ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O82318 | MSTSHHHHHPPYLITTLFFLFLNFSCLHANELELLLSFKSSIQDPLKHLSSWSYSSTNDVCLWSGVVCNNISRVVSLDLSGKNMSGQILTAATFRLPFLQTINLSNNNLSGPIPHDIFTTSSPSLRYLNLSNNNFSGSIPRGFLPNLYTLDLSNNMFTGEIYNDIGVFSNLRVLDLGGNVLTGHVPGYLGNLSRLEFLTLASNQLTGGVPVELGKMKNLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYNNLSGPIPPSLGDLKKLEYMFLYQNKLSGQIPPSIFSLQNLISLDFSDNSLSGEIPELVAQMQSLEILHL... | Function: Receptor with a serine/threonine-protein kinase activity (By similarity). Together with SKM2, LRR-rich receptor-like kinase (LRR-RLK) required for male fertility by the perception of CLE43 and CLE45 peptides and the transduction of their promoting action in pollen tubes, especially under relatively high tempe... |
Q12469 | MKGVKKEGWISYKVDGLFSFLWQKRYLVLNDSYLAFYKSDKCNEEPVLSVPLTSITNVSRIQLKQNCFEILRATDQKENISPINSYFYESNSKRSIFISTRTERDLHGWLDAIFAKCPLLSGVSSPTNFTHKVHVGFDPKVGNFVGVPDSWAKLLQTSEITYDDWNRNSKAVIKALQFYEDYNGLDTMQFNDHLNTSLDLKPLKSPTRYIINKRTNSIKRSVSRTLRKGKTDSILPVYQSELKPFPRPSDDDYKFTNIEDNKVREEGRVHVSKESTADSQTKQLGKKEQKVIQSHLRRHDNNSTFRPHRLAPSAPATKNH... | Function: May be involved in cellular signaling or cytoskeletal functions. May play a role in morphogenetic control.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 75331
Sequence Length: 655
EC: 2.7.11.1
|
P34707 | MGGSSRRQRSTSATRRDDKRRRRQCFSSVADDEEETTSIYGVSSIFIWILATSSLILVISSPSSNTSIQSSSYDRITTKHLLDNISPTFKMYTDSNNRNFDEVNHQHQQEQDFNGQSKYDYPQFNRPMGLRWRDDQRMMEYFMSNGPVETVPVMPILTEHPPASPFGRGPSTERPTTSSRYEYSSPSLEDIDLIDVLWRSDIAGEKGTRQVAPADQYECDLQTLTEKSTVAPLTAEENARYEDLSKGFYNGFFESFNNNQYQQKHQQQQREQIKTPTLEHPTQKAELEDDLFDEDLAQLFEDVSREEGQLNQLFDNKQQH... | Function: Transcription factor . Required to specify the fate of ventral blastomeres in the early embryo, and postembryonically for the development of the intestine . Directly regulates expression of zygotically expressed med-1 and med-2 to direct mesendoderm development . In response to oxidative stress and anoxia, re... |
P87024 | MERDLTYNAPKIKFTDTEGQEEHFYFNRSNNSTNDLTSHDSSSTQLQDANSRRQAPPPPPHNPFSDNSHENSTESLYQSETRFHQPLLHNDSNNSNSSIGNNRQRIPSQQHDTSSLYSASPISTSPLVSNFQSYSDNQDEMTRGKYNQNTNRSSSNYIQHSPTSAGYDRYPLKTQSSIGGSMSRIGLSSSSPSQQQQQHMYDNNSSNRSSYSPDSATDLMVYENGEFSPFGGYPASLFPLSIDEKEPDDYLHNPDPVQDAEYDKNRFLYDLKTMDKKSMNGLIAFIVMFLIAIAIFIILPVFTYTGYNPKAKNFENYEVL... | Function: Required for synthesis of the major beta-glucans of the cell wall.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 83708
Sequence Length: 737
Subcellular Location: Membrane
|
P23791 | MLLWSAVRGLSPPRIVPSLLVVVALAGLLPGLRSHGLQLSPTDSTTPDSQPSRERSIGDVTTAPPEVTPESRPVNRSVTEHGMKPRKAFPVLGIDYTHVRTPFEISLWILLACLMKIGFHVIPTISSIVPESCLLIVVGLLVGGLIKGVGEKPPFLQSEVFFLFLLPPIILDAGYFLPLRQFTENLGTILIFAVVGTLWNAFFLGGLMYAVCLVGGEQINNIGLLDNLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLNDAVTVVLYHLFEEFANYDHVGIVDIVLGFLSFFVVALGGVFVGVVYGVIAAFTS... | Function: Electroneutral Na(+) /H(+) antiporter that extrudes Na(+) in exchange for external protons driven by the inward sodium ion chemical gradient, protecting cells from acidification that occurs from metabolism (Probable). Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry (By similari... |
P26431 | MMLRWSGIWGLYPPRIFPSLLVVVALVGLLPVLRSHGLQLNPTASTIRGSEPPRERSIGDVTTAPSEPLHHPDDRNLTNLYIEHGAKPVRKAFPVLDIDYLHVRTPFEISLWILLACLMKIGFHVIPTISSIVPESCLLIVVGLLVGGLIKGVGETPPFLQSDVFFLFLLPPIILDAGYFLPLRQFTENLGTILIFAVVGTLWNAFFLGGLLYAVCLVGGEQINNIGLLDTLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLNDAVTVVLYHLFEEFASYEYVGISDIFLGFLSFFVVSLGGVFVGVVYGVIA... | Function: Electroneutral Na(+) /H(+) antiporter that extrudes Na(+) in exchange for external protons driven by the inward sodium ion chemical gradient, protecting cells from acidification that occurs from metabolism (Probable) . Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry . Plays a ke... |
Q3ZAS0 | MGPRGTAHSVRAPLSWLLLLLLSLQVAVPAGALAETLLDAPRARGASSNPPSPASVVAPGTTPFEESRLPVFTLDYPHVQIPFEITLWILLASLAKIGFHLYHKLPTIVPESCLLIMVGLLLGGIIFGVDEKSPPAMKTDVFFLYLLPPIVLDAGYFMPTRPFFENFGTIFWYAVVGTLWNSIGIGVSLFGICQIEAFGLSDITLLQNLLFGSLISAVDPVAVLAVFENIHVNEQLYILVFGESLLNDAVTVVLYNLFKSFCQMKTIQTVDVFAGIANFFVVGIGGVLIGILLGFIAAFTTRFTHNIRVIEPLFVFLYSY... | Function: Plasma membrane Na(+)/H(+) antiporter . Mediates the electroneutral exchange of intracellular H(+) ions for extracellular Na(+) . Major apical Na(+)/H(+) exchanger in the base of the colonic crypt . Controls in the colonic crypt intracellular pH (pHi) to direct colonic epithelial cell differentiation into the... |
P48763 | MGPSGTAHRMRAPLSWLLLLLLSLQVAVPAGALAETLLDAPGARGASSNPPSPASVVAPGTTPFEESRLPVFTLDYPHVQIPFEITLWILLASLAKIGFHLYHKLPTIVPESCLLIMVGLLLGGIIFGVDEKSPPAMKTDVFFLYLLPPIVLDAGYFMPTRPFFENLGTIFWYAVVGTLWNSIGIGLSLFGICQIEAFGLSDITLLQNLLFGSLISAVDPVAVLAVFENIHVNEQLYILVFGESLLNDAVTVVLYNLFKSFCQMKTIQTVDVFAGIANFFVVGIGGVLIGILLGFIAAFTTRFTHNIRVIEPLFVFLYSY... | Function: Plasma membrane Na(+)/H(+) antiporter. Mediates the electroneutral exchange of intracellular H(+) ions for extracellular Na(+) . Major apical Na(+)/H(+) exchanger in the base of the colonic crypt. Controls in the colonic crypt intracellular pH (pHi) to direct colonic epithelial cell differentiation into the a... |
P48764 | MWGLGARGPDRGLLLALALGGLARAGGVEVEPGGAHGESGGFQVVTFEWAHVQDPYVIALWILVASLAKIGFHLSHKVTSVVPESALLIVLGLVLGGIVWAADHIASFTLTPTVFFFYLLPPIVLDAGYFMPNRLFFGNLGTILLYAVVGTVWNAATTGLSLYGVFLSGLMGDLQIGLLDFLLFGSLMAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFESFVALGGDNVTGVDCVKGIVSFFVVSLGGTLVGVVFAFLLSLVTRFTKHVRIIEPGFVFIISYLSYLTSEMLSLSAILAITFCGICCQ... | Function: Plasma membrane Na(+)/H(+) antiporter . Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, playing a key role in salt and fluid absorption and pH homeostasis (By similarity). Major apical Na(+)/H(+) exchanger in kidney and intestine playing an important role in renal and intestine... |
P26432 | MSGRGGCGPCWGLLLALVLALGALPWTQGAEQEHHDEIQGFQIVTFKWHHVQDPYIIALWVLVASLAKIVFHLSHKVTSVVPESALLIVLGLVLGGIVLAADHIASFTLTPTVFFFYLLPPIVLDAGYFMPNRLFFSNLGSILLYAVVGTVWNAATTGLSLYGVFLSGIMGELKIGLLDFLLFGSLIAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFQSFVTLGGDKVTGVDCVKGIVSFFVVSLGGTLVGVVFAFLLSLVTRFTKHVRVIEPGFVFIISYLSYLTSEMLSLSSILAITFCGICCQK... | Function: Plasma membrane Na(+)/H(+) antiporter. Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, playing a key role in salt and fluid absorption and pH homeostasis . Major apical Na(+)/H(+) exchanger in kidney and intestine playing an important role in renal and intestine Na(+) absorptio... |
P26433 | MWHPALGPGWKPLLALALALTSLRGVRGIEEEPNSGGSFQIVTFKWHHVQDPYIIALWILVASLAKIVFHLSHKVTSVVPESALLIVLGLVLGGIVWAADHIASFTLTPTLFFFYLLPPIVLDAGYFMPNRLFFGNLGTILLYAVIGTIWNAATTGLSLYGVFLSGLMGELKIGLLDFLLFGSLIAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFESFVTLGGDAVTGVDCVKGIVSFFVVSLGGTLVGVIFAFLLSLVTRFTKHVRIIEPGFVFVISYLSYLTSEMLSLSAILAITFCGICCQKYV... | Function: Plasma membrane Na(+)/H(+) antiporter. Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, playing a key role in salt and fluid absorption and pH homeostasis . Major apical Na(+)/H(+) exchanger in kidney and intestine playing an important role in renal and intestine Na(+) absorptio... |
Q6AI14 | MALQMFVTYSPWNCLLLLVALECSEASSDLNESANSTAQYASNAWFAAASSEPEEGISVFELDYDYVQIPYEVTLWILLASLAKIGFHLYHRLPGLMPESCLLILVGALVGGIIFGTDHKSPPVMDSSIYFLYLLPPIVLEGGYFMPTRPFFENIGSILWWAVLGALINALGIGLSLYLICQVKAFGLGDVNLLQNLLFGSLISAVDPVAVLAVFEEARVNEQLYMMIFGEALLNDGITVVLYNMLIAFTKMHKFEDIETVDILAGCARFIVVGLGGVLFGIVFGFISAFITRFTQNISAIEPLIVFMFSYLSYLAAETL... | Function: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. May play a specialized role in the kidney in rectifying c... |
Q8BUE1 | MGPAMFMAFRLWNWLLLLAVLTRSEATSYVNESSNPTAQQAPDARFAASSSDPDEGISVFELDYDYVQIPYEVTLWILLASLAKIGFHLYHRLPHLMPESCLLIIVGALVGGIIFGTHHKSPPVMDSSIYFLYLLPPIVLESGYFMPTRPFFENIGSILWWAGLGALINAFGIGLSLYFICQIKAFGLGDINLLHNLLFGSLISAVDPVAVLAVFEEARVNEQLYMMIFGEALLNDGISVVLYNILIAFTKMHKFEDIEAVDILAGCARFVIVGCGGVFFGIIFGFISAFITRFTQNISAIEPLIVFMFSYLSYLAAETL... | Function: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. May play a specialized role in the kidney in rectifying c... |
Q14940 | MLRAALSLLALPLAGAAEEPTQKPESPGEPPPGLELFRWQWHEVEAPYLVALWILVASLAKIVFHLSRKVTSLVPESCLLILLGLVLGGIVLAVAKKAEYQLEPGTFFLFLLPPIVLDSGYFMPSRLFFDNLGAILTYAVVGTLWNAFTTGAALWGLQQAGLVAPRVQAGLLDFLLFGSLISAVDPVAVLAVFEEVHVNETLFIIVFGESLLNDAVTVVLYKVCNSFVEMGSANVQATDYLKGVASLFVVSLGGAAVGLVFAFLLALTTRFTKRVRIIEPLLVFLLAYAAYLTAEMASLSAILAVTMCGLGCKKYVEANI... | Function: Plasma membrane Na(+)/H(+) antiporter. Mediates the electroneutral exchange of intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, thus regulating intracellular pH homeostasis, in particular in neural tissues . Acts as a negative regulator of dendritic spine growth . Plays a role in postsyna... |
B2RXE2 | MLSAALLLLPGLPLAGAGATEEPTQESGPLGEPPPGLALFRWQWHEVEAPYLVALWILVASLAKIVFHLSRKVTSLVPESCLLILLGLVLGGIVLAVAKKAEYQLEPGTFFLFLLPPIVLDSGYFMPSRLFFDNLGAILTYAVVGTLWNAFTTGVALWGLQQAGLVAPRVQAGLLDFLLFGSLISAVDPVAVLAVFEEVHVNQTLFIIIFGESLLNDAVTVVLYKVCNSFVEMGSANVQATDYLKGVASLFVVSLGGAAVGLVFAFLLALTTRFTKRVRIIEPLLVFLLAYAAYLTAEMASLSAILAVTMCGLGCKKYVE... | Function: Plasma membrane Na(+)/H(+) antiporter. Mediates the electroneutral exchange of intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry. Responsible for regulating intracellular pH homeostasis, in particular in neural tissues. Acts as a negative regulator of dendritic spine growth. Plays a role in... |
A8E1U5 | STLEVRSQATQDLSEYYNRPYFDLRNLSGYREGNTVTFINHYQQTDVKLEGKDKDKIKDGNNENLDVFVVREGSGRQADNNSIGGITKTNRTQHIDTVQNVNLLVSKSTGQHTTSVTSTNYSIYKEEISLKELDFKLRKHLIDKHDLYKTEPKDSKIRVTMKNGDFYTFELNKKLQTHRMGDVIDGRNIEKIEVNL | Function: Secreted protein that plays a role in the inhibition of host immune system. Targets myeloid cells such as monocytes or granulocytes through binding with sialyllactosamine-containing glycoproteins . Prevents initial rolling of neutrophils toward the site of infection by interacting with host SELPLG . Disrupts ... |
Q4PRD1 | MGRFISVSFGCLVVFLSLSGTEAVLDCPSGWLSYEQHCYKGFNDLKNWTDAEKFCTEQKKGSHLVSLHSREEEEFVVNLISENLEYPATWIGLGNMWKDCRMEWSDRGNVKYKALAEESYCLIMITHEKEWKSMTCNFIAPVVCKF | Function: Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite ... |
Q4PRD2 | MGRFISVSFGLLVVFLSLSGTGAGLDCPPDSSLYRYFCYRVFKEHKTWEAAERFCMEHPNNGHLVSIESMEEAEFVAKLLSNTTGKFITHFWIGLMIKDKEQECSSEWSDGSSVSYDKLGKQEFRKCFVLEKESGYRMWFNRNCEERYLFVCKVPPEC | Function: Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite ... |
P40485 | MSKNNTMTSAVSDMLSQQQLNLQHLHNLQQHTRSMTSADHANVLQQQQQQQQQQQQQQQQQQQSASFQNGSLTSDINQQSYLNGQPVPSTSNSTFQNNRTLTMNSGGLQGIISNGSPNIDSNTNVTIAVPDPNNNNGKQLQGKNSLTNTSILSRARSSLQRQRLAQQQQQQQDPRSPLVILVPTAAQPTDILAARFSAWRNVIKSVIVYLTEIASIQDEIVRQQLRLSHAVQFPFFSIENQYQPSSQEDKSVQKFFLPLGNGSIQDLPTILNQYHESLASSASKASRELTNDVIPRLEDLRRDLIVKIKEIKSLQSDFKN... | Function: Together with SLM2, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by ... |
Q9JXM5 | MLYFRYGFLVVWCAAGVSAAYGADAPAILDDKALLQVQRSVSDKWAESDWKVENDAPRVVDGDFLLAHPKMLEHSLRDALNGNQADLIASLADLYAKLPDYDAVLYGRARALLAKLAGRPAEAVARYRELHGENAADERILLDLAAAEFDDFRLKSAERHFAEAAKLDLPAPVLENVGRFRKKTEGLTGWRFSGGISPAVNRNANNAAPQYCRQNGGRQICSVSRAERAAGLNYEIEAEKLTPLADNHYLLFRSNIGGTSYYFSKKSAYDDGFGRAYLGWQYKNARQTAGILPFYQVQLSGSDGFDAKTKRVNNRRLPPY... | Function: Required for correct export to the cell surface of cell outer membrane lipoprotein HpuA heterologously in E.coli (hpuA does not exist in N.meningitidis strain MC58).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56756
Sequence Length: 505
Domain: Consists of a soluble N-terminal domain an... |
P53955 | MSYQRNSARASLDLRSQYQQLEGRMRSEHFNPAYQQQQQKGQNIPLSLPSSLAQRNPIPYPIDAVTSDPTIPAQLNVYDHDRQNSIVDAAAGTNTTHSLNSNNIPSSQNNNINNNNINNVGSFTDPSMLTLPKMSLHSHQKQYDSNQNDPRSPLAILIPTSAQPTDVLSARFSAWRNVIRAILVYLSETASIQDEIVRQQLRLSHAVQFPFFSIENQYQPVSNEDKSMQKFFLPLGSGSVQDLPTMLTKYHDNLASLASKSSKELTSEIIPRLEDLRRDLLVKIKEIKALQSDFKNSCNKELQQTKHLMKLFNESLKECK... | Function: Together with SLM1, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by ... |
P38247 | MVMLHSKNVKGFLENTLKPYDLHSVDFKTSSLQSSMIITATNGGILSYATSNNDVPKNSINEINSVNNLKMMSLLIKDKWSEDENDTEEQHSNSCYPVEIDSFKTKIYTYEMEDLHTCVAQIPNSDLLLLFIAEGSFPYGLLVIKIERAMRELTDLFGYKLG | Function: Component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome . Component of the EGO complex, a complex involved in the regulation of microautophagy .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18354
Sequence Length: 162
Subcellular Loca... |
Q14BN4 | MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLPDGMEARLRSDVIHAPLPSPVDKVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK... | Function: May play a role during myoblast fusion.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 95198
Sequence Length: 828
Subcellular Location: Cell membrane
|
Q3URD3 | MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLPDGMEARLRSDVIHAPLPSPVDKVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK... | Function: May play a role during myoblast fusion.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 96933
Sequence Length: 845
Subcellular Location: Cell membrane
|
O95391 | MSATVVDAVNAAPLSGSKEMSLEEPKKMTREDWRKKKELEEQRKLGNAPAEVDEEGKDINPHIPQYISSVPWYIDPSKRPTLKHQRPQPEKQKQFSSSGEWYKRGVKENSIITKYRKGACENCGAMTHKKKDCFERPRRVGAKFTGTNIAPDEHVQPQLMFDYDGKRDRWNGYNPEEHMKIVEEYAKVDLAKRTLKAQKLQEELASGKLVEQANSPKHQWGEEEPNSQMEKDHNSEDEDEDKYADDIDMPGQNFDSKRRITVRNLRIREDIAKYLRNLDPNSAYYDPKTRAMRENPYANAGKNPDEVSYAGDNFVRYTGD... | Function: Required for pre-mRNA splicing as component of the spliceosome . Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and... |
Q24179 | MLTLRERQINAIKQMLNLNSQQPKALAAEPVWKILIYDRVGQDIISPIISIKELRELGVTLHVQLHSDRDSIPDVPAIYFCLPTDENLDRIQQDFSSGLYDVYHLNFLAPITRSKIENLAAAALHAGCVANIHRVYDQYVNFISLEDDFFILKHQQSDQLSYYAINRANTRDEEMEALMDSIVDSLFALFVTLGNVPIIRCPRNSAAEMVARKLEKKLRENLWDARANLFHMDATQAGGGVFSFQRPVLLLLDRNMDLATPLHHTWSYQALVHDVLDLGLNLVYVEDETASAGARKKPKACDLDRNDRFWMTHKGSPFPT... | Function: Non-vital for development.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 72366
Sequence Length: 639
Subcellular Location: Cytoplasm
|
Q8SS97 | MLRELQKQRIKAFLVAPNNPWKILVLDSRTQQIIGPLMKVSELRECGITAHFLVTQERHPISNTPAVYFVESADGVLDDVLAELYSEYYLNFATSVTRGEIESLGLGLSERGLGLRIRSVYDQFVDFIALQDDMFTLGMKGSFIEMENPDTWRRMVMSVMSVFVTLGEVPFIVATDDDVTTQMARMLETKIRNTGVIKRGSKRPVLVLVSRSHDVITPVQHVWSYSALMNDLFALESNKITLKSGKVFDLDPQDELWRRNANEYFPVVVERVEKELLEYKKEMALRSIDEKTDKKVIQEALDKAPELAKRNESVNAHISI... | Function: Involved in vesicular transport between the endoplasmic reticulum and the Golgi.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59195
Sequence Length: 521
Subcellular Location: Cytoplasm
|
P22213 | MAVEEIASRKDISLRDMQISAILKMLFLNKDLNNNDNITTITDDIFNQQEIIWKVLILDIKSTATISSVLRVNDLLKAGITVHSLIKQDRSPLPDVPAIYFVSPTKENIDIIVNDLKSDKYSEFYINFTSSLPRNLLEDLAQQVSITGKSDKIKQVYDQYLDFIVTEPELFSLEISNAYLTLNDPKTTEEEITGLCANIADGLFNTVLTINSIPIIRAAKGGPAEIIAEKLGTKLRDFVINTNSSSTSTLQGNDSLERGVLIILDRNIDFASMFSHSWIYQCMVFDIFKLSRNTVTIPLESKENGTDNTTAKPLATKKYD... | Function: Able to suppress the functional loss of YPT1. SLY1 is essential for cell viability. May interact indirectly, or directly with YPT1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74679
Sequence Length: 666
Subcellular Location: Cytoplasm
|
P22215 | MIQTQSTAIKRRNSVHKNLFDPSLYQIPEPPRGGFQHQKKEYSKETFSNQVFGYDITSLKKRFTQLFPSNIQGYLPEVDLRITIICSIWYVTSSISSNLSKAILRTFNHPIALTELQFLVSAVLCVGFASIVNLFRLPRLKHTKFSKALNSFPDGILPEYLDGNFRSSILHKFLVPSKLVLMTTFPMGIFQFIGHITSHKAVSMIPVSLVHSVKALSPIITVGYYKFFEHRYYNSMTYYTLLLLIFGVMTTCWSTHGSKRASDNKSGSSLIGLLFAFISMIIFVAQNIFAKNILTIRRKVGILPSSSTDDVTSKEGQPSL... | Function: Able to suppress the functional loss of YPT1. May form a channel. Protein SLY41 is not essential for cell viability. The SLY41 gene is a multicopy suppressor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50903
Sequence Length: 453
Subcellular Location: Membrane
|
P23126 | MFSFHERMKKKHVTIRVYKHERILVFLFVLFISTTDFSTEIIMIQTINWIVWKLFIIYISLDLFSLKLVNSEENSNSIITDEDYDHYNSSLDSSNNVKHSQEAFHRNSDPDGFPEYEFLNETSIEIKEELGQELHQLQLILDELSRRIRATPNSANKYMKNEFLMSSCIVITLNLFIFMYKS | Function: Major antigen in the surface tegument.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21649
Sequence Length: 182
Subcellular Location: Cell membrane
|
Q4VNK0 | MVTGNTKAETFYSMKELLKETGGYAIIDGGLATELERHGADLNDPLWSAKCLLTSPHLIHTVHLDYLEAGADIISSASYQATIQGFEAKGYSIEKSESLLRKSVEIACEARSTYYDKCKDDDDKKILKKRPILVAASVGSYGAFLADGSEYSGIYGDLITLETLKDFHRRRVQVLAESGADIIAFETIPNKLEAQAFAELLDEGVAKIPGWFSFNSKDGVNVVSGDSIKECIAIAEACEKVVAVGINCTPPRFIEGLVLEIAKVTSKPILVYPNSGERYDPERKEWVENTGVGNEDFVSYVEKWMDAGVSLLGGCCRTTP... | Function: Catalyzes the methylation of DL- and L-selenocysteine with S-methylmethionine as donor. Methylates also DL-homocysteine, DL- and L-cysteine in vitro. May be involved in selenium detoxification.
Catalytic Activity: L-selenocysteine + S-methyl-L-methionine = H(+) + L-methionine + Se-methyl-L-selenocysteine
Sequ... |
A9WC40 | MAKASRLTRSTGQPTEVSEGQVTGTSEMPPTGEEPSGHAESKPPASDPMSTPGTGQEQLPLSGIRVIDVGNFLAGPYAASILGEFGAEVLKIEHPLGGDPMRRFGTATARHDATLAWLSEARNRKSVTIDLRQQEGVALFLKLVAKSDILIENFRPGTMEEWGLSWPVLQATNPGLIMLRVSGYGQTGPYRRRSGFAHIAHAFSGLSYLAGFPGETPVLPGTAPLGDYIASLFGAIGILIALRHKEQTGRGQLIDVGIYEAVFRILDEIAPAYGLFGKIREREGAGSFIAVPHGHFRSKDGKWVAIACTTDKMFERLAEA... | Function: Involved in the 3-hydroxypropionate cycle used for autotrophic carbon dioxide fixation. Catalyzes the transfer of CoA moiety from succinyl-CoA to L-malate to yield L-malyl-CoA (By similarity).
Catalytic Activity: (S)-malate + succinyl-CoA = (S)-malyl-CoA + succinate
Sequence Mass (Da): 49514
Sequence Length: ... |
A9WC39 | MDGTTTTLPLAGIRVIDAATVIAAPFCATLLGEFGADVLKVEHPIGGDALRRFGTPTARGDTLTWLSESRNKRSVTLNLQHPEGARVFKELIAHSDVLCENFRPGTLEKWGLGWDVLSKINPRLIMLRVTGYGQTGPYRDRPGFARIAHAVGGIAYLAGMPKGTPVTPGSTTLADYMTGLYGCIGVLLALRHREQTGRGQYIDAALYESVFRCSDELVPAYGMYRKVRERHGSHYNEFACPHGHFQTKDGKWVAISCATDKLFARLANAMGRPELASSSVYGDQKVRLAHASDVNEIVRDWCSSLTRAEVLERCYATATP... | Function: Involved in the 3-hydroxypropionate cycle used for autotrophic carbon dioxide fixation. Catalyzes the transfer of CoA moiety from succinyl-CoA to L-malate to yield L-malyl-CoA (By similarity).
Catalytic Activity: (S)-malate + succinyl-CoA = (S)-malyl-CoA + succinate
Sequence Mass (Da): 44384
Sequence Length: ... |
A0A1U8QNM5 | MSEEKKSVELSGDIDFIETPPAKASQFETGEDCGIEVTKAAAIPNPPLAVDGPGNESFSNYLLGGTLVGLPAFLTWFFGGGAKTFVFFFLLSVLPVLVAFWTYASTFSPRTNEKVKLPGRPVEHYITFKREEDKAKWHGKNKIPMQTFAEMYLDGLVDFNGDTLDVMEYRHDWANFSFTWDLFKFIVGTFFVDVLFHTKAQDEEQVRPNYDSGNDHYAWFLGPRMIYTSGIISDPEKEETLEEMQDNKMAIVCEKIGLKEGETMLDIGCGWGTLARFASLNYGAKVTGLTIAENQTAWGNDALRKAGIPEEQSKILCMDY... | Function: Catalyzes methylation of the sphingoid base component of glucosylceramides (GluCers) at the C9-position . Sphingolipid C9-methylation requires 4,8-desaturated ceramides as substrates (By similarity). Glucosylceramides play important roles in growth, differentiation and pathogenicity . The methyl group at the ... |
A8MU46 | MEQKEGKLSEDGTTVSPAADNPEMSGGGAPAEETKGTAGKAINEGPPTESGKQEKAPAEDGMSAELQGEANGLDEVKVESQREAGGKEDAEAELKKEDGEKEETTVGSQEMTGRKEETKSEPKEAEEKESTLASEKQKAEEKEAKPESGQKADANDRDKPEPKATVEEEDAKTASQEETGQRKECSTEPKEKATDEEAKAESQKAVVEDEAKAEPKEPDGKEEAKHGAKEEADAKEEAEDAEEAEPGSPSEEQEQDVEKEPEGGAGVIPSSPEEWPESPTGEGHNLSTDGLGPDCVASGQTSPSASESSPSDVPQSPPES... | Function: Plays a role in the regulation of contractile properties of both striated and smooth muscles. When unphosphorylated, may inhibit myosin dephosphorylation. Phosphorylation at Ser-299 reduces this inhibitory activity (By similarity).
PTM: Maximal phosphorylation of Ser-336 correlates with maximal relaxation of ... |
Q99LM3 | MEQTEGNSSEDGTTVSPTAGNLETPGSQGIAEEVAEGTVGTSDKEGPSDWAEHLCKAASKSGESGGSPGEASILDELKTDLQGEARGKDEAQGDLAEEKVGKEDTTAASQEDTGKKEETKPEPNEVREKEEAMLASEKQKVDEKETNLESKEKSDVNDKAKPEPKEDAGAEVTVNEAETESQEEADVKDQAKPELPEVDGKETGSDTKELVEPESPTEEQEQGKENESEERAAVIPSSPEEWPESPTDEGPSLSPDGLAPESTGETSPSASESSPSEVPGSPTEPQPSEKKKDRAPERRVSAPSRPRGPRAQNRKAIMDK... | Function: Plays a role in the regulation of contractile properties of both striated and smooth muscles. When unphosphorylated, may inhibit myosin dephosphorylation. Phosphorylation at Ser-301 reduces this inhibitory activity.
PTM: Maximal phosphorylation of Ser-301 correlates with maximal relaxation of aorta in respons... |
H2E7U0 | MVSELVSMYVPPIVEAAKAVTPWQAAAGVTAAIFIGSYLWHSASLRKQRRTGTADGGLFSLTAGGIKKQDVTKLVDSFSQAYKTEDDGQLTCHHITREQSVEMVNTFYDLITDLYEWAWDTSFHFSCRPRWANFAQAQVLHEWRIANLANIQPGMKVLDVGTGVGNPGRTIASLSGAQVTGVTINAYQVKRALHHTRKAKLEDFYKPVQADFTDTPFEDDTFDAAFAIEATCHAPKLEQVYKEVYRVLKPGAYFALYDGVTKPNFDPKNERHVQLMNATVIGNGCPDMRTWKECEEIGKEVGFKLHMSYDAGEASRVLHP... | Function: Unable to convert squalene, botryococcene, cycloartenol, zymosterol or lanosterol to mono-, di-, tri- or tetramethylated derivatives.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 43903
Sequence Length: 392
Subcellular Location: Microsome membrane
EC: 2.1.1.-
|
Q64666 | MLSIHPLKPEALHLPLGTSEFLGCQRRHTLPASEFRCLTPEDATSAFEIEREAFISVSGTCPLHLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLTQESLTLHRPGGRTAHLHVLAVHRTFRQQGKGSVLLWRYLHHLGSQPAVRRAVLMCENALVPFYEKFGFQAMGPCAITMGSLTFTELQCSLRCHTFLRRNSGC | Function: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.
PTM: cAMP-dependent phosphorylation on both N-terminal Thr-29 and C-terminal Ser-203 regulates AANAT activity by promo... |
Q29495 | MSTPSVHCLKPSPLHLPSGIPGSPGRQRRHTLPANEFRCLTPEDAAGVFEIEREAFISVSGNCPLNLDEVQHFLTLCPELSLGWFVEGRLVAFIIGSLWDEERLTQESLALHRPRGHSAHLHALAVHRSFRQQGKGSVLLWRYLHHVGAQPAVRRAVLMCEDALVPFYQRFGFHPAGPCAIVVGSLTFTEMHCSLRGHAALRRNSDR | Function: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.
PTM: cAMP-dependent phosphorylation on both N-terminal Thr-31 and C-terminal Ser-205 regulates AANAT activity by promo... |
P31109 | MSSSTPFDPYALSEHDEERPQNVQSKSRTAELQAEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAVSAQGFKRGANRVRKAMWYKDLKMKMCLALVIIILLVVIIVPIAVHFSR | Function: SNC1 and SNC2 are vesicle-targeting proteins essential for normal secretory traffic between the Golgi and the plasma membrane. They may also be involved in vesicle fusion.
PTM: Palmitoylated by SWF1.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 13201
Sequence Length: 117
Subcell... |
P33328 | MSSSVPYDPYVPPEESNSGANPNSQNKTAALRQEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAISAQGFKRGANRVRKQMWWKDLKMRMCLFLVVIILLVVIIVPIVVHFS | Function: SNC1 and SNC2 are vesicle-targeting proteins essential for normal secretory traffic between the Golgi and the plasma membrane. They may also be involved in vesicle fusion.
PTM: Palmitoylated by SWF1.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 12957
Sequence Length: 115
Subcell... |
Q9Y6H5 | MEAPEYLDLDEIDFSDDISYSVTSLKTIPELCRRCDTQNEDRSVSSSSWNCGISTLITNTQKPTGIADVYSKFRPVKRVSPLKHQPETLENNESDDQKNQKVVEYQKGGESDLGPQPQELGPGDGVGGPPGKSSEPSTSLGELEHYDLDMDEILDVPYIKSSQQLASFTKVTSEKRILGLCTTINGLSGKACSTGSSESSSSNMAPFCVLSPVKSPHLRKASAVIHDQHKLSTEETEISPPLVKCGSAYEPENQSKDFLNKTFSDPHGRKVEKTTPDCQLRAFHLQSSAAESKPEEQVSGLNRTSSQGPEERSEYLKKVK... | Function: Isoform 2 inhibits the ubiquitin ligase activity of SIAH1 and inhibits proteasomal degradation of target proteins. Isoform 2 inhibits autoubiquitination and proteasomal degradation of SIAH1, and thereby increases cellular levels of SIAH. Isoform 2 modulates SNCA monoubiquitination by SIAH1.
PTM: Ubiquitinated... |
Q9W0S7 | MATAANTATAAGAAKDAPPAPTKSLSGIVKQVLSGDTVVIRATKGAPPPEKQITFSHVLAPKLARRPGAGGDETKDEPWAWESREFLRKKLIGVEVTFTFDKPANSNREYGFVWIGKDKETGENVVESIVREGLVSVRREGRPTAEQQTLIELEDQARAAGRGKWSPTASAADKVRNIKWSHENPAHLVDIYGGNPVKAIIEHVRDGSTVRAFLLPDFHYITLMISGIRCPGVKLDADGKPDLSVKVPFADEARYYVETRLLQRDVEIRLESVNNSNFIGTILYPKGNIAESLLREGLAKCVDWSMAVMKTGTDKLRAAE... | Function: Endonuclease which shows activity towards both DNA and RNA substrates . Has a role in translation regulation throught its association with the with the RNA-induced silencing complex (RISC) . Plays a role in spermatogenesis probably by negatively regulating piwi expression in the germline . Together with piwi,... |
Q7KZF4 | MASSAQSGGSSGGPAVPTVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKPVNAIIEHVRDGSVVRALLLPDYYLVTVMLSGIKCPTFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNILGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKE... | Function: Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs . As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition . Functions as a bridging factor between STAT6 and the basal transcription factor . Plays a role in PIM1 regulation of MYB activity ... |
O43290 | MGSSKKHRGEKEAAGTTAAAGTGGATEQPPRHREHKKHKHRSGGSGGSGGERRKRSRERGGERGSGRRGAEAEARSSTHGRERSQAEPSERRVKREKRDDGYEAAASSKTSSGDASSLSIEETNKLRAKLGLKPLEVNAIKKEAGTKEEPVTADVINPMALRQREELREKLAAAKEKRLLNQKLGKIKTLGEDDPWLDDTAAWIERSRQLQKEKDLAEKRAKLLEEMDQEFGVSTLVEEEFGQRRQDLYSARDLQGLTVEHAIDSFREGETMILTLKDKGVLQEEEDVLVNVNLVDKERAEKNVELRKKKPDYLPYAEDE... | Function: Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA.
PTM: Sumoylated with SUMO2.
Sequence Mass (Da): 90255
Sequence Length: 800
Subcellular Location: Nucleus
|
Q9Z315 | MGSSKKHRGEKEAAGTTAAAGTGGTTEQPPRHREHKKHKHRSSGGGSSGGERRKRSRERGSERGSGRRGAEAEARSGAHGRERSQAEPSERRVKREKRDDGYEAAASSKASSGDASSLSIEETNKLRAKLGLKPLEVNAVKKEAGTKEEPVAADVINPMALRQREELREKLAAAKEKRLLNQKLGKIKTLGEDDPWLDDTAAWIERSRQLQKEKDLAEKRAKLLEEMDQEFGVSTLVEEEFEQRRQDLYSARDLQGLTVEHAIDSFREGETVVLTLKDKGVLQDGEDVLVNVNMVDKERADKNVELRKKKPDYLPYAEDE... | Function: Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA. Appears to play a role in hypoxia-induced regulation of EPO gene expression.
PTM: Sumoylated with SUMO2.
Sequence Mass (Da): 90885
Sequence Length: 806
Subcellular Locat... |
Q5B797 | MDHDDFDSVSWRHGPDSDISRPTTSGTDTAESPETRRDPNGKRRMSSASEIPQAGPHADALDLAGIGDGVLECRVDTPIKENDGTKDAYISYLVTTHTDFKSFQKADFTVRRRFTDFVFLYKTLYREYPACAVPPLPDKHKMEYVRGDRFGAEFTTRRAWSLHRFLKRLTLHPVLRRAPLLAIFLESPDWNAHMRLRGSRASTSGSDGGGTGIFDNFTDTFVNAFTKVHKPDRRFIEVREKADKLDEDLTHVEKIVARVARREADLETDYNDLATQFRKLVPLEPEVEVPLQVFAASVEETARGIKNLKDHTDQNYLGSL... | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Pe... |
I1RXT2 | MTATEQQQDDFSNVSWSEHVHDQQTRSVPDAEEPGHDMNAPGTGLERDAPSLGNEKLECTVDTPIKENDGTKDAFVSYLITTHSTFSSFQRSTTTVRRRFTDFVFLYKQLTRDYPAAAVPPLPDKQRMEYVRGDRFGSDFTTRRANSLQRFLSRLSLHPTLRRAPILHTFLESPDWNATMRSRGSRVSSASDPGSAGVFDNFADTFINAFTKLHRPDRRFLEVKEKSDKLDDDLGHIEKVIARVARREADLEVDLRDLAEQFQKLIPLEPHVEPAVHGFSASIEDTASHLRKLKDMTDQDYLGSLRDMQAYSIALKNLLK... | Function: Sorting nexin involved in the separation or division of vacuoles throughout the entire life cycle of the cells (By similarity). Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), mitophagy, and pexophagy (By similarity). A... |
O95219 | MEQAPPDPERQLQPAPLEPLGSPDAGLGAAVGKEAEGAGEESSGVDTMTHNNFWLKKIEISVSEAEKRTGRNAMNMQETYTAYLIETRSVEHTDGQSVLTDSLWRRYSEFELLRSYLLVYYPHIVVPPLPEKRAEFVWHKLSADNMDPDFVERRRIGLENFLLRIASHPILCRDKIFYLFLTQEGNWKETVNETGFQLKADSRLKALNATFRVKNPDKRFTDLKHYSDELQSVISHLLRVRARVADRLYGVYKVHGNYGRVFSEWSAIEKEMGDGLQSAGHHMDVYASSIDDILEDEEHYADQLKEYLFYAEALRAVCRK... | Function: Involved in the regulation of endocytosis and in several stages of intracellular trafficking . Plays a role in recycling endocytosed transferrin receptor and prevent its degradation . Involved in autophagosome assembly by regulating trafficking and recycling of phospholipid scramblase ATG9A .
Location Topolog... |
Q7SGV1 | MAVIDQDNFSNISWHSEQNAESAASTAQVHHESNSSPEYARSGPDDGRPGDNAAGMEHDELDHSGGEILDCTVSDPHKENDGTKDAYVSYLITTNTTFPSFQKPKTTVRRRFTDFVFLYKVLCRDYQACAVPPLPDKQRMEYVRGDRFGTDFTARRAYSLQRFLARLALHPILRKADILHAFLESPDWNATMRSRSVRGSLASPGGIGDSTLGGSAAAGGGGGVFDTFADSFMNAFTKVHKPDRRFIEIKEKSDKLDEDLNHIEKVVARVARREADIESDLKDLAEQFQKLITLEPGVETAVRAFAASVEDTASGLKKLK... | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), mitophagy, and pexophagy (By similarity).
Location Topolog... |
Q5H7C3 | MSDQFTSIQWDRTEPEGDVPGDSNDHSQVQINSSINLIEEDQGQEQEQDDLVTTNTVVRGGNDSDSNPNEQIPPRDVYIRSKVSQPLKESDGQNFYISYLIETETNEPGLAKTKLKVRRRFSDSNFLYNCLANDFPTSIIPPLPNKQRLEYIKGDRFGEYFTTKRSIALNNFLNRISKHPLLKQAKIYHIFLEDSVNWNTFKQNLKISSNPNSTVGGGSTTSANANGELDSFSDYIMNAFKKPTYESENAKEFQEITDKSNKLQENINKIDKIYQRVVKRQSEISEDFRLFGDEFKKLNQILTEGSDTQFDKELSQQFTS... | Function: Required for glucose-induced micropexophagy and ethanol-induced macropexophagy . Involved in the fusion between the pexophagosome and the vacuole. Also involved in the separation or division of vacuoles throughout the entire life cycle of the cells .
Location Topology: Peripheral membrane protein
Sequence Mas... |
O14243 | MSDSVNLDEPSTNSTHFLQCLVTEPRKELQGSRDTHVSYLIITKTNLSIFTRAECKVRRRFSDFVKLQEILSRMNEDCVVPPLPAKHKLEYIKGGRFSDNFINRRAKLLNRYITRCALHPVLHQSPHFIAFLENPNWNNYVRFFIQPKLNNTSKLDEISDSLLNAFSKLKEEPTEFDIQRDHVQQFMFGISNLEGSIQKLLRLEKALESDYEDVSIQFDRLASLDQALDVPIESIQNALQQTGTEYANLTEKLTLLLDTIKDVESYAHSLKELLKRRDQKQQDVEALQEYSAKLSLERDKISSGGSNGFSLSKTLDDLRG... | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Pe... |
P47057 | MTDKGKNDLTSKAKDKARGNPEKPPYWFEIIVSDPQKRTGDPGSSSGYVSYQISTKTNNTSFYDNRGDPESIIVVHRRYSDLLLLHDILLNRFPTCIIPPLPDKKVFQYIAGDRFSQRFTQKRCHSLQNFLRRVSLHPDLSQSKVFKTFLVSKDWESHRKVLQDSLQPNKDEVTDAFMNAFKTVHKQNEEFTEIREKSDKLDRTVTKIDKLFHKVVKKNDSMSEDYTKLGSNLQELQELVTGENEELAAKLKIFNEGVTQLSYGLQDLTKYLDYEYIVDLKDLEHYIDSMRQLIKLKDQKQIDYEELSDYLTRSIKEKNN... | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells . Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy . Involved in proper ... |
Q3ZBM5 | MAAVPEVLQQQEEDRSKLRSVSVDLNVDPSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGFFKSVVKSADEVLFSGVKEVDDFFEQEKTFLINYYNRIKDSCAKADRMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVESRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYE... | Function: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol lipids. Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi netw... |
Q9Y5X3 | MAAVPELLQQQEEDRSKLRSVSVDLNVDPSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGFFKSVVKSADEVLFTGVKEVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYE... | Function: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) . Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates r... |
Q9UNH6 | MDMNSFSPMMPTSPLSMINQIKFEDEPDLKDLFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVERFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQAWELSSHKKQGPGLLSRMGQTVRAVASSMRGVKNRPEEFMEMNNFIELFSQKINLIDKISQRIYKEEREYFDEMKEYGPIHILWSASEEDLVDTLKDVASCIDRCCKATEKRMSGLSEALLPVVHEYVLYSEMLMGVMKRRDQIQAELDSKVEVLTYKKADTDLLPEEIGKLE... | Function: Involved in the regulation of endocytosis and in several stages of intracellular trafficking . Together with SNX4, involved in autophagosome assembly by regulating trafficking and recycling of phospholipid scramblase ATG9A .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45303
Sequence Len... |
P80566 | MATLKAVCVMKGDAPVEGVIHFQQQGSGPVKVTGKITGLSDGDHGFHVHEFGDNTNGCTSAGAHFNPEGKQHGGPKDADRHVGDLGNVTAKGGVAEVEIEDSVISLTGPHCIIGRTMVVHAKSDDLGRGGDNESKLTGNAGPRLACGVIGIAKC | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15704
Sequence Length: 154
Subcellular Location: Cytoplasm
EC: 1.15.1.1
|
Q96VL0 | MVKAVAVLRGDAKVGGTVVFEQESESAPTTITWDITGNDANAKRGFHIHTFGDNTNGCTSAGPHFNPHGKTHGAPTDEARHVGDLGNLETDGQGNAKGSVKDEHVKLIGPHSVIGRTVVIHAGTDDLGKGDNEESLKTGNAGPRPACGVIGISS | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15839
Sequence Length: 154
Subcellular Location: Cytoplasm
EC: 1.15.1.1
|
Q9C0N4 | MVKAVAVLKGDSPVTGVITFTQEKEGAPVTVSGDIKNLDANAERGFHVHEFGDNTNGCTSAGPHFNPHGKNHGAPSDSERHVGDLGNVKTDGNGVASVNISDKSLSLFGPYSIIGRTIVVHAGTDDFGKGGNAESLKTGNAGARAACGVIGISN | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15637
Sequence Length: 154
Subcellular Location: Cytoplasm
EC: 1.15.1.1
|
J9VLJ9 | MVKAVVVLKGESYVHGTVCFTQESENAPVCITGEIKDMDADAKRGMHVHEFGDNTNGCTSAGPHYNPFKKHHGAPTDSERHVGDLGNIQTNSCGAAQLDFSDKIISLYGPHSIIGRSLVVHASTDDLGKGGNEESLKTGNAGARLACGVIGIST | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems . Destroys radicals produced by host defense mechanisms .
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Location Topology: Peripheral membrane protein
Sequ... |
O73872 | MVNKAVCVLKGTGEVTGTVYFNQEGEKKPVKVTGEITGLTPGKHGFHVHAFGDNTNGCISAGPHFNPHDKTHGGPTDSVRHVGDLGNVTADASGVAKIEIEDAMLTLSGQHSIIGRTMVIHEKEDDLGKGGNEESLKTGNAGGRLACGVIGITQ | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15953
Sequence Length: 154
Subