDNFVQCPVEALKWEERKCLILEEILAYQPDILCLQEVDHYFDTFQPLLSRLGYQGTFFPKPWSPCLDVEHNNGPDGCALFFLQNRFKLISSTNIRLTAMTLKTNQVAIAQTLECKESGRQFCIAVTHLKARTGWERFRSAQGCDLLQNLQNITQGAKIPLIVCGDFNAEPTEEVYKHFASSSLNLNSAYKLLSPDGQSEPPYTTWKIRTSGECRHTLDYIWYSRHALSVTSALDLLTEEQIGPNRLPSFHYPSDHLSLVCDFSFNEEPHELF
|
Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (By similarity). Shows a small preference for NADPH over NADP(+) (By similarity). Represses translation and promotes degradation of target mRNA molecules (By similarity). Plays an important role in post-transcriptional regulation of metabolic genes under circadian control. Exerts a rhythmic post-transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis. Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance. Promotes adipogenesis by facilitating PPARG nuclear translocation which activates its transcriptional activity. Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone. Critical for proper development of early embryos.
|
O35714
|
TNR18_MOUSE
|
Tumor necrosis factor receptor superfamily member 18 (Glucocorticoid-induced TNFR-related protein) (CD antigen CD357)
|
MGAWAMLYGVSMLCVLDLGQPSVVEEPGCGPGKVQNGSGNNTRCCSLYAPGKEDCPKERCICVTPEYHCGDPQCKICKHYPCQPGQRVESQGDIVFGFRCVACAMGTFSAGRDGHCRLWTNCSQFGFLTMFPGNKTHNAVCIPEPLPTEQYGHLTVIFLVMAACIFFLTTVQLGLHIWQLRRQHMCPRETQPFAEVQLSAEDACSFQFPEEERGEQTEEKCHLGGRWP
|
Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway (By similarity).
|
O35716
|
SOCS1_MOUSE
|
Suppressor of cytokine signaling 1 (SOCS-1) (JAK-binding protein) (JAB) (STAT-induced STAT inhibitor 1) (SSI-1)
|
MVARNQVAADNAISPAAEPRRRSEPSSSSSSSSPAAPVRPRPCPAVPAPAPGDTHFRTFRSHSDYRRITRTSALLDACGFYWGPLSVHGAHERLRAEPVGTFLVRDSRQRNCFFALSVKMASGPTSIRVHFQAGRFHLDGSRETFDCLFELLEHYVAAPRRMLGAPLRQRRVRPLQELCRQRIVAAVGRENLARIPLNPVLRDYLSSFPFQI
|
Essential negative regulator of type I and type II interferon (IFN) signaling, as well as that of other cytokines, including IL2, IL4, IL6 and leukemia inhibitory factor (LIF). Downregulates cytokine signaling by inhibiting the JAK/STAT signaling pathway. Acts by binding to JAK proteins and to IFNGR1 and inhibiting their kinase activity. In vitro, suppresses Tec protein-tyrosine activity (By similarity). Regulates IFN-gamma (IFNG)-mediated sensory neuron survival. Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
|
O35717
|
SOCS2_MOUSE
|
Suppressor of cytokine signaling 2 (SOCS-2) (Cytokine-inducible SH2 protein 2) (CIS-2)
|
MTLRCLEPSGNGADRTRSQWGTAGLPEEQSPEAARLAKALRELSQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVHLYLTKPLYTSAPTLQHFCRLAINKCTGTIWGLPLPTRLKDYLEEYKFQV
|
SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
|
O35718
|
SOCS3_MOUSE
|
Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (Protein EF-10)
|
MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGTPSFSLPPTEPSSEVPEQPPAQALPGSTPKRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL
|
SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
|
O35719
|
RA51B_MOUSE
|
DNA repair protein RAD51 homolog 2 (R51H2) (RAD51 homolog B) (RAD51-like protein 1)
|
MSSKKLRRVGLSPELCDRLSRYQIVNCQHFLSLSPLELMKVTGLSYRGVHELLHTVSKACAPQMQTAYELKTRRSAHLSPAFLSTTLCALDEALHGGVPCGSLTEITGPPGCGKTQFCIMMSVLATLPTSLGGLEGAVVYIDTESAFTAERLVEIAESRFPQYFNTEEKLLLTSSRVHLCRELTCEGLLQRLESLEEEIISKGVKLVIVDSIASVVRKEFDPKLQGNIKERNKFLGKGASLLKYLAGEFSIPVILTNQITTHLSGALPSQADLVSPADDLSLSEGTSGSSCLVAALGNTWGHCVNTRLILQYLDSERRQILIAKSPLAAFTSFVYTIKGEGLVLQGHERP
|
Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. May promote the assembly of presynaptic RAD51 nucleoprotein filaments. Binds single-stranded DNA and double-stranded DNA and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway.
|
O35728
|
CP4AE_MOUSE
|
Cytochrome P450 4A14 (CYPIVA14) (Lauric acid hydroxylase)
|
MGFFLFSPTRYLDGISGFFQWAFLLSLFLVLFKAVQFYLRRQWLLKTLQHFPCMPSHWLWGHHLKDKELQQILIWVEKFPSACLQCLSGSNIRVLLYDPDYVKVVLGRSDPKASGIYQFFAPWIGYGLLLLNGKKWFQHRRMLTPAFHYDILKPYVKIMADSVNIMLDKWEKLDGQDHPLEIFHCVSLMTLDTVMKCAFSYQGSVQLDENSKLYTKAVEDLNNLTFFRLRNAFYKYNIIYNMSSDGRLSHHACQIAHEHTDGVIKMRKSQLQNEEELQKARKKRHLDFLDILLFARMEDRNSLSDEDLRAEVDTFMFEGHDTTASGISWIFYALATHPEHQQRCREEVQSILGDGTSVTWDHLGQMPYTTMCIKEALRLYPPVISVSRELSSPVTFPDGRSIPKGITATISIYGLHHNPRFWPNPKVFDPSRFAPDSSHHSHAYLPFSGGSRNCIGKQFAMNELKVAVALTLLRFELLPDPTRIPVPIARLVLKSKNGIHLCLKKLR
|
A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of saturated carbon hydrogen bonds of fatty acids. May act as a major omega- and ommega-1 hydroxylase for dodecanoic (lauric) acid in kidney. Catalyzes with low efficiency the epoxidation of 11,12-double bond of arachidonic acid.
|
O35730
|
RING1_MOUSE
|
E3 ubiquitin-protein ligase RING1 (EC 2.3.2.27) (Polycomb complex protein RING1) (RING finger protein 1) (RING-type E3 ubiquitin transferase RING1) (Transcription repressor Ring1A)
|
MTTPANAQNASKTWELSLYELHRTPQEAIMDGTEIAVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSREEYEAHQDRVLIRLSRLHNQQALSSSIEEGLRMQAMHRAQRVRRPMPGSDQTATMSGGEGEPGEGEGDGEDVSSDSAPDSAPGPAPKRPRGAGAGASSVGTGGGAAGGACGGAGSEDSGDRGGTLGGGTLGPPSPPGAPSPPEPGGEIELVFRPHPLLVEKGEYCQTRYVKTTGNATVDHLSKYLALRIALERRQQQETTEPGGPGGGASDTGGPDGGGGERGVAGGGEGPEEPALPSLEGVSEKQYTIYIAPGGGAFTTLNGSLTLELVNEKFWKVSRPLELCYAPTKDPK
|
Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:16710298, ECO:0000269|PubMed:9312051}.
|
O35732
|
CFLAR_MOUSE
|
CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
|
MAQSPVSAEVIHQVEECLDEDEKEMMLFLCRDVTENLAAPNVRDLLDSLSERGQLSFATLAELLYRVRRFDLLKRILKTDKATVEDHLRRNPHLVSDYRVLLMEIGESLDQNDVSSLVFLTRDYTGRGKIAKDKSFLDLVIELEKLNLIASDQLNLLEKCLKNIHRIDLNTKIQKYTQSSQGARSNMNTLQASLPKLSIKYNSRLQNGRSKEPRFVEYRDSQRTLVKTSIQESGAFLPPHIREETYRMQSKPLGICLIIDCIGNDTKYLQETFTSLGYHIQLFLFPKSHDITQIVRRYASMAQHQDYDSFACVLVSLGGSQSMMGRDQVHSGFSLDHVKNMFTGDTCPSLRGKPKLFFIQNYESLGSQLEDSSLEVDGPSIKNVDSKPLQPRHCTTHPEADIFWSLCTADVSHLEKPSSSSSVYLQKLSQQLKQGRRRPLVDLHVELMDKVYAWNSGVSSKEKYSLSLQHTLRKKLILAPT
|
Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:10602037, ECO:0000269|PubMed:10894163}.
|
O35734
|
TNFA_MARMO
|
Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
|
MSTESMIRDVELAEEALPKEAWGPQGSSRCLCLSLFSFLLVAGATTLFCLLHFGVIGPQREEFLNNLPLSPQAQMLTLRSSSQNMNDKPVAHVVAKNEDKEQLVWLSRRANALLANGMELIDNQLVVPANGLYLVYSQVLFKGQGCPSYVLLTHTVSRFAVSYQDKVNLLSAIKSPCPKESLEGAEFKPWYEPIYLGGVFELQKGDRLSAEVNLPSYLDFAESGQVYFGVIAL
|
Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity).
|
O35738
|
KLF12_MOUSE
|
Krueppel-like factor 12 (Transcriptional repressor AP-2rep)
|
MNIHMKRKTIKNLSALENRMLMLDGMPAVRVKTELVESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLPVDHFQTQTEPVDLSINKARTSPTAASSSPVSMTASASSPSSTSTSSSSSSRPASSPTVITSVSSASSSSTVLSPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRIPVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKAQMEPRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQKFACSISPFSIESTRRQRRSESPDSRKRRIHRCDFEGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHYRKHTGVKPFKCADCDRSFSRSDHLALHRRRHMLV
|
Confers strong transcriptional repression to the AP-2-alpha gene. Binds to a regulatory element (A32) in the AP-2-alpha gene promoter.
|
O35739
|
KLF9_MOUSE
|
Krueppel-like factor 9 (Basic transcription element-binding protein 1) (BTE-binding protein 1) (GC-box-binding protein 1) (Transcription factor BTEB1)
|
MSAAAYMDFVAAQCLVSISNRAAVPEHGGAPEAERLRLPEREVTKEHGDPGDTWKDYCTLVTIAKSLLDLNKYRPIQTPSVCSDSLESPDEDIGSDSDVTTESGSSPSHSPEERQDSGSAPSPLSLLHSGVASKGKHASEKRHKCPYSGCGKVYGKSSHLKAHYRVHTGERPFPCTWPDCLKKFSRSDELTRHYRTHTGEKQFRCPLCEKRFMRSDHLTKHARRHTVFHPSMIKRSKKALACPL
|
Transcription factor that binds to GC box promoter elements. Selectively activates mRNA synthesis from genes containing tandem repeats of GC boxes but represses genes with a single GC box. Acts as an epidermal circadian transcription factor regulating keratinocyte proliferation.
|
O35740
|
CITE2_MOUSE
|
Cbp/p300-interacting transactivator 2 (MSG-related protein 1) (MRG-1) (P35srj)
|
MADHMMAMNHGRFPDGTNGLHHHPAHRMGMGQFPSPHHHQQQQPQHAFNALMGEHIHYGAGNMNATSGIRHAMGPGTVNGGHPPSALAPAARFNNSQFMGPPVASQGGSLPASMQLQKLNNQYFNHHPYPHNHYMPDLHPTAGHQMNGTNQHFRDCNPKHSGGSSTPGGAGGSGTPGGSGGTSGGAGGSSAGGSGGGSTMPASVAHVPAAMLPPNVIDTDFIDEEVLMSLVIEMGLDRIKELPELWLGQNEFDFMTDFVCKQQPSRVSC
|
Transcriptional coactivator of the p300/CBP-mediated transcription complex. Acts as a bridge, linking TFAP2 transcription factors and the p300/CBP transcriptional coactivator complex in order to stimulate TFAP2-mediated transcriptional activation. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Stimulates the peroxisome proliferator-activated receptors PPARA transcriptional activity. Enhances estrogen-dependent transactivation mediated by estrogen receptors. Acts also as a transcriptional corepressor interferes with the binding of the transcription factors HIF1A or STAT2 and the p300/CBP transcriptional coactivator complex. Participates in sex determination and early gonad development by stimulating transcription activation of SRY. Plays a role in controlling left-right patterning during embryogenesis potentiates transcriptional activation of NODAL-mediated gene transcription in the left lateral plate mesoderm (LPM). Plays an essential role in differentiation of the adrenal cortex from the adrenogonadal primordium (AGP) stimulates WT1-mediated transcription activation thereby up-regulating the nuclear hormone receptor NR5A1 promoter activity. Associates with chromatin to the PITX2 P1 promoter region.
|
O35744
|
CHIL3_MOUSE
|
Chitinase-like protein 3 (EC 3.2.1.52) (Beta-N-acetylhexosaminidase Ym1) (Chitinase-3-like protein 3) (ECF-L) (Eosinophil chemotactic cytokine) (Secreted protein Ym1)
|
MAKLILVTGLAILLNVQLGSSYQLMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQNNEITYTHEQDLRDYEALNGLKDKNTELKTLLAIGGWKFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVKEMRKAFEEESVEKDIPRLLLTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSADLNVDSIISYWKDHGAASEKLIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDAPQEVPYAYQGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDDFSGSFCHQRHFPLTSTLKGDLNIHSASCKGPY
|
Lectin that binds saccharides with a free amino group, such as glucosamine or galactosamine. Binding to oligomeric saccharides is much stronger than binding to mono- or disaccharides. Also binds chitin and heparin. Has weak hexosaminidase activity but no chitinase activity. Has chemotactic activity for T-lymphocytes, bone marrow cells and eosinophils. May play a role in inflammation and allergy.
|
O35750
|
SHOX2_RAT
|
Short stature homeobox protein 2 (Paired family homeodomain protein Prx3)
|
RELDMGAAERSREPGSPRLTEVSPELKDRKEDAKGMEDEGQTKIKQRRSRTNFTLEQLNELERLFDETHYPDAFMREELSQRLGLSEARVQVWFQNRRAKCRKQENQLHKGVLIGAASQFEACRVAPYVNVGALRMPFQQDSHCNVTPLSFQVQAHVQLDSAVRAAHHHLHPHLAAHGPYMMFPAPPFGLPLATLAADSASAASVVAAAAAAKTTSKNSSIADLRLKAKKHAAALGL
|
May be a growth regulator and have a role in specifying neural systems involved in processing somatosensory information, as well as in face and body structure formation.
|
O35757
|
VEGFC_RAT
|
Vascular endothelial growth factor C (VEGF-C) (Flt4 ligand) (Flt4-L) (Vascular endothelial growth factor-related protein) (VRP)
|
MHLLCFLSLACSLLAAALIPGPREAPATVAAFESGLGFSEAEPDGGEVKGFEGKDLEEQLRSVSSVDELMSVLYPDYWKMYKCQLRKGGWQQPSLNMRTGDTVKLAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGAATNTFFKPPCVSVYRCGGCCNSEGLQCMNTSTGYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRRSLPATLPQCQAANKTCPANYVWNNYMCQCLAQQDFIFYSNVEDDSSNGFHDVCGPNKELDEDTCQCVCKGGLRPSSCGPHKELDRDSCQCVCKNKLFLNSCGANREFDENTCQCVCKRTCPRNQPLNPGKCACECTENTQKCFLKGKKFHHQTCSCYRRPCTNRLKHCDPGLSFSEEVCRCVPSYWKRPHLN
|
Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates KDR/VEGFR2 and FLT4/VEGFR3 receptors.
|
O35762
|
NKX61_RAT
|
Homeobox protein Nkx-6.1 (Homeobox protein NK-6 homolog A)
|
MLAVGAMEGPRQSAFLLSSPPLAALHSMAEMKTPLYPAAYPPLPTGPPSSSSSSSSSSSPSPPLGAHNPGGLKPPAAGGLSSLGSPPQQLSAATPHGINDILSRPSMPVASGAALPSASPSGSSSSSSSSASATSASAAAAAAAAAAAAAASSPAGLLAGLPRFSSLSPPPPPPGLYFSPSAAAVAAVGRYPKPLAELPGRTPIFWPGVMQSPPWRDARLACTPHQGSILLDKDGKRKHTRPTFSGQQIFALEKTFEQTKYLAGPERARLAYSLGMTESQVKVWFQNRRTKWRKKHAAEMATAKKKQDSETERLKGTSENEEDDDDYNKPLDPNSDDEKITQLLKKHKSSGGSLLLHASEAEGSS
|
Transcription factor which binds to specific A/T-rich DNA sequences in the promoter regions of a number of genes. Involved in the development of insulin-producing beta cells in the islets of Langerhans at the secondary transition (By similarity). Together with NKX2-2 and IRX3 acts to restrict the generation of motor neurons to the appropriate region of the neural tube. Belongs to the class II proteins of neuronal progenitor factors, which are induced by SHH signals (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q99MA9}.
|
O35763
|
MOES_RAT
|
Moesin (Membrane-organizing extension spike protein)
|
MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKAFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERALLENEKKKRELAEKEKEKIEREKEELMEKLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLASEMAELTARVSQLEMARKKKESEAEECHQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEHDEQDENGAEASAELRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTTNDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM
|
Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton. Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement. These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction. The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (By similarity). Modulates phagolysosomal biogenesis in macrophages (By similarity). Participates also in immunologic synapse formation (By similarity).
|
O35764
|
NPTXR_RAT
|
Neuronal pentraxin receptor
|
MKFLAVLLAAGMLAFLGAVICIIASVPLAASPARALPGGTDNASAASAAGAPGPQRSLSALQGAGGSAGPSVLPGEPAASVFPPPPGPLLSRFLCTPLAAACPSGAEQGDAAGERAELLLLQSTAEQLRQTALQQEARIRADRDTIRELTGKLGRCESGLPRGLQDAGPRRDTMADGAWDSPALLVELENAVRALRDRIERIEQELPARGNLSSSAPAPAVPTALHSKMDELEGQLLAKVLALEKERAALSHGSHQQRQEVEKELDALQGRVAELEHGSSAYSPPDAFKVSIPIRNNYMYARVRKAVPELYAFTACMWLRSRSGGSGQGTPFSYSVPGQANEIVLLEAGLEPMELLINDKVAQLPLSLKDSNWHHICIAWTTRDGLWSAYQDGELRGSGENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWDHALTPAQVLGIANCTGPLMGNVLPWEDKLVEAFGGAKKAAFDVCKRRAKA
|
May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses.
|
O35767
|
NKX25_RAT
|
Homeobox protein Nkx-2.5 (rNKx-2.5) (Homeobox protein NK-2 homolog E)
|
MFPSPALTHTPFSVKDILNLEQQQRSLAAGDLSARLEATLAPASCMLAAFKPDGYSGPEAAAPGLAELRAELGPAPSPPKCSPAFPTAPTFYPRAYGDPDPAKDPRADKKELCALQKAVELDKAETDGAERRRPRRRRKPRVLFSQAQVYELERRFKQQRYLSPAERDQLASVLKLTSTQVKIWFQNRRYKCKRQRQDQTLELLGPPPPPARRIAVPVLVRDGKPCLGDSAAYAPAYGLGLNAYGYNAYPYPGYGGAACSPAYSCAAYPAAPPAAHAPAASANSNFVNFGVGDLNTVQSPGMPQGNSGVSTLHGIRAW
|
Transcription factor required for the development of the heart and the spleen (By similarity). During heart development, acts as a transcriptional activator of NPPA/ANF in cooperation with GATA4 (By similarity). May cooperate with TBX2 to negatively modulate expression of NPPA/ANF in the atrioventricular canal (By similarity). Binds to the core DNA motif of NPPA promoter. Together with PBX1, required for spleen development through a mechanism that involves CDKN2B repression (By similarity). Positively regulates transcription of genes such as COL3A1 and MMP2, resulting in increased pulmonary endothelial fibrosis in response to hypoxia (By similarity).
|
O35776
|
HYAS2_RAT
|
Hyaluronan synthase 2 (EC 2.4.1.212) (Hyaluronate synthase 2) (Hyaluronic acid synthase 2) (HA synthase 2)
|
MHCERFLCVLRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQSLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVIDGNSDDDLYMMDIFSEVMGRDKSVTYIWKNNFHERGPGETEESHKESSQHVTQLVLSNKSICIMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYNQEFMGNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFREWLYNAMWFHKHHLWMTYEAVITGFFPFFLIATVIQLFYRGKIWNILLFLLTVQLVGLIKSSFASCLRGNIVMVFMSLYSVLYMSSLLPAKMFAIATINKAGWGTSGRKTIVVNFIGLIPVSVWFTILLGGVIFTIYKESKKPFSESKQTVLIVGTLIYACYWVVLLTLYVVLINKCGRRKKGQQYDMVLDV
|
Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation (By similarity). This is one of three isoenzymes responsible for cellular hyaluronan synthesis and it is particularly responsible for the synthesis of high molecular mass hyaluronan (By similarity).
|
O35779
|
BHE41_RAT
|
Class E basic helix-loop-helix protein 41 (bHLHe41) (Class B basic helix-loop-helix protein 3) (bHLHb3) (Enhancer-of-split and hairy-related protein 1) (SHARP-1)
|
MDEGIPHLQERQLLEHRDFIGLDYSSLYMCKPKRSLKRDDTKDTYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHLKALTALTEQQHQKIIALQNGERSLKSPVQADLDAFHSGFQTCAKEVLQYLARFESWTPREPRCAQLVSHLHAVATQLLTPQVTPGRGPGRAPCSAGAAAASGSERVARCVPVIQRTQPGTEPEHDTDTDSGYGGEAEQGRAAVKQEPPGDPSAAPKRLKLEARGALLGPEPALLGSLVALGGGAPFAQPAAAPFCLPFYLLSPSAAAYVQPWLDKSGLDKYLYPAAAAPFPLLYPGIPAAAAAAAAAAFPCLSSVLSPPPEKAGSAAGAPFLAHEVAPPGSLRPQHAHSRTHLPHAVNPESSQEDATQPAKDAP
|
Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA/B/G, NR1H3/LXRA, NR1H4 and VDR transactivation activity (By similarity). Inhibits HNF1A-mediated transactivation of CYP1A2, CYP2E1 and CYP3A11 (By similarity).
|
O35780
|
BHE40_RAT
|
Class E basic helix-loop-helix protein 40 (bHLHe40) (Class B basic helix-loop-helix protein 2) (bHLHb2) (Enhancer-of-split and hairy-related protein 2) (SHARP-2)
|
MERIPSAQPPPTCLPKTPGLEHGDLSGMDFAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIMALQSGLQAGDLSGKNIEAGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGSASRKPLDSAPKPVDFKEKPSFLAKGSEGPGKNCVPVIQRTFAPSGGEQSGSDTDTDSGYGGELEKGDLRSEQPYFKSDHGRRFTVGERVSTIKQESEEPPTKKSRMQLSDEEGHFVGSDLMGSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPLLYPGLNTSAAALSSFMNPDKIPTPLLLPQRLPSPLAHSSLDSSALLQALKQIPPLNLETKD
|
Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1/2 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-BMAL1|BMAL2 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA and NR1H3/LXRA transactivation activity. May be involved in the regulation of chondrocyte differentiation via the cAMP pathway (By similarity). Represses the transcription of NR0B2 and attentuates the transactivation of NR0B2 by the CLOCK-BMAL1 complex (By similarity). Drives the circadian rhythm of blood pressure through transcriptional repression of ATP1B1 in the cardiovascular system (By similarity).
|
O35783
|
CALU_RAT
|
Calumenin (CBP-50) (Crocalbin)
|
MDLRQFLMCLSLCTAFALSKPTEKKDRVHHEPQLSDKVHNDAQNFDYDHDAFLGAEEAKSFGQLTPEESKEKLGMIVDKIDTDKDGFVTEGELKSRIKHAQKKYIYDNVENQWQEFDMNQDGLISWDEYRNVTYGTYLDDPDPDDGFNYKPIMVRDERRFKMADQDGDLIATKEEFTAFLHPEEYDYMKDIVLQETMEDIDQNADGFIDLEEYIGDMYSHDGNADEPQWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQDKDGKLTKEEIVDKYDLFVGSQATDFGEALVRHDEF
|
Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low affinity (By similarity). {ECO:0000250, ECO:0000269|PubMed:15075329}.
|
O35786
|
CML1_RAT
|
Chemerin-like receptor 1 (Chemokine-like receptor 1) (G-protein coupled chemoattractant-like receptor) (G-protein coupled receptor DEZ)
|
MEYEGYNDSSIYGEEYSDGSDYIVDLEEAGPLEAKVAEVFLVVIYSLVCFLGILGNGLVIVIATFKMKKTVNTVWFVNLAVADFLFNIFLPIHITYAAMDYHWVFGKAMCKISSFLLSHNMYTSVFLLTVISFDRCISVLLPVWSQNHRSVRLAYMTCVVVWVLAFFLSSPSLVFRDTVSTSHGKITCFNNFSLAAPEPFSHSTHPRTDPVGYSRHVAVTVTRFLCGFLIPVFIITACYLTIVFKLQRNRLAKTKKPFKIIITIIITFFLCWCPYHTLYLLELHHTAVPASVFSLGLPLATAVAIANSCMNPILYVFMGHDFKKFKVALFSRLVNALSEDTGPSSYPSHRSFTKMSSLIEKASVNEKETSTL
|
Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 initiates activation of G proteins G(i)/G(o) and beta-arrestin pathways inducing cellular responses via second messenger pathways such as intracellular calcium mobilization, phosphorylation of MAP kinases MAPK1/MAPK3 (ERK1/2), TYRO3, MAPK14/P38MAPK and PI3K leading to multifunctional effects, like, reduction of immune responses, enhancing of adipogenesis and angionesis. Resolvin E1 down-regulates cytokine production in macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-kappa-B. Positively regulates adipogenesis and adipocyte metabolism (By similarity).
|
O35787
|
KIF1C_RAT
|
Kinesin-like protein KIF1C (Kinesin-like protein KIF1D)
|
MAGASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSRMFLKASFDYSYWSHTSVEDPQFASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEPGQQGIVPQLCEDLFSRVNVNQSAQLSYSVEVSYMEIYCERVRDLLNPKSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQLTGLDSEKVSKISLVNLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLQSKKRKSDFIPYRDSVLTWLLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAVINEDPNARLIRELQEEVARLRELLMAQGLSASALGGLKVEEGSPGGVLPAASSPPAPASPSSPPPHNGELEPSFSPSAEPQIGPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGSPGGWRTVGVFSPKKTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLTGQFIREQHCLFRSIPQPDGEVMVTLEPCEGAETYVNGKLVTEPLVLKSGNRIVMGKNHVFRFNHPEQARLERERGVPPPPGPPSEPVDWNFAQKDWLEQQGIDIKLEMEKRLQDLENQYRKEKEEADLLLEQQRLYADSDSGEDSDKRSCEESWRLISSLRDELPPNTVQTIVKRCGLPSSGKRRAPRRVYQIPQRRRLQGKDPRWATMADLKMQAVKEICYEVALADFRHGRAEIEALAALKMRELCRTYGKPEGPGDAWRAVARDVWDTVGEEEGCGGGGGGGEEGARGAEVEDLRAHIDKLTGILQEVKLQNSSKDRELQALRDRMLRMERVIPLTQDLEDDNEESGLVTWAPPEGSEAVEEAVSNDHSPAVRPSSPPQSSWERVSRLMEEDPAFRRGRLRWLKQEQLRLQGLQGSGGRGGGLRRPPARFVPPHDCKLRFPFKSNPQHRESWPGMGSGEAPGPQPPEEVTAPPPPPNRRPPSPRRPHRPRRNSLDGGSRSRGGGSTQPEPQHLRPQKHNSYPQQPQPYPAQRPGPRYPPYTTPPRMRRQRSAPDLKESGAAV
|
Probable motor protein.
|
O35789
|
B3GA1_RAT
|
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase 1) (Glucuronosyltransferase P) (GlcAT-P) (UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase) (GlcUAT-P)
|
MPKRRDILAIVLIVLPWTLLITVWHQSSLAPLLAVHKDEGSDPRHEAPPGADPREYCMSDRDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVVEDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRETFPRNSTQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVGWKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPKAANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI
|
Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group.
|
O35793
|
GREM1_RAT
|
Gremlin-1 (Cysteine knot superfamily 1, BMP antagonist 1) (Down-regulated in Mos-transformed cells protein)
|
MNRTAYTVGALLLLLGTLLPAAEGKKKGSQGAIPPPDKAQHNDSEQTQSPPQPGSRTRGRGQGRGTAMPGEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVKQCRCISIDLD
|
Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as a BMP antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop. Down-regulates the BMP4 signaling in a dose-dependent manner (By similarity). Antagonist of BMP2 inhibits BMP2-mediated differentiation of osteoblasts (in vitro) (By similarity). Acts as inhibitor of monocyte chemotaxis. Can inhibit the growth or viability of normal cells but not transformed cells when is overexpressed.
|
O35795
|
ENTP2_RAT
|
Ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase 2) (EC 3.6.1.-) (CD39 antigen-like 1) (Ecto-ATP diphosphohydrolase 2) (Ecto-ATPDase 2) (Ecto-ATPase 2)
|
MAGKLVSLVPPLLLAAAGLTGLLLLCVPTQDVREPPALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVGQHSSCDVQGGGISSYANDPSKAGQSLVRCLEQALRDVPRDRHASTPLYLGATAGMRPFNLTSPEATARVLEAVTQTLTQYPFDFRGARILSGQDEGVFGWVTANYLLENFIKYGWVGRWIRPRKGTLGAMDLGGASTQITFETTSPSEDPGNEVHLRLYGQHYRVYTHSFLCYGRDQILLRLLASALQIHRFHPCWPKGYSTQVLLQEVYQSPCTMGQRPRAFNGSAIVSLSGTSNATLCRDLVSRLFNISSCPFSQCSFNGVFQPPVAGNFIAFSAFYYTVDFLTTVMGLPVGTLKQLEEATEITCNQTWTELQARVPGQKTRLADYCAVAMFIHQLLSRGYHFDERSFREVVFQKKAADTAVGWALGYMLNLTNLIPADLPGLRKGTHFSSWVALLLLFTVLILAALVLLLRQVRSAKSPGAL
|
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent.
|
O35796
|
C1QBP_RAT
|
Complement component 1 Q subcomponent-binding protein, mitochondrial (GC1q-R protein) (Glycoprotein gC1qBP) (C1qBP)
|
MLPLLRCVPRALGAAATGLRASIPAPPLRHLLQPAPRPCLRPFGLLSVRAGSARRSGLLQPPVPCACGCGALHTEGDKAFVEFLTDEIKEEKKIQKHKSLPKMSGDWELEVNGTEAKLLRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKAEEQEPELTSTPNFVVEVTKTDGKKTLVLDCHYPEDEIGHEDEAESDIFSIKEVSFQTTGDSEWRDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ
|
Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q specifically binds to the globular 'heads' of C1q thus inhibiting C1 may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense.
|
O35799
|
HFE_RAT
|
Hereditary hemochromatosis protein homolog (RT1-CAFE)
|
MDRSAGLPVRLLLLLLLLLLWSVAPQALRPGSHSLRYLFMGASKPDLGLPFFEALGYVDDQLFVSYNHESRRAEPRAPWILGQTSSQLWLQLSQSLKGWDYMFIVDFWTIMGNYNHSKVTKLRVVPESHILQVILGCEVHEDNSTSGFWKYGYDGQDHLEFCPKTLNWSAAEPRAWATKMEWEEHRIRARQSRDYLQRDCPQQLKQVLELQRGVLGQQVPTLVKVTRHWASTGTSLRCQALNFFPQNITMRWLKDSQPLDAKDVNPENVLPNGDGTYQGWLTLAVAPGEETRFSCQVEHPGLDQPLTATWEPSRSQDMIIGIISGITICAIFFVGILILVLRKRKVSGGTMGDYVLTECE
|
Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin.
|
O35800
|
HIF1A_RAT
|
Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha)
|
MEGAGGENEKKKMSSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDEMKAQMNCFYLKAPDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGPVRKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTSSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKDSQPQCIVCVNYVVSGIIQHDLIFSLQQTESVLKPVESSDMKMTQLFTKVESEDTSCLFDKLKKEPDALTLLAPAAGDTIISLDFGSDDTETEDQQLEDVPLYNDVMFPSSNEKLNINLAMSPLPASETPKPLRSSADPALNQEVALKLESSPESLGLSFTMPQIQDQPASPSDGSTRQSSPEPNSPSEYCFDVDSDMVNVFKLELVEKLFAEDTEAKNPFSAQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESNSPSPPSVSTVTGFQQTQLQKPTITVTAATATTATTTDESKAVTKDNIEDIKILIASPPSTQVPQEMTTAKASAYSGTHSRTASPDRAGKRVIEKTDKAHPRSLNLSVTLNQRNTVPEEELNPRTIALQNAQRKRKMEHDGSLFQAAGIGTLLQQPGDRAPTMSLSWKRVKGYISSEQDGMEQKTIFLIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN
|
Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease (By similarity). Heterodimerizes with ARNT heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with NCOA1 and/or NCOA2. Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (By similarity).
|
O35811
|
P2RY4_RAT
|
P2Y purinoceptor 4 (P2Y4)
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MTSAESLLFTSLGPSPSSGDGDCRFNEEFKFILLPMSYAVVFVLGLALNAPTLWLFLFRLRPWDATATYMFHLALSDTLYVLSLPTLVYYYAARNHWPFGTGLCKFVRFLFYWNLYCSVLFLTCISVHRYLGICHPLRAIRWGRPRFASLLCLGVWLVVAGCLVPNLFFVTTNANGTTILCHDTTLPEEFDHYVYFSSAVMVLLFGLPFLITLVCYGLMARRLYRPLPGAGQSSSRLRSLRTIAVVLTVFAVCFVPFHITRTIYYQARLLQADCHVLNIVNVVYKVTRPLASANSCLDPVLYLFTGDKYRNQLQQLCRGSKPKPRTAASSLALVTLHEESISRWADTHQDSTFSAYEGDRL
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Receptor for ATP and UTP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. Not activated by ADP or UDP.
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O35814
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STIP1_RAT
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Stress-induced-phosphoprotein 1 (STI1) (Hsc70/Hsp90-organizing protein) (Hop)
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MEQVNELKEKGNKALSAGNIDDALQCYSEAIKLDPQNHVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANNLQLKEGLQNMEARLAERKFMNPFNLPNLYQKLENDPRTRTLLSDPTYRELIEQLQNKPSDLGTKLQDPRVMTTLSVLLGVDLGSMDEEEEAATPPPPPPPKKEAKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDKALKHYDKAKELDPTNMTYITNQAAVHFEKGDYNKCRELCEKAIEVGRENREDYRQIAKAYARIGNSYFKEERYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQERLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPRDAKLYSNRAACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDVYQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMSDPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR
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Acts as a co-chaperone for HSP90AA1 (By similarity). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90.
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O35815
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ATX3_RAT
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Ataxin-3 (EC 3.4.19.12) (Machado-Joseph disease protein 1 homolog)
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MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERLRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIKVQQMHRPKLIGEELAHLKEQSALKADLERVLEAADGPGMFDDDEDDLQRALAMSRQEIDMEDEEADLRRAIQLSMQGSSRGMCEDSPQTSSTDLSSEELRKRREAYFEKQQHQQQEADRPGYLSYPCERPTTSSGGLRSNQAGNAMSEEDVLRATVTVSLETAKDSLKAERKK
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Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates. Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (By similarity). Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (By similarity). Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription (By similarity). Regulates autophagy via the deubiquitination of 'Lys-402' of BECN1 leading to the stabilization of BECN1 (By similarity).
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O35819
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KLF6_RAT
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Krueppel-like factor 6 (Core promoter element-binding protein) (Transcription factor Zf9)
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MDVLPMCSIFQELQIVHETGYFSALPSLEEYWQQTCLELERYLQSEPCYVSASEIKFDNQEDLWTKIILARERKEESELKISSSPPEDSLISSGFNYNLETNSLNSDVSSESSDSSEELSPTTKFTSDPIGEVLVNSGNLSSSVISTPPSSPEVNRESSQLWGCGPGDLPSPGKVRSGTSGKSGDKGSGDASPDGRRRVHRCHFNGCRKVYTKSSHLKAHQRTHTGEKPYRCSWEGCEWRFARSDELTRHFRKHTGAKPFKCSHCDRCFSRSDHLALHMKRHL
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Transcriptional activator. Binds a GC box motif. Could play a role in B-cell growth and development (By similarity).
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O35820
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DNPH1_RAT
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2'-deoxynucleoside 5'-phosphate N-hydrolase 1 (EC 3.2.2.-) (Deoxyribonucleoside 5'-monophosphate N-glycosidase) (c-Myc-responsive protein Rcl)
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MAASGEQAPCSVYFCGSIRGGREDQALYARIVSRLRRYGKVLTEHVADAELEPLGEEAAGGDQFIHEQDLNWLQQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEGEVETMLDRYFEAYLPQKTASSSHPSA
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Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases. {ECO:0000255|HAMAP-Rule:MF_03036, ECO:0000269|PubMed:17234634, ECO:0000269|PubMed:19822152, ECO:0000269|PubMed:24260472, ECO:0000269|PubMed:25108359}.
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O35821
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MBB1A_RAT
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Myb-binding protein 1A (PAR-interacting protein) (PIP)
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MAEMKSPTKAEPASPAEAPQGDRRSLLEHSREFLDFFWDIAKPDQETRLRATEKLLEYLRTRPSDSEMKYALKRLITGLGVGREAARPCYSLALAQLLQSFEDIQLCDILGQIQEKYNLQAMNKAMMRPTLFANLFGVLALFQSGRLVKDKEALMKCVRLLKILSHHYNHLQGQPVKALVDILSEVPESMFQEILPKVLKGDMKVILSSPKYLELFLLARQRVPAELESLVGSVDLFSEDNIPSLVNILKVAANSVKKEQKLPDVALNLLRLALQENKFERFWKEVLEEGLLKKPSYTSSYMCFRLLGASLPLLSDEQLQLVMRGDLIRHFGEHMVVSKSQNPLRFIPEISAYVGTFLEGCQDDPKRQFTVMVAFTAITNQGLPVMPTFWRVTRFLNTEALQNYVTWLRDMFLQPDLDSLVDFSTANQKRVQVASLNVPERTVFRLRKWIIHRLVSLVDHLHLEKDEAVVEQIARFCLFHAFFKTKKATPQIPETKQHFSFPLEDGNRGVIVSAFFSLLQTLSVKFRQTPDLAENGKPWTYRLVQLADMLLKHNRNVANVTPLTAQQRQAWDQMMSTLKELEAQSSETRAIAFQHLLLLVGLHLFKSPAESCDVLGDIQTCIKKSMEQNLRRSRSRAKASQEPVWVEVMVEILLSLLAQPSNLMRQVVRSVFGHVCSHLTPRGLQLILAVLNPETNEDEEDNVVVTDTDEKQLKHGEDADSDSEDSKNSESDVDSEDGEESEEEDRDKDVDPGFRQQLMEVLQAGNALGGEEEEEEELGDEAMMALDQNLASLFAEQKMRIQARHEEKNKLQKEKQLRRDFQIRALDLIEVLVTKQPEHPLILELLEPLLNIIQRSMRSRGSTKQEQDLLHKTARIFMHHLCRARHYCHEVEPGAEALHAQVERLVQQAGNQADASVALYYFNASLYLLRVLKGNTTKRYQDGQKLEGADIKSEPKDSEVQTTSCLDLDFVTRVYSASLESLLTKRNSPLTIPMFLDLFSRYPVICKNLLPIVVQHVAGSSRPRHQAQACLLLQKALSARELRVCFEDPEWEQLISQVLGKTTQTLQTLGEAQSKGEHQRELSILELLNTVFRIVNHEKLSVDLTAFLGMLQGKQQKLQQNLQQGNHSSGSSRLYDLYWQAMNLLGVQRPKSEKKNVKDIPSDSQSPISTKRKKKGFLPETKKRKKLKSEGTTSEKKAASQQDAVTEGAMPAATGKDQPPSTGKKRRKRVKANTPSQVNGVTVAKSPAPNNPTLSPSTPPAKTPKVQKKKEKLSQVNGSTPVSPVEPESKKHQKALSTKEVKRRSSQSALPKKRARLSLVSRSPSLLQSGIRKRRVARRRVQTP
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May activate or repress transcription via interactions with sequence specific DNA-binding proteins (By similarity). Repression may be mediated at least in part by histone deacetylase activity (HDAC activity) (By similarity). Acts as a corepressor and in concert with CRY1, represses the transcription of the core circadian clock component PER2 (By similarity). Preferentially binds to dimethylated histone H3 'Lys-9' (H3K9me2) on the PER2 promoter (By similarity). Has a role in rRNA biogenesis together with PWP1 (By similarity).
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O35826
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GLCNE_RAT
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Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (UDP-GlcNAc-2-epimerase/ManAc kinase) [Includes: UDP-N-acetylglucosamine 2-epimerase (hydrolyzing) (EC 3.2.1.183) (UDP-GlcNAc-2-epimerase) (Uridine diphosphate-N-acetylglucosamine-2-epimerase); N-acetylmannosamine kinase (EC 2.7.1.60) (ManAc kinase)]
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MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPAFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKCKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVRDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRRIH
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Regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. Plays an essential role in early development (By similarity).
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O35831
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CDK17_RAT
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Cyclin-dependent kinase 17 (EC 2.7.11.22) (Cell division protein kinase 17) (PCTAIRE-motif protein kinase 2) (Serine/threonine-protein kinase PCTAIRE-2)
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MKKFKRRLSLTLRGSQTIDESLSELAEQMTIEESSSKDNEPIVKNGRPPTSHSMHSFLHQYTGSFKKPPLRRPHSVIGGSLGSFMAMPRNGSRLDIVHENLKMGSDGESDQASGTSSDEVQSPTGVCLRNRIHRRISMEDLNKRLSLPADIRIPDGYLEKLQISSPPFDQPMSRRSRRASLSEIGFGKMETYIKLEKLGEGTYATVYKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKDLKQYMDDCGSIMSMHNVKLFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPSQETWPGVSSNDEFKNYNFPKYKPQPLINHAPRLDSEGIELITKFLQYESKKRAPAEEAMKHVYFRSLGPRIHALPESVSIFSLKEIQLQKDPGFRNSSYPETGVFVINHFTCRS
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May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1.
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O35854
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BCAT2_RAT
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Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT(m)) (EC 2.6.1.42)
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MSAAILGQVWTRKLLPIPWRLCVPGRCVSSNFKAADLQVQVTREPQKKPAPSQPLLFGKTFTDHMLMVEWNSKTGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPGDSMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQQEAQKKGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGELELATPPLDGIILPGVVRQSLLDLARTWGEFRVAERKVTMKELKRALEEGRVREVFGSGTACQVCPVHQILYEGKQLHIPTMENGPELILRFQKELKAIQYGTSAHDWMLRV
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Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.
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O35855
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BCAT2_MOUSE
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Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT(m)) (EC 2.6.1.42)
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MAAATLGQVWARKLLPVPWLLCGSKRCVSSIFKAADLQIQMTKEPQKKPAPSQALLFGKTFTDHMLMVEWNNKAGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGGDQQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTSLYVRPVLIGNEPSLGVGMVTQALLYVILCPVGSYFPGDSMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQREAQKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDLARTWGEFRVAERKVTMKELKRALEEGRVREVFGSGTACQVCPVHQILYEGKQLHIPTMENGPELILRFQKELKAIQYGASAHDWMFRV
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Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine (By similarity). May also function as a transporter of branched chain alpha-keto acids (By similarity).
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O35864
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CSN5_MOUSE
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COP9 signalosome complex subunit 5 (SGN5) (Signalosome subunit 5) (EC 3.4.-.-) (Jun activation domain-binding protein 1) (Kip1 C-terminus-interacting protein 2)
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MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINVA
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Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Promotes the proteasomal degradation of BRSK2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex.
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O35867
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NEB1_RAT
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Neurabin-1 (Neurabin-I) (Neural tissue-specific F-actin-binding protein I) (PP1bp175) (Protein phosphatase 1 regulatory subunit 9A) (p180)
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MLKAESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKPDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPNENAAIIAKTRGKGRPSSPQKRMKPKEFVEKTDGSVVKLESSVSERISRFDTMHDGPSYAKFTETRKMFERSGHESGQNNRHSPKKEKAGEAEPQDEWGGSKSNRGSSDSLDSLSPRTEAVSPTVSQLSAVFENSESPGAITPGKAENSNYSVTGHYPLNLPSVTVTNLDTFGRLKDSNSRPSSNKQATDTEEPEKSEAVPVPEVAQKGTSLASLPSEERQLSTEAEDVTAQPDTPDSTDKDSPGEPSAESQAMPKSNTLSRPKEPLEDAEANVVGSEAEQPQRRDLTGGGDLTSPDASASSCGKEVPEDSNSFEGSHVYMHSDYNVYRVRSRYNSDWGETGTEQDEGDDSDENNYYQPDMEYSEIVGLPQEEEIPANRKIKFSCAPIKVFNTYSNEDYDRRNDDVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVGADAGLEKLGIFVKTVTEGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGNVRFVIGREKPGQVSEVAQLISQTLEQERRQRELLERHYAQYDADDDETGEYATDEEEDEVGPILPGGDMAIEVFELPENEDMFSPSDLDTSKLSHKFKELQIKHAVTEAEIQKLKTKLQAAENEKVRWELEKNQLQQNIEENKERMVKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIRRQEVERKKLEEVEKAHLVEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRPSPGEVSKGDTMENVEVKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPTRTRLYDSVSSTDGEDSLERKNFTFNDDFSPSSTSSADLSGLGAEPKTPGLSQSLALSSDESLDMIDDEILDDGQSPKHTQSQSRAVHEWSVQQVSHWLVGLSLDQYVSEFSAQNISGEQLLQLDGNKLKALGMTSSQDRALVKKKLKEMKMSLEKARKAQEKMEKQREKLRRKEQEQMQRKSKKSEKMTSTTEQP
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Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May be involved in neurite formation. Inhibits protein phosphatase 1-alpha activity. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction.
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O35874
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SATT_MOUSE
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Neutral amino acid transporter A (Alanine/serine/cysteine/threonine transporter 1) (ASCT-1) (Solute carrier family 1 member 4)
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MEKSGETNGYLDGTQAEPAAGPRTPETAMGKSQRCASFFRRHALVLLTVSGVLVGAGMGAALRGLQLTRTQITYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASSLGRLGGIAVAYFGLTTLSASALAVALAFIIKPGAGAQTLQSSSLGLENSGPPPVSKETVDSFLDLLRNLFPSNLVVAAFTTSATDYTVVTHNTSSGNVTKEKIPVVTDVEGMNILGLVLFALVLGVALKKLGPEGEDLIRFFNSFNEATMVLVSWIMWYVPIGIMFLIGSKIVEMKDIVMLVTSLGKYIFASMLGHVIHGGIVLPLVYFAFTRKNPFTFLLGLLTPFATAFATCSSSATLPSMMKCIEENNGVDKRISRFILPIGATVNMDGAAIFQCVAAVFIAQLNNVDLNAGQIFTILVTATASSVGAAGVPAGGVLTIAIILEAIGLPTHDLSLILAVDWIVDRTTTVVNVEGDALGAGILNHLNQKVVKKGEQELQEVKVEAIPNSKSEEETSPLVTHQNPAGPVAIAPELESKESVL
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Sodium-dependent neutral amino-acid transporter that mediates transport of alanine, serine, cysteine, proline, hydroxyproline and threonine.
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O35876
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SMN_RAT
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Survival motor neuron protein
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MAMGSGGGAGSEQEDTVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDMCETSDKPKGTARRKPAKKNKNQKKNATAPLKQWKAGDKCSAVWSEDGCVYPATITSVDLKRETCVVVYTGYGNKEEQNLSDLLSPTCEVANNTEQNTQENESQVSTDDSEHSSRSLRSKAHSKSKAAPWTSFLPPPPPVPGAGLGPGKPGLRFSGPPPPPPPPPPFLPCWMPPFPSGPPIIPPPPPISPDCLDDTDALGSMLISWYMSGYHTGYYMGFRQNKKEGKKCSHTN
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The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, SMN1 acts as a structural backbone and together with GEMIN2 it gathers the Sm complex subunits. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs).
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O35885
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ASCL2_MOUSE
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Achaete-scute homolog 2 (ASH-2) (mASH-2) (mASH2)
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MEAHLDWYGVPGLQEASDACPRESCSSALPEAREGANVHFPPHPVPREHFSCAAPELVAGAQGLNASLMDGGALPRLMPTSSGVAGACAARRRQASPELLRCSRRRRSGATEASSSSAAVARRNERERNRVKLVNLGFQALRQHVPHGGANKKLSKVETLRSAVEYIRALQRLLAEHDAVRAALAGGLLTPATPPSDECAQPSASPASASLSCASTSPSPDRLGCSEPTSPRSAYSSEESSCEGELSPMEQELLDFSSWLGGY
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Transcription factor. Binds to E-box motifs 5'-CANNTG-3' in the regulatory elements of target genes, probably as a heterodimer with another basic helix-loop-helix (bHLH) protein such as the transcription factor TCF3. May bind both open and closed chromatin, acting as a pioneer transcription factor to allow other factors to bind and activate lineage-specific genes. Required during post-implantation development for the generation of some differentiated trophoblast cell types. Transcriptional activity of ASCL2 may be antagonised in a subset of trophoblast cells by bHLH transcription factor HAND1, perhaps by competing for dimerization with other bHLH proteins. Involved in differentiation and function of follicular T-helper (Tfh) cells, thereby playing a role in germinal center responses probably modulates expression of genes involved in Tfh cell function, such as BCL6. May also act as a suppressor of Th1-, Th2- and Th17-cell differentiation. Induces the formation of stem cells in intestinal crypts in vitro, synergistically activating transcription of target genes, such as SOX9, together with TCF4/beta-catenin. May form a bistable transcriptional switch, controlling expression of its own gene together with Wnt/R-spondin signaling, and thereby maintaining stem cell characteristics. Modulates expression of target genes, including perhaps down-regulating EGR1/Krox24 and chemokine CXCL10/Mob-1 and up-regulating CXCR4 and CDKN1C/p57kip2, in Schwann cells (By similarity). May play a role in reducing proliferation of Schwann cells, perhaps acting via modulation of expression of CDKN1C (By similarity). May be dispensable for blastocyst formation and later embryonic function. May be involved in the determination of neuronal precursors (By similarity).
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O35889
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AFAD_RAT
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Afadin (Afadin adherens junction formation factor) (Protein Af-6)
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MSAGGRDEERRKLADIIHHWNANRLDLFEISQPTEDLEFHGVMRFYFQDKAAGNFATKCIRVSSTATTQDVIETLAEKFRPDMRMLSSPKYSLYEVHVSGERRLDIDEKPLVVQLNWNKDDREGRFVLKNENDAIPAKKAQSNGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKEERPSQGDDSENSRLAAEVYKDMPETSFTRTISNPEVVMKRRRQQKLEKRMQEFRSSDGRPDSGGTLRIYADSLKPNIPYKTILLSTTDPADFAVAESLEKYGLEKENPKDYCIARVMLPPGAQHSDERGAKEIILDDDECPLQIFREWPSDKGILVFQLKRRPPDYIPKKMKKHVEGKPLKGKDRADGSGYGSALPPEKLPYLVELSPGRRNHFAYYSYHTYEDGSDSRDKPKLYRLQLSVTEVGTEKFDDNSIQLFGPGIQPHHCDLTNMDGVVTVTPRSMDAETYVDGQRISETTMLQSGMRLQFGTSHVFKFVDPIQDHVLSKRSVDGGLMVKGPRHKPGAVQETTFELGGDIHSGTALPASRSTTRLDSDRVSSASSTAERGMVKPMIRLDQEQDYRRRESRTQDAAGPELMLPASIEFRESSEDSFLSAIINYTNSSTVHFKLSPTYVLYMACRYVLSSQHRPDISPTERTHKAIAVVNKMVSMMEGVIQEVDQVDQKQKNIAGALAFWMANASELLNFIKQDRDLSRITLDAQDVLAHLVQMAFKYLVHCLQSELNNYMPAFLDDPEENSLQRPKIDDVLHTLTGAMSLLRRCRVNAALTIQLFSQLFHFINMWLFNRLVTDPDSGLCSHYWGAIIRQQLGHIEAWAEKQGLELAADCHLSRIVQATTLLTMDKYVPDDIPNINSTCFKLNSLQLQALLQNYHCAPDEPFIPTDLIENVVAVAENTADELARSDGRDVQLEEDPDLQLPFLLPEDGYSCDVVRNIPNGLQEFLDPLCQRGFCRLVPHTRSPGTWTIYFEGADYESHLMRENTELTQPLRKEPEVITVTLKKQNGMGLSIVAAKGAGQDKLGIYVKSVVKGGAADVDGRLAAGDQLLSVDGRSLVGLSQERAAELMTRTSSVVTLEVAKQGAIYHGLATLLNQPSPMMQRISDRRGSGKPRPKSEGFELYNNSAQNGSPESPQMPWTEYSEPKKLPGDDRLMKNRADHRSSPNVANQPPSPGGKSPYTSGTAAKITSVSTGNLCTEEQTPPPRPEAYPIPTQTYTREYFTFPASKSQDRMAPVQNQWPNYEEKPHMHTESDHASIAIQRVTRSQEELREEKVYQLERHRVESGMDRKCDSDMWINQSSSVESSTSSQEHLNHSSKSVTPASTLTKSGPGRWKTPAAVLPTPVAVSQPIRTDLPPPPPPPPAHYTSDFDGISMDLPLPPPPANQAAPQSAQVAAAERKKREEHQRWYEKEKARLEEERERKRREQERKLGQMRTQSLNPASFSPLATQAKPEKPSTLQRPQETVIRELQPQQQPRTIERRDLQYITISKEELSSGDSLSPDPWKRDAREKLEKQQQMHIVDMLSKEIHELQNKGDRTAEESDRLRKLMLEWQFQKRLQESKQKDEDDDEEEDDDVDTMLIMQRLEAERRARLQDEERRRQQQLEEMRKREVEDRVRQEEDGRHQEEERVKRDAEEKRRQEEGYYSRLEAERRRQHEEAARRLLEPEEPGLSRPPLPQDYEPPSQSSAPSAPPPPPQRNASYLKTQVLSPDSLFTAKFVAYDDDDEEENYVPAGPNSYSGSAGTTAGTYDAPRDTREKLSRSQDADLPGSSGAPENLTFRERQRLFSQGQDVSDKVKASRKLTELENELNTK
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Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity). Essential for the organization of adherens junctions (By similarity).
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O35892
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SP100_MOUSE
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Nuclear autoantigen Sp-100 (Nuclear dot-associated Sp100 protein) (Speckled 100 kDa)
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MEGSDGSPRMSTEQENTEMHLIECMLKHFKTQKVAISNAIRSTFPFLESLRDHEFITGKMYEDLLDSCRSLVPVDKVIYRALEELEKKFDMTVLCELFNEVNMEKYPDLNLIRRSFGCVFPNELCFQGIDGGNPNSQLSLEQGPGASYSQGSPNGSSLDLSASEGWRSNDRRNSNLMQANQTENHQLAESPGHLDSCELQVQLNNRDATPESCSLLPQNEERAVQLNYELQINPCFVQLVDVKKENSSFSLAGNQQTRARTNQNEDSEIIELSSGDSDNGENFSEATTTVPSQPAPAYSRKPPTLRRDRGGDTSDTESSIIIRRRKRTGRKKRERLGSYLIRNIKIPMKPSWKTAFLARSANPSSQRRRKRGPRIPREENADFGGAELPVVCGNAQGFLDKEKFKQGIYVRSIRGKTGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVLQDPPRKKKETPRNPRQTRRQVNAL
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Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. May also play a role in infection by viruses through mechanisms that may involve chromatin and/or transcriptional regulation (By similarity).
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O35893
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SP100_MUSCR
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Nuclear autoantigen Sp-100 (Nuclear dot-associated Sp100 protein) (Speckled 100 kDa)
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MEDSNASPRMSTEHENTEMHPFEYMFKHFKTQKVAISNAIRSTFPFLESLRDREFITGKMYEDLIDSCRSLVPVDKVIYKALDELEKKFDVTVLWELFNEVNMEKYPDLNPIRRSFECVFPNELSFQGIDRGNPNSQLSLEQGPSASYSQGSLNGSSLDLSSSEGWRSNDRRNSNLMQANQTENHQLAESPGHLDSCELQVQLNNGDATPESYSLLPQHEERAVQLNNEFQINPCFVQLIDVKKENSSFSLAGNQQTRARTNQNEDSEVIELSSGDSDDGENFSEATTTIPSQPAPAYSRTPPTLRTDRRGDTSDTESSIIIRRRKRTGRKKRERLGSYLIRNIKIPMKTSWKTAVLARSANTSSQRRRKRGPRIPREENADFGGAELPAVCGNVQGFLNKEKFKQGIYVRSIRSETGRLFTPMDFEIEGNCEKAKNWRQTIRCKGWTLRELIQKGVLQDPPRKKKENPRNPRQMKRQVNAL
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Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. May also play a role in infection by viruses through mechanisms that may involve chromatin and/or transcriptional regulation (By similarity).
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O35899
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SC6A4_CAVPO
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Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4)
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METTALNSQKAPSVCKDREDCQENSILQKSGPTSAGGVESGQIFNGYSSVPSTGMGDDAEHSVPTATTTLVAEVHHGERETWGKKVDFLLSVIGYAVDLGNIWRFPYVCYQNGGGAFLLPYIIMAIFGGIPLFYMELALGQYHRNGCISIWRKICPIFKGIGYTICIIAFYIASYYNTIIAWALYYLISSFTDRLPWTSCRNSWNTANCTNYFSEDNITWTLHSTSPAEEFYIRHILQIHRSKGLQDVGGVSWQLTLCIMLIFTIIYFSIWKGVKTSGKVVWVTATFPYIVLSVLLVRGATLPGAWKGVLFYLKPNWQKLLETGVWIDAAAQIFFSLGPGFGVLLAFASYNKFNNNCYQDALVTSAVNCMTSFVSGFVIFTVLGYMAEMRSEDVSEVAKDAGPSLLFITYAEAIANMPASTFFAIIFFLMLITLGLDSTFAGLEGVITAVLDEFPHIWAKHREWFVLAVVITCFFGSLTTLTFGGAYVVKLLEEYATGPAVLTVVFIEAIAVSWFYGVTQFCSDVKEMLGFSPGWFWRICWVAVSPVFLLFIICSFLMSPPQLRLFQYSYPHWSVILGYCIGTSSVICIPTYITYRLVTTPGTLKERIIKSITPETPTEIPCGDICLNAV
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Serotonin transporter that cotransports serotonin with one Na(+) ion in exchange for one K(+) ion and possibly one proton in an overall electroneutral transport cycle. Transports serotonin across the plasma membrane from the extracellular compartment to the cytosol thus limiting serotonin intercellular signaling (By similarity). Essential for serotonin homeostasis in the central nervous system. In the developing somatosensory cortex, acts in glutamatergic neurons to control serotonin uptake and its trophic functions accounting for proper spatial organization of cortical neurons and elaboration of sensory circuits. In the mature cortex, acts primarily in brainstem raphe neurons to mediate serotonin uptake from the synaptic cleft back into the pre-synaptic terminal thus terminating serotonin signaling at the synapse (By similarity). Modulates mucosal serotonin levels in the gastrointestinal tract through uptake and clearance of serotonin in enterocytes. Required for enteric neurogenesis and gastrointestinal reflexes (By similarity). Regulates blood serotonin levels by ensuring rapid high affinity uptake of serotonin from plasma to platelets, where it is further stored in dense granules via vesicular monoamine transporters and then released upon stimulation. Mechanistically, the transport cycle starts with an outward-open conformation having Na1(+) and Cl(-) sites occupied. The binding of a second extracellular Na2(+) ion and serotonin substrate leads to structural changes to outward-occluded to inward-occluded to inward-open, where the Na2(+) ion and serotonin are released into the cytosol. Binding of intracellular K(+) ion induces conformational transitions to inward-occluded to outward-open and completes the cycle by releasing K(+) possibly together with a proton bound to Asp-98 into the extracellular compartment. Na1(+) and Cl(-) ions remain bound throughout the transport cycle (By similarity). Additionally, displays serotonin-induced channel-like conductance for monovalent cations, mainly Na(+) ions. The channel activity is uncoupled from the transport cycle and may contribute to the membrane resting potential or excitability (By similarity).
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O35902
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DSG3_MOUSE
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Desmoglein-3 (130 kDa pemphigus vulgaris antigen homolog)
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MTCLFPRALGSLALLMVVLLVQGELHVKPGGQHREDGTALQLAKRRYKREWVKFAKPCREREDNSRRNPIAKITSDFQKNQKITYRISGVGIDQPPFGIFVVDPNNGDINITAIVDREETPSFLITCRALNALGQDVERPLILTVKILDVNDNPPIFSQTIFKGEIEENSASNSLVMILNATDADEPNHMNSKIAFKIVSQEPAGMSMFLISRNTGEVRTLTSSLDREQISSYHLVVSGADNDGTGLSTQCECSIKIKDVNDNFPVLRESQYSARIEENTLNAELLRFQVTDWDEEYTDNWLAVYFFTSGNEGNWFEIETDPRTNEGILKVVKALDYEQVQSMQFSIAVRNKAEFHQSVISQYRVQSTPVTIQVIDVREGISFRPPSKTFTVQRGVSTNKLVGYILGTYQATDEDTGKAASSVRYVLGRNDGGLLVIDSKTAQIKFVKNIDRDSTFIVNKTISAEVLAIDENTGKTSTGTIYVEVPSFNENCPSVVLEKKDICTSSPSVTLSVRTLDRGKYTGPYTVSLEEQPLKLPVMWTITTLNATSALLQAQQQVSPGVYNVPVIVKDNQDGLCDTPESLTLTVCQCDDRSMCRAPIPSREPNTYGESSWRLGPAAIGLILLGLLMLLLAPLLLLTCDCGSGPIGGAATGGFIPVPDGSEGTIHQWGIEGAQPEDKEITNICVPPVTTNGADFMESSEVCTNTYAGGTMVEGASGMEMITKLGGATGATAALGPCSLGYSGTMRTRHSTGGTLKDYAAPVNMTFLGSYFSQKSLAYAEEEDEREVNDCLLIYDDEGEDAAPHSPTLSSCSIFGDDLDDNFLDSLGPKFKKLAEICLGIDDEAKQAKPGPKDSGSGADTCARSMEVPQSGSNRYQTLPGSLEVTQTGSKICHTLSGNQETSVMSTSGSVHPAVAIPDPLQLGNYLLTETYSTSGSFAQPTTVTFDPHVTQNVTVTERVICPLPSASSSIVAPTELRGSYNMLYTKETCSHL
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Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
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O35903
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CCL25_MOUSE
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C-C motif chemokine 25 (Chemokine TECK) (Small-inducible cytokine A25) (Thymus-expressed chemokine)
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MKLWLFACLVACFVGAWMPVVHAQGAFEDCCLGYQHRIKWNVLRHARNYHQQEVSGSCNLRAVRFYFRQKVVCGNPEDMNVKRAMRILTARKRLVHWKSASDSQTERKKSNHMKSKVENPNSTSVRSATLGHPRMVMMPRKTNN
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Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4.
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O35904
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PK3CD_MOUSE
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Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform (PI3-kinase subunit delta) (PI3K-delta) (PI3Kdelta) (PtdIns-3-kinase subunit delta) (EC 2.7.1.137) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta) (PtdIns-3-kinase subunit p110-delta) (p110delta)
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MPPGVDCPMEFWTKEESQSVVVDFLLPTGVYLNFPVSRNANLSTIKQVLWHRAQYEPLFHMLSDPEAYVFTCVNQTAEQQELEDEQRRLCDIQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLRDPEVNDFRTKMRQFCEEAAAHRQQLGWVEWLQYSFPLQLEPSARGWRAGLLRVSNRALLVNVKFEGSEESFTFQVSTKDMPLALMACALRKKATVFRQPLVEQPEEYALQVNGRHEYLYGNYPLCHFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFSIELIEGRKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVNVCSEPVWKQRLEFDISVCDLPRMARLCFALYAVVEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPAGTVRGNPNTESAAALVIYLPEVAPHPVYFPALEKILELGRHGERGRITEEELQLREILERRGSGELYEHEKDLVWKMRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCYVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLGRALANRKIGHFLFWHLRSEMHVPSVALRFGLIMEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKVSSQKTTKPQTKEMMHMCMRQETYMEALSHLQSPLDPSTLLEEVCVEQCTFMDSKMKPLWIMYSSEEAGSAGNVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLHSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ
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Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides. Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Plays a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Plays important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function.
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O35906
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SPIB_MOUSE
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Transcription factor Spi-B
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MLALEAAQLDGPHLSCLYPEGVFYDLDSCKPFSYPDSDGGLDSTWGWTEAPPAPAIAPYEAFDPATAAFSHSQTVQLCYSHGPNPSTYSPMGTLDPAPSLEAPGPGLQVYPPEDFTSQTLGSLAYAPYPSPVLSEEEDIMLDSPALEVSDSESDEALLAGSEGRGSEAGARKKLRLYQFLLGLLLRGDMRECVWWVEPGAGVFQFSSKHKELLARRWGQQKGNRKRMTYQKLARALRNYAKTGEIRKVKRKLTYQFDSALLPASRHV
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Sequence specific transcriptional activator which binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a lymphoid-specific enhancer. Promotes development of plasmacytoid dendritic cells (pDCs), also known as type 2 DC precursors (pre-DC2) or natural interferon (IFN)-producing cells. These cells have the capacity to produce large amounts of interferon and block viral replication. Required for B-cell receptor (BCR) signaling, which is necessary for normal B-cell development and antigenic stimulation.
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O35910
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MOT4_RAT
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Monocarboxylate transporter 4 (MCT 4) (Monocarboxylate transporter 3) (MCT 3) (Solute carrier family 16 member 3)
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MGGAVVDEGPTGIKAPDGGWGWAVLFGCFIITGFSYAFPKAVSVFFKELMHEFGIGYSDTAWISSILLAMLYGTGPLCSMCVNRFGCRPVMLVGGLFASLGMVAASFCRSIIQIYLTTGVITGLGLALNFQPSLIMLNRYFNKRRPMANGLAAAGSPVFLCALSPLGQLLQDHYGWRGGFLILGGLLLNCCVCAALMRPLVAPQASGGAEPHGPQRPSPRLLDLSVFRDRGFLIYAVAASIMVLGLFVPPVFVVSYAKDMGVPDTKAAFLLTILGFIDIFARPTAGFITGLKKVRPYSVYLFSFAMFFNGFTDLTGSTASDYGGLVVFCIFFGISYGMVGALQFEVLMAIVGTQKFSSAIGLVLLLEAVAVLIGPPSGGKLLDATKVYKYVFILAGAEVLTSSLVLLLGNFFCIGKRKRPEVTKPEEVASEEEKLHKPPVDVRVDSREVEHFLKAEPEKNGEVVHTPETSV
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Proton-dependent transporter of monocarboxylates such as L-lactate and pyruvate (By similarity). Plays a predominant role in the L-lactate efflux from highly glycolytic cells.
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O35913
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SO1A4_RAT
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Solute carrier organic anion transporter family member 1A4 (Brain digoxin carrier protein) (Brain-specific organic anion transporter) (OATP-B1) (Sodium-independent organic anion-transporting polypeptide 2) (Solute carrier family 21 member 5)
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MGKSEKRVATHGVRCFAKIKMFLLALTCAYVSKSLSGTYMNSMLTQIERQFGIPTSIVGLINGSFEIGNLLLIIFVSYFGTKLHRPIMIGVGCAVMGLGCFLISLPHFLMGQYEYETILPTSNVSSNSFFCVENRSQTLNPTQDPSECVKEMKSLMWIYVLVGNIIRGIGETPIMPLGISYIEDFAKSENSPLYIGILETGMTIGPLIGLLLASSCANIYVDIESVNTDDLTITPTDTRWVGAWWIGFLVCAGVNILTSFPFFFFPKTLPKEGLQENVDGTENAKEKKHRKKAKEEKRGITKDFFVFMKSLSCNPIYMLFILISVLQFNAFINSFTFMPKYLEQQYGKSTAEVVFLMGLYMLPPICLGYLIGGLIMKKFKVTVKKAAHLAFWLCLSEYLLSFLSYVMTCDNFPVAGLTTSYEGVQHQLYVENKVLADCNTRCNCSTNTWDPVCGDNGLAYMSACLAGCEKSVGTGTNMVFQNCSCIQSSGNSSAVLGLCNKGPDCANKLQYFLIIAIFGCFIYSLAGIPGYMVLLRCIKSEEKSLGVGLHAFCIRILAGIPAPIYFGALIDRTCLHWGTLKCGEPGACRMYDINSFRRLYLGLPAALRGASFVPAFFILRLTRTFQFPGDIESSKTDHAEMKLTLKESECTEVLRSKVTED
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Mediates the Na(+)-independent transport of organic anions such as taurocholate, cholate, 17-beta-glucuronosyl estradiol, prostaglandin E2, estrone 3-sulfate, L-thyroxine (T4), the cardiac glycosides ouabain and digoxin and thyroid hormones. May play an especially important role in the brain accumulation and toxicity of digoxin and in the hepatobiliary and renal excretion of cardiac glycosides. Shows a pH-sensitive substrate specificity which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment. Hydrogencarbonate/HCO3(-) acts as the probable counteranion that exchanges for organic anions.
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O35914
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BNC1_MOUSE
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Zinc finger protein basonuclin-1
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MAEAIGCTLNCSCQCFKPGKINHRQCEQCRHGWVAHALSKLRIPPVYPTSQVEIVQSNVVFDISSLMLYGTQAIPVRLKILLDRLFSVLKQDEVLQILHALDWTLQDYIRGYVLQDASGKVLDHWSIMTSEEEVATLQQFLRFGETKSIVELMAIQEKEEQSVIVPPTTANVDIRAFIESCGHRSASLPTPVDKGSPGGMHPFENLISNMTFMLPFQFFNPLPPALIGSLPEQYMLEQGQDQSQEPKQELHGPFSDSSFLTSTPFQVEKEQCLNCPETVPQKEDSAHLSDSSSYSIASKLERTQLSPEAKVKPERNSLSAKKGRVFCTACEKTFYDKGTLKIHYNAVHLKIKHKCTIEGCNMVFSSLRSRNRHSANPNPRLHMPMNRNNRDKDLRNSLNLASSETYKRPGFTVVSPDCGPLPGYTGSVEDSKGQPAFSSIGQNGVLFPNLKTVQPVLPFYRSPATPAELANTPGMLPSLPLLSSSIPEQLVSTDMPFDALPKKKSRKSSMPIKIEKEAVEIAEEKRHSLSSDDEVPLQVVSEDEPEDSSPRSDRVPEEQHTQLSLEEPLPQGERACHLESVIESHGALSRTLEQTTLTEREAEQKVALSSVMPREVEDGGHERHFTAGLVPQIPFPDYMELQQRLLAGGLFGALSNRGMAFPFLEESKELEHLGEHALVRQKEEARFQCDICKKTFKNACSMKTHEKNTHARETHACTVEGCGAAFPSRRSRDRHSSNLSLHQKVLNEEALETSEDHFRAAYLLQDVAKEAYQDVAFTPQASQTSVIFKGTSGMGSLVYPISQVHSASLESYNSGPPSEGTILDLSTTSSMKSESSSHSSWDSDGVSEEGTALMEDSDGNCEGQSLVSGEDEYPLCVLMEKADQSLASLPSGLPITCHLCQKIYSNKGTFRAHYKTVHLRQLHKCKVPGCNTMFSSVRSRNRHSQNPNLHKSLASSPSHLQ
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Transcriptional activator. It is likely involved in the regulation of keratinocytes terminal differentiation in squamous epithelia and hair follicles (By similarity). Required for the maintenance of spermatogenesis. It is involved in the positive regulation of oocyte maturation, probably acting through the control of BMP15 levels and regulation of AKT signaling cascade (By similarity). May also play a role in the early development of embryos.
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O35921
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EAA4_RAT
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Excitatory amino acid transporter 4 (High-affinity neuronal glutamate transporter) (Sodium-dependent glutamate/aspartate transporter) (Solute carrier family 1 member 6)
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MSSHGNSLFLRESGAGGGCLQGLQDSLQQRALRTRLRLQTMTREHVRRFLRRNAFILLTVSAVIIGVSLAFALRPYQLTYRQIKYFSFPGELLMRMLQMLVLPLIVSSRVTGMASLDNKATGRMGMRAAVYYMVTTVIAVFIGILMVTIIHPGKGSKEGLHREGRIETVPTADAFMDLVRNMFPPNLVEACFKQFKTQYSTRVVTRTIVRTDNGSELGASISPPSSAENETSILENVTRALGTLQEVISFEETVPVPGSANGINALGLVVFSVAFGLVIGGMKHKGRVLRDFFDSLNEAIMRLVGIIIWYAPVGILFLIAGKILEMEDMAVLGGQLGMYTLTVIVGLFLHAGGVLPLIYFLVTHRNPFPFIGGILQALITAMGTSSSSATLPITFRCLEEGLGVDRRITRFVLPVGATVNMDGTALYEALAAIFIAQVNNYELNLGQITTISITATAASVGAAGIPQAGLVTMVIVLTSVGLPTEDITLIIAVDWFLDRLRTMTNVLGDSIGAAVIEHLSQRELELQEAELTLPSLGKPYKSLMAQAKGASRGRGGNESVM
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Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (Probable).
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O35923
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BRCA2_RAT
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Breast cancer type 2 susceptibility protein homolog (Fanconi anemia group D1 protein homolog)
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MTVEYKRRPTFWEIFKARCSTADLGPISLNWFEELFSEAPPYNTEHPEESEYKPQGHEPQLFKTPQRNPSYHQFASTPIMFKEQSQTLPLDQSPFKELGNVVANSKRKHHSKKKARKDPVVDVASLPLKACPSESPCTPRCTQVAPQRRKPVVSGSLFYTPKLEETPKHISESLGVEVDPDMSWTSSLATPPTLSSTVLIARDEEAHRNAFPADSPASLKSYFSNHNESLKKNDRFIPSVSDSENKSQQEAFSQGLEKMLGDSSSKINRFRDCLRKPIPNVLEDGETAVDTSGEDSFSLCFPKRRTRNLQKTRMGKMKKKIFSETRTDGLSEEARGQADDKNSFALEIEPRDSEPLDPSVTNQKPLYSQSGDISSEAGQCSDSIWSQPDPSGLNGTQTRKIPLLHISFHKQSILEDFIDMKKEGTGSITFPHISSLPEPEKMFSEETLVDKEHEGQHLESLEDSISGKQMVSGTSQTACLSPSIRKSIVKMREPLEETLDTVFSDSMTSSAFTEELDASAGGLEIHTACSQREDSLCPSSVDTGSWPTTLTDTSATVKNAGLITTLKNKRRKFIYSVSDDASHQGKKLQTQRQSELTNLSAPFEASAFEVPFPFTNVDSGIPDSSIKRSNLPNDPEEPSLSLTNSFVTAASKEISYIHALISQDLNDKEAILSEEKPQPYTALEADFLSCLPERSCENDQKSPKVSDRKEKVLVSACRPSGRLAAAVQLSSISFDSQENPLGSHNVTSTLKLTPSPKTPLSKPVVVSRGKMCKMPEKLQCKSCKDNIELSKNIPLGVNEMCVLSENSETPELLPPLEYITEVSSSVKSQFNQNTKIAVVQKDQKDSTFISEVTVHMNSEELFPEKENNFAFQVTNESNKPNIGSTVEFQEEDLSHAKGHSLKNSPMTVDRDLDDEQAGQVLITEDSDSLAVVHDCTKKSRNTIEQHQKGTADKDFKSNSSLYLKSDGNNDYLDKWSEFLDPLMNHKLGGSFRTASNKEIKLSEDNVKKSKMFFKDIEEQYPTSLDCIDTVSTLQLANKKRLSEPHTFDLKSGTTVSTQCHSQSSVSHEDTHTAPQMLSSKQDFHSSHNLTPSQKAEITELSTILEESGSQFEFTQFKNPSHIAQNNTSAVLGNQMAVVRTASEEWKDVDLHLPLNPSSVGQIDHNKKFECLVGVKQSSSHLLEDTCNQNTSCFLPIKEMEFGGFCSALGTKLSVSNEALRKAMKLFSDIENISEEPSTKVGPRGFSSCAHHDSVASVFKIKKQNTDKSFDEKSSKCQVTVQNNKEMTTCILVDENPENYVKNIKQDNNYTGSQRNAYKLENSDVSKSSTSGTVYINKGDSDLPFAAEKGNKYPESCTQYVREENAQIKESVSDLTCLEVMKAEETCHMKSSDKEQLPSDKMEQNMKEFNISFQTASGKNIRVSKESLNKSVNILDQETEDLTVTSDSLNSKILCGINKDKMHISCHKKSINIKKVFEEHFPIGTVSQLPALQQYPEYEIESIKEPTLLSFHTASGKKVKIMQESLDKVKNLFDETQYVRKTTNFGHQESKPLKDREDYKERLTLAYEKIEVTASKCEEMQNFVSKQTEMLPQQNDHMYRQTENLTSNGSSPKVHGNIENKIEKNPRICCICQSSYFVTEDSALACYTGDSRKTCVGESSLSKGKKWLREQSDKLGTRNTIEIQCVKEHTEDFAGNALYEHSLVIIRTEIDTSHVSENQASTLFSDPNVCHSYLSHSSFCHHDDMHNDSGYFLKDKIDSDVQPDMKNTEGNAIFPKISATKEIKLHPQTVNEECVQKLETNASPYANKNIAIDSAMLDLRNCKVGSPVFITTHSQETVRMKEIFTDNCSKIVEQNRESKPDTCQTSCHKALDNSEDFICPSSSGDVCINSPMAIFYPQSEQILQHNQSVSGLKKAATPPVSLETWDTCKSIRGSPQEVHPSRTYGFFSTASGKAVQVSDASLEKARQVFSEIDGDAKQLASMVSLEGNEKSHHSVKRESSVVHNTHGVLSLRKTLPGNVSSFVFSGFSTAGGKLVTVSESALHKVKGMLEEFDLIRTEHTLQHSPTPEDVSKIPPQPCLESRTPEYSVSSKLQKTYNDKSRSPSNYKESGSSGNTQSLEVSPQLSQMERKQETQSVLGTKVSQRKTNILEKKQNLPQNIKIESNKMETFSDVSMKTNVGEYYSKEPENYFETEAVEIAKAFMEDDELTDSEQTHAKCSLFACPQNEALLNSRTRKRGGMAGVAVGQPPIKRSLLNEFDRIIESKGKSLTPSKSTPDGTIKDRRLFTHHMSLEPVTCGPFCSSKERQETQSPHVTSPAQGLQSKEHPSRHSAVGKSSSNPTVSALRSERTRHSVSDKSTKVFVPPFKVKSRFHRDEHFDSKNVNLEGKNQKSADGVSEDGNDSDFPQFNKDLMSSLQNARDLQDIRIKNKERHHLCPQPGSLYLTKSSTLPRISLQAAVGDSVPSACSPKQLYMYGVSKACISVNSKNAEYFQFAIEDHFGKEALCAGKGFRLADGGWLIPSDDGKAGKEEFYRALCDTPGVDPKLISSVWVSNHYRWIVWKLAAMEFAFPKEFANRCLNPERVLLQLKYRYDVEIDNSSRSALKKILERDDTAAKTLVLCVSDIISLSTNVSETSGSKASSEDSNKVDTIELTDGWYAVKAQLDPPLLALVKSGRLTVGQKIITQGAELVGSPDACAPLEAPDSLRLKISANSTRPARWHSKLGFFHDPRPFPLPLSSLFSDGGNVGCVDVIVQRVYPLQWVEKTVSGSYIFRNEREEEKEALRFAEAQQKKLEALFTKVHTELKEHEEDIAQRRVLSRALTRQQVHALQDGAELYAAVQDASDPEHLETCFSEEQLRALNNYRQMLSDKKQARIQSEFRKALEAAEKEEGLSRDVSTVWKLRVTSYKKREKSALLSIWRPSSDLPSLLTEGQRYRIYHLSVSKSKNKFEWPSIQLTATKRTQYQQLPVSSETLLQLYQPRELLPFSKLSDPAFQPPCSEVDVVGVVVSVVKPIGLAPLVYLSDECLHLLVVKFGIDLNEDIKPRVLIAASNLQWRPESTSRVPTLFAGNFSVFSASPKEAHFQERVTNMKHAIENIDTFYKEAEKKLIQVLKGDSPKWSTPNKDPTREPYPASTCSASDLASGGQLPRSSPTDQQSYRSPLSCCTPTGKSTPLAHSAWMAAKSCSGENEIEDPKTCRKKRALDLLSRLPLPPPLSPVCTFVSPAAQKAFQPPRSCGTKYPTPLKKEGPSSPWSRAPFQKASGVSLLDCDSVADEELALLSTQALVPHSVGGSEQVFPSDSTRTEGPSASTEARPANRSKRESLRDCRDDSDGKLAAETVPDYS
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Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability, independently of its known role in homologous recombination (By similarity).
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O35926
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CD5R2_MOUSE
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Cyclin-dependent kinase 5 activator 2 (CDK5 activator 2) (Cyclin-dependent kinase 5 regulatory subunit 2) (p39) (p39I)
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MGTVLSLSPASSAKGRRPGGLPEEKKKAPPAGDEALGGYGAPPAGKGGKGESRLKRPSVLISALTWKRLVAASAKKKKGSKKVTPKPASTGPDPLVQQRNRENLLRKGRDGPDGGGTAKPLAVPVPTVPTTAATCEPPSGGSAAAPPPGSGGGKPPPPPPPAPQAAPPAPGGSPRRVIVQASTGELLRCLGDFVCRRCYRLKELSPGELVGWFRGVDRSLLLQGWQDQAFITPANLVFVYLLCRESLRGDELASAAELQAAFLTCLYLAYSYMGNEISYPLKPFLVEPDKERFWQRCLRLIQRLSPQMLRLNADPHFFTQVFQDLKNEGEAAASTGGPPSGSSASTTSSSSARDSCATGAKHWTMNLDR
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Activator of CDK5/TPKII.
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O35927
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CTND2_MOUSE
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Catenin delta-2 (Neural plakophilin-related ARM-repeat protein) (NPRAP) (Neurojungin)
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MFARKQSGAAPFGAMPVPDQPPSASEKNSSLSPGLNTSNGDGSETETTSAILASVKEQELQFERLTRELEAERQIVASQLERCKLGSETGSMSSISSAGEQFHWQTQDGQKDIEDELTTGLELVDSCIRSLQESGILDPQDYSTSERPSLLSQSALQLNSKPEGSFQYPASYHSNQTLALGDTAPSQLPARSTQARAAGQSFSQGTTGRAGHLAGSEPAPPPPPPREPFAPSLGSAFHLPDAPPAAAALYYSSSTLPAPPRGGSPLTTTQGGSPTKLQRGGSAPEGAAYAAPRGSSPKQSPSRLAKSYSTSSPINIVVSSAGLSPIRVTSPPTVQSTISSSPIHQLSSTIGTYATLSPTKRLVHASEQYSKHSQELYATATLQRPGSLAAGSRASYSSQHGHLAPELRALQSPEHHIDPIYEDRVYQKPPMRSLSQSQGDPLPPAHTGTFRTSTAPSSPGVDSVPLQRTGSQHGPQNAAAATFQRASYAAGPASNYADPYRQLQYCASVDSPYSKSGPALPPEGTLARSPSIDSIQKDPREFGWRDPELPEVIQMLQHQFPSVQSNAAAYLQHLCFGDNKIKAEIRRQGGIQLLVDLLDHRMTEVHRSACGALRNLVYGKANDDNKIALKNCGGIPALVRLLRKTTDLEIRELVTGVLWNLSSCDALKMPIIQDALAVLTNAVIIPHSGWENSPLQDDRKIQLHSSQVLRNATGCLRNVSSAGEEARRRMRECDGLTDALLYVIQSALGSSEIDSKTVENCVCILRNLSYRLAAETSQGQHMGTDELDGLLCGETNGKDTESSGCWGKKKKKKKSQDQWDGVGPLPDCAEPPKGIQMLWHPSIVKPYLTLLSECSNPDTLEGAAGALQNLAAGSWKGWAEDVAGMAYALRSLPEGAPCLPQWSVYIRAAVRKEKGLPILVELLRIDNDRVVCAVATALRNMALDVRNKELIGKYAMRDLVHRLPGGNNSNNSGSKAMSDDTVTAVCCTLHEVITKNMENAKALRDAGGIEKLVGISKSKGDKHSPKVVKAASQVLNSMWQYRDLRSLYKKDGWSQYHFVASSSTIERDRQRPYSSSRTPSISPVRVSPNNRSASAPASPREMISLKERKTDYESAGNNATYHGTKGEHTSRKDTMTAQNTGVSTLYRNSYGAPAEDIKQNQVSTQPVPQEPSRKDYETYQPFPNSTRNYDESFFEDQVHHRPPASEYTMHLGLKSTGNYVDFYSAARPYSELNYETSHYPASPDSWV
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Has a critical role in neuronal development, particularly in the formation and/or maintenance of dendritic spines and synapses. Involved in the regulation of canonical Wnt signaling (By similarity). It probably acts on beta-catenin turnover, facilitating beta-catenin interaction with GSK3B, phosphorylation, ubiquitination and degradation. May be involved in neuronal cell adhesion and tissue morphogenesis and integrity by regulating adhesion molecules. Functions as a transcriptional activator when bound to ZBTB33.
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O35929
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REM1_MOUSE
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GTP-binding protein REM 1 (Rad and Gem-like GTP-binding protein 1)
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MTLNTQQEAKTTLRRRASTPLPLSSRGHQPGRLCTAPSAPSQHPRLGQSVSLNPPVRKPSPAQDGWSSESSDSEGSWEALYRVVLLGDPGVGKTSLASLFAEKQDRDPHEQLGGVYERTLSVDGEDTTLVVMDTWEAEKLDESWCQESCLQAGSAYVIVYSIADRSSFESASELRIQLRRTHQANHVPIILVGNKADLARCREVSVEEGRACAVVFDCKFIETSATLQHNVTELFEGVVRQLRLRRQDNAAPETPSPRRRASLGQRARRFLARLTARSARRRALKARSKSCHNLAVL
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Promotes endothelial cell sprouting and actin cytoskeletal reorganization (By similarity). May be involved in angiogenesis. May function in Ca(2+) signaling.
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O35930
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GP1BA_MOUSE
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Platelet glycoprotein Ib alpha chain (GP-Ib alpha) (GPIb-alpha) (GPIbA) (Glycoprotein Ibalpha) (CD antigen CD42b) [Cleaved into: Glycocalicin]
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MALLILLFLLPSPLHSQHTCSISKVTSLLEVNCENKKLTALPADLPADTGILHLGENQLGTFSTASLVHFTHLTYLYLDRCELTSLQTNGKLIKLENLDLSHNNLKSLPSLGWALPALTTLDVSFNKLGSLSPGVLDGLSQLQELYLQNNDLKSLPPGLLLPTTKLKKLNLANNKLRELPSGLLDGLEDLDTLYLQRNWLRTIPKGFFGTLLLPFVFLHANSWYCDCEILYFRHWLQENANNVYLWKQGVDVKDTTPNVASVRCANLDNAPVYSYPGKGCPTSSGDTDYDDYDDIPDVPATRTEVKFSTNTKVHTTHWSLLAAAPSTSQDSQMISLPPTHKPTKKQSTFIHTQSPGFTTLPETMESNPTFYSLKLNTVLIPSPTTLEPTSTQATPEPNIQPMLTTSTLTTPEHSTTPVPTTTILTTPEHSTIPVPTTAILTTPKPSTIPVPTTATLTTLEPSTTPVPTTATLTTPEPSTTLVPTTATLTTPEHSTTPVPTTATLTTPEHSTTPVPTTATLTTPEPSTTLTNLVSTISPVLTTTLTTPESTPIETILEQFFTTELTLLPTLESTTTIIPEQNSFLNLPEVALVSSDTSESSPFLNSDFCCFLPLGFYVLGLLWLLFASVVLILLLTWTWHVTPHSLDMEQSAALATSTHTTSLEVQRARQVTMPRAWLLFLQGSLPTFRSSLFLWVRPNGRVGPLVAGRRPSALSQGRGQDLLGTVGIRYSGHSL
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GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium.
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O35936
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ALOX8_MOUSE
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Polyunsaturated fatty acid lipoxygenase ALOX8 (15-lipoxygenase 2) (15-LOX-2) (Arachidonate 15-lipoxygenase B) (15-LOX-B) (Arachidonate 8S-lipoxygenase) (8-LOX) (8S-LOX) (EC 1.13.11.-) (Linoleate 9S-lipoxygenase ALOX8) (EC 1.13.11.58)
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MAKCRVRVSTGEACGAGTWDKVSVSIVGTHGESPLVPLDHLGKEFSAGAEEDFEVTLPQDVGTVLMLRVHKAPPEVSLPLMSFRSDAWFCRWFELEWLPGAALHFPCYQWLEGAGELVLREGAAKVSWQDHHPTLQDQRQKELESRQKMYSWKTYIEGWPRCLDHETVKDLDLNIKYSAMKNAKLFFKAHSAYTELKVKGLLDRTGLWRSLREMRRLFNFRKTPAAEYVFAHWQEDAFFASQFLNGINPVLIRRCHSLPNNFPVTDEMVAPVLGPGTSLQAELEKGSLFLVDHGILSGVHTNILNGKPQFSAAPMTLLHQSSGSGPLLPIAIQLKQTPGPDNPIFLPSDDTWDWLLAKTWVRNSEFYIHEAVTHLLHAHLIPEVFALATLRQLPRCHPLFKLLIPHIRYTLHINTLARELLVAPGKLIDKSTGLGTGGFSDLIKRNMEQLNYSVLCLPEDIRARGVEDIPGYYYRDDGMQIWGAIKSFVSEIVSIYYPSDTSVQDDQELQAWVREIFSEGFLGRESSGMPSLLDTREALVQYITMVIFTCSAKHAAVSSGQFDSCVWMPNLPPTMQLPPPTSKGQARPESFIATLPAVNSSSYHIIALWLLSAEPGDQRPLGHYPDEHFTEDAPRRSVAAFQRKLIQISKGIRERNRGLALPYTYLDPPLIENSVSI
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Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Catalyzes the peroxidation of arachidonate and linoleate into (8S)-HPETE and (9S)-HPODE respectively. In addition to generate (8S)-HPETE from free arachidonic acid (AA), may produce other HETE isomers from phospholipid-esterified polyunsaturated fatty acids and minor products derived from (8S)-HPETE itself that may include leukotriene A4 and 8,15-diHPETE. With free arachidonate as substrate, has no detectable 15S-lipoxygenase activity and only displays a 8S-lipoxygenase activity. However may have a 15S-lipoxygenase activity with (8S)-HPETE to produce (8S,15S)-diHPETE and when oxidizes directly arachidonic acid esterified to membrane-bound phospholipids to produce a phospholipid-esterified 15-HpETE. May also catalyze (15S)-HPETE peroxidation to produce 8,15-diHPETE. May play a role in keratinocyte differentiation through activation of the peroxisome proliferator activated receptor signaling pathway.
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O35942
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NEK2_MOUSE
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Serine/threonine-protein kinase Nek2 (EC 2.7.11.1) (Never in mitosis A-related kinase 2) (NimA-related protein kinase 2)
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MPSRVEDYEVLHSIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEVEKQMLVSEVNLLRELKHPNIVSYYDRIIDRTNTTLYIVMEYCEGGDLASVISKGTKDRQYLEEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDSKHNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMSCLSYNEKSDIWSLGCLLYELCALMPPFTAFNQKELAGKIREGRFRRIPYRYSDGLNDLITRMLNLKDYHRPSVEEILESPLIADLVAEEQRRNLERRGRRSGEPSKLPDSSPVLSELKLKERQLQDREQALRAREDILEQKERELCIRERLAEDKLARAESLMKNYSLLKEHRLLCLAGGPELDLPSSAMKKKVHFHGESKENTARSENSESYLAKSKCRDLKKRLHAAQLRAQALADIEKNYQLKSRQILGMR
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Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC SGO1 NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (By similarity). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (By similarity). Phosphorylates and activates NEK11 in G1/S-arrested cells. Involved in the regulation of centrosome disjunction (By similarity).
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O35943
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FRDA_MOUSE
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Frataxin, mitochondrial (Fxn) (EC 1.16.3.1) [Cleaved into: Frataxin intermediate form; Frataxin mature form; Extramitochondrial frataxin]
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MWAFGGRAAVGLLPRTASRASAWVGNPRWREPIVTCGRRGLHVTVNAGATRHAHLNLHYLQILNIKKQSVCVVHLRNLGTLDNPSSLDETAYERLAEETLDSLAEFFEDLADKPYTLEDYDVSFGDGVLTIKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLARELTKALNTKLDLSSLAYSGKGT
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[Frataxin mature form]: Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly. Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release. Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+) the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation. May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (By similarity).
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O35945
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AL1A7_MOUSE
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Aldehyde dehydrogenase, cytosolic 1 (EC 1.2.1.3) (ALDH class 1) (ALDH-E1) (ALHDII) (Aldehyde dehydrogenase family 1 member A7) (Aldehyde dehydrogenase phenobarbital-inducible)
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MSSPAQPAVPAPLANLKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMQISQKNS
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Can oxidize benzaldehyde, propionaldehyde and acetaldehyde (By similarity). No detectable activity with retinal. {ECO:0000250, ECO:0000269|PubMed:10191271}.
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O35949
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ELOV3_MOUSE
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Elongation of very long chain fatty acids protein 3 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl3) (CIN-2) (Cold-inducible glycoprotein of 30 kDa) (ELOVL fatty acid elongase 3) (ELOVL FA elongase 3) (Very long chain 3-ketoacyl-CoA synthase 3) (Very long chain 3-oxoacyl-CoA synthase 3)
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MDTSMNFSRGLKMDLMQPYDFETFQDLRPFLEEYWVSSFLIVVVYLLLIVVGQTYMRTRKSFSLQRPLILWSFFLAIFSILGTLRMWKFMATVMFTVGLKQTVCFAIYTDDAVVRFWSFLFLLSKVVELGDTAFIILRKRPLIFVHWYHHSTVLLFTSFGYKNKVPSGGWFMTMNFGVHSVMYTYYTMKAAKLKHPNLLPMVITSLQILQMVLGTIFGILNYIWRQEKGCHTTTEHFFWSFMLYGTYFILFAHFFHRAYLRPKGKVASKSQ
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Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated and unsaturated acyl-CoA substrates with higher activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Participates in the formation of certain VLCFA and triglycerides in certain cells of the hair follicles and the sebaceous glands, required for skin barrier function. Critical enzyme for lipid accumulation and metabolic activity in brown adipocytes during the early phase of the tissue recruitment. Plays a role in lipid storage and in resistance to diet-induced obesity. {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10791983, ECO:0000269|PubMed:14581464, ECO:0000269|PubMed:16326704, ECO:0000269|PubMed:20605947}.
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O35952
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GLO2_RAT
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Hydroxyacylglutathione hydrolase, mitochondrial (EC 3.1.2.6) (Glyoxalase II) (Glx II) (Round spermatid protein RSP29)
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MVLGRGSLCLRSLSVLGAACARRGLGQALLGLSLCHTDFRKNLTVQQDMMKIELLPALTDNYMYLIIDEDTQEAAVVDPVQPQKVIETVKKHRVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYGGDDRIGALTHKVTHLSTLEVGSLSVKCLSTPCHTSGHICYFVSKPGSSEPSAVFTGDTLFVAGCGKFYEGTADEMYKALLEVLGRLPPDTKVICGHEYTVNNLKFARHVEPGNTAVQEKLAWAKEKNAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAGETDPVTTMRAIRREKDQFKVPRD
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Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
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O35954
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PITM1_MOUSE
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Membrane-associated phosphatidylinositol transfer protein 1 (Drosophila retinal degeneration B homolog 1) (RdgB1) (Mpt-1) (Phosphatidylinositol transfer protein, membrane-associated 1) (PITPnm 1) (Pyk2 N-terminal domain-interacting receptor 2) (NIR-2)
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MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGNGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRIVDTIDIVRDAVAPGEYKAEEDPRLYRSAKTGRGPLADDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWIELSMADIRALEEETARMLAQRMAKCNTGSEGPEAQTPGKSSTEARPGTSTAGTPDGPEAPPGPDASPDASFGKQWSSSSRSSYSSQHGGGVSPQSLSEWRMQNIARDSENSSEEEFFDAHEGFSDSDEVFPKEMTKWNSNDFIDAFASPTEVEGVPDPTVMATKGIEDGARAPRDSEGLDGAGDLVVEACSVHALFLILHSGSILDSGPGDTNSKQADVQTLSTAFEAVTRVHFPEALGHVALRLVPCPPICAAAYALVSNLSPYSHDGDSLSRSQDHIPLAALPLLATSSSRYQGAVATVIARTNQAYAAFLRSSEGTGFCGQVVLIGDGVGGILGFDALCHSASAGPGSRGSSRRGSMNNEMLSPEVGPVRDPLADGVEVLGRASPEPSALPAQRTFSDMANPDPDGSQNSLQVASTATSSGEPRRASTASCPPASSEAPDGPTNAARLDFKVSGFFLFGSPLGLVLALRKTVMPALEVAQLRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLAVPRYQKFPLGDGSSLLLADTLQTHSSLFLEELEMMVPSTPTSASGAFWKGSELGNEPASQTAAPSTTSEVVKILDRWWGNKRIDYSLYCPEALTAFPTVTLPHLFHASYWESADVVAFILRQVIEKERPQLTECEEPSIYSPAFPREKWQRKRTQVKIRNVTSNHRASDTVVCEGRPQVLNGRFMYGPLDVVTLTGEKVDVYVMTQPLSGKWIHFGTEVTNSSGRLTFPVPSERALGIGVYPVRMVVRGDHTYAECCLTVVSRGTEAVVFSIDGSFTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQHNFPHGVVSFCDGLTHDPLRQKAMFLQSLVQEVELNIVAGYGSPKDVAVYAALGLSPSQTYIVGRAVRKLQAQCQFLSDGYVAHLGQLEAGSHSHAPSGPPRAALAKSSYAVAAPVDFLRKQSQLLRSRGPSQVDREGPGTPPTTLARGKTRSISLKLDSEE
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Catalyzes the transfer of phosphatidylinositol (PI) between membranes (By similarity). Binds PI. Also binds phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding affinity order of PI > PA > PC (By similarity). Regulates RHOA activity, and plays a role in cytoskeleton remodeling (By similarity). Necessary for normal completion of cytokinesis (By similarity). Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus (By similarity). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus (By similarity). Required for protein export from the endoplasmic reticulum and the Golgi (By similarity). Binds calcium ions (By similarity).
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O35955
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PSB10_MOUSE
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Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i)
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MLKQAVEPTGGFSFENCQRNASLEHVLPGLRVPHARKTGTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEAITAGILSDLGSGGNVDACVITAGGAKLQRALSTPTEPVQRAGRYRFAPGTTPVLTREVRPLTLELLEETVQAMEVE
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The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Plays a role in determining the T-cell repertoire for an antiviral T-cell response.
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O35956
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S22A6_RAT
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Solute carrier family 22 member 6 (Organic anion transporter 1) (rOAT1) (renal organic anion transporter 1) (rROAT1)
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MAFNDLLKQVGGVGRFQLIQVTMVVAPLLLMASHNTLQNFTAAIPPHHCRPPANANLSKDGGLEAWLPLDKQGQPESCLRFTSPQWGPPFYNGTEANGTRVTEPCIDGWVYDNSTFPSTIVTEWNLVCSHRAFRQLAQSLYMVGVLLGAMVFGYLADRLGRRKVLILNYLQTAVSGTCAAYAPNYTVYCVFRLLSGMSLASIAINCMTLNVEWMPIHTRAYVGTLIGYVYSLGQFLLAGIAYAVPHWRHLQLVVSVPFFIAFIYSWFFIESARWYSSSGRLDLTLRALQRVARINGKQEEGAKLSIEVLRTSLQKELTLSKGQASAMELLRCPTLRHLFLCLSMLWFATSFAYYGLVMDLQGFGVSMYLIQVIFGAVDLPAKFVCFLVINSMGRRPAQMASLLLAGICILVNGIIPKSHTIIRTSLAVLGKGCLASSFNCIFLYTGELYPTVIRQTGLGMGSTMARVGSIVSPLVSMTAEFYPSMPLFIFGAVPVVASAVTALLPETLGQPLPDTVQDLKSRSRGKQNQQQQEQQKQMMPLQASTQEKNGL
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Secondary active transporter that functions as a Na(+)-independent organic anion (OA)/dicarboxylate antiporter where the uptake of one molecule of OA into the cell is coupled with an efflux of one molecule of intracellular dicarboxylate such as alpha-ketoglutarate or glutarate. Mediates the uptake of OA across the basolateral side of proximal tubule epithelial cells, thereby contributing to the renal elimination of endogenous OA from the systemic circulation into the urine (By similarity). Function as a biopterin transporters involved in the uptake and the secretion of coenzymes tetrahydrobiopterin (BH4) dihydrobiopterin (BH2) and sepiapterin to urine, thereby determining baseline levels of blood biopterins (By similarity). Transports prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) and may contribute to their renal excretion. Also mediates the uptake of cyclic nucleotides such as cAMP and cGMP. Involved in the transport of neuroactive tryptophan metabolites kynurenate (KYNA) and xanthurenate (XA) and may contribute to their secretion from the brain. May transport glutamate (By similarity). Also involved in the disposition of uremic toxins and potentially toxic xenobiotics by the renal organic anion secretory pathway, helping reduce their undesired toxicological effects on the body. Uremic toxins include the indoxyl sulfate (IS), hippurate, indole acetate (IA), 3-carboxy-4- methyl-5-propyl-2-furanpropionate(CMPF) and urate. Xenobiotics include the mycotoxin ochratoxin (OTA) (By similarity). May also contribute to the transport of organic compounds in testes across the blood-testis-barrier (By similarity). May also work as a bidirectional OA/dicarboxylate exchanger.
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O35963
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RB33B_MOUSE
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Ras-related protein Rab-33B
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MTSEMESSLEVSFSSSCAVSGASGCLPPARSRIFKIIVIGDSNVGKTCLTYRFCAGRFPDRTEATIGVDFRERAVDIDGERIKIQLWDTAGQERFRKSMVQHYYRNVHAVVFVYDMTNMASFHSLPAWIEECKQHLLANDIPRILVGNKCDLRSAIQVPTDLAQKFADTHSMPLFETSAKNPNDNDHVEAIFMTLAHKLKSHKPLMLSQLPDNRISLKPETKPAVTCWC
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Protein transport. Acts, in coordination with RAB6A, to regulate intra-Golgi retrograde trafficking (By similarity). It is involved in autophagy, acting as a modulator of autophagosome formation. {ECO:0000250, ECO:0000269|PubMed:18448665}.
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O35964
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SH3G1_RAT
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Endophilin-A2 (Endophilin-2) (SH3 domain protein 2B) (SH3 domain-containing GRB2-like protein 1) (SH3p8)
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MSVAGLKKQFYKASQLVSEKVGGAEGTKLDDDFREMEKKVDITSKAVAEVLVRTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGECMVRHGKELGGESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILEELADKLKRRVREASSRPRREFKPRPQEPFELGELEQPNGGFPCASAPKITASSSFRSGDKPTRTPSKSMPPLDQPSCKALYDFEPENDGELGFREGDLITLTNQIDENWYEGMLHGQSGFFPLSYVQVLVPLPQ
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Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity).
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O35969
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GAMT_MOUSE
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Guanidinoacetate N-methyltransferase (EC 2.1.1.2)
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MSSSAASPLFAPGEDCGPAWRAAPAAYDASDTHLQILGKPVMERWETPYMHALAAAAASRGGRVLEVGFGMAIAASRVQQAPIEEHWIIECNDGVFQRLQDWALRQPHKVVPLKGLWEEVAPTLPDGHFDGILYDTYPLSEEAWHTHQFNFIKNHAFRLLKTGGVLTYCNLTSWGELMKSKYTDITTMFEETQVPALQEAGFLKENICTEVMALVPPADCRYYAFPQMITPLVTKH
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Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. Important in nervous system development.
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O35973
|
PER1_MOUSE
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Period circadian protein homolog 1 (mPER1) (Circadian clock protein PERIOD 1) (Circadian pacemaker protein Rigui)
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MSGPLEGADGGGDPRPGEPFCPGGVPSPGAPQHRPCPGPSLADDTDANSNGSSGNESNGPESRGASQRSSHSSSSGNGKDSALLETTESSKSTNSQSPSPPSSSIAYSLLSASSEQDNPSTSGCSSEQSARARTQKELMTALRELKLRLPPERRGKGRSGTLATLQYALACVKQVQANQEYYQQWSLEEGEPCAMDMSTYTLEELEHITSEYTLRNQDTFSVAVSFLTGRIVYISEQAGVLLRCKRDVFRGARFSELLAPQDVGVFYGSTTPSRLPTWGTGTSAGSGLKDFTQEKSVFCRIRGGPDRDPGPRYQPFRLTPYVTKIRVSDGAPAQPCCLLIAERIHSGYEAPRIPPDKRIFTTRHTPSCLFQDVDERAAPLLGYLPQDLLGAPVLLFLHPEDRPLMLAIHKKILQLAGQPFDHSPIRFCARNGEYVTMDTSWAGFVHPWSRKVAFVLGRHKVRTAPLNEDVFTPPAPSPAPSLDSDIQELSEQIHRLLLQPVHSSSPTGLCGVGPLMSPGPLHSPGSSSDSNGGDAEGPGPPAPVTFQQICKDVHLVKHQGQQLFIESRAKPPPRPRLLATGTFKAKVLPCQSPNPELEVAPVPDQASLALAPEEPERKETSGCSYQQINCLDSILRYLESCNIPSTTKRKCASSSSYTASSASDDDKQRAGPVPVGAKKDPSSAMLSGEGATPRKEPVVGGTLSPLALANKAESVVSVTSQCSFSSTIVHVGDKKPPESDIIMMEDLPGLAPGPAPSPAPSPTVAPDPTPDAYRPVGLTKAVLSLHTQKEEQAFLNRFRDLGRLRGLDTSSVAPSAPGCHHGPIPPGRRHHCRSKAKRSRHHHHQTPRPETPCYVSHPSPVPSSGPWPPPPATTPFPAMVQPYPLPVFSPRGGPQPLPPAPTSVSPATFPSPLVTPMVALVLPNYLFPTPPSYPYGVSQAPVEGPPTPASHSPSPSLPPPPLSPPHRPDSPLFNSRCSSPLQLNLLQLEESPRTEGGAAAGGPGSSAGPLPPSEETAEPEARLVEVTESSNQDALSGSSDLLELLLQEDSRSGTGSAASGSLGSGLGSGSGSGSHEGGSTSASITRSSQSSHTSKYFGSIDSSEAEAGAARARTEPGDQVIKCVLQDPIWLLMANADQRVMMTYQVPSRDAASVLKQDRERLRAMQKQQPRFSEDQRRELGAVHSWVRKGQLPRALDVTACVDCGSSVQDPGHSDDPLFSELDGLGLEPMEEGGGEGGGCGVGGGGGDGGEEAQTQIGAKGSSSQDSAMEEEEQGGGSSSPALPAEENSTS
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Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates circadian target genes expression at post-transcriptional levels, but may not be required for the repression at transcriptional level. Controls PER2 protein decay. Represses CRY2 preventing its repression on CLOCK/BMAL1 target genes such as FXYD5 and SCNN1A in kidney and PPARA in liver. Besides its involvement in the maintenance of the circadian clock, has an important function in the regulation of several processes. Participates in the repression of glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) by BMAL1:CLOCK. Plays a role in the modulation of the neuroinflammatory state via the regulation of inflammatory mediators release, such as CCL2 and IL6. In spinal astrocytes, negatively regulates the MAPK14/p38 and MAPK8/JNK MAPK cascades as well as the subsequent activation of NFkappaB. Coordinately regulates the expression of multiple genes that are involved in the regulation of renal sodium reabsorption. Can act as gene expression activator in a gene and tissue specific manner, in kidney enhances WNK1 and SLC12A3 expression in collaboration with CLOCK. Modulates hair follicle cycling. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1.
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O35975
|
NAR2B_MOUSE
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T-cell ecto-ADP-ribosyltransferase 2 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 2) (ARTC2) (Mono(ADP-ribosyl)transferase 2B) (NAD(+) glycohydrolase) (EC 3.2.2.5) (T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 2) (T-cell differentiation marker Rt6 homolog 2) (T-cell mono(ADP-ribosyl)transferase 2)
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MTSKIFKFFLTWWLTQQVTGLAVPFMLDMAPNAFDDQYESCVEDMEKKAPQLLQEDFNMNEELKLEWEKAEINWKEIKNSTSYPAGFHDFHGTALVAYTGNLAIDFNRAVRDFKKSPDNFHYKAFHYYLTRAVQLLNDQGCSLVYRGTKVMFEYTGKGSVRFGQFSSSSLTKRVALSSNFFSNHGTLFIIRTCLGVNIKEFSSFPREEEVLIPGYEVYHKVTAQNDNGYNEIFLDSPERKKSNFNCFYNGSAQTVNIDFSISGSRESCVSLFLVVLLGLLVQQLTLAEL
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Has both NAD(+) glycohydrolase and ADP-ribosyltransferase activity.
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O35980
|
NTH_MOUSE
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Endonuclease III-like protein 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
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MNSGVRMVTRSRSRATRIASEGCREELAPREAAAEGRKSHRPVRHPRRTQKTHVAYEAANGEEGEDAEPLKVPVWEPQNWQQQLANIRIMRSKKDAPVDQLGAEHCYDASASPKVRRYQVLLSLMLSSQTKDQVTAGAMQRLRARGLTVESILQTDDDTLGRLIYPVGFWRNKVKYIKQTTAILQQRYEGDIPASVAELVALPGVGPKMAHLAMAVAWGTISGIAVDTHVHRIANRLRWTKKMTKTPEETRKNLEEWLPRVLWSEVNGLLVGFGQQICLPVHPRCQACLNKALCPAAQDL
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Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:9743625}.
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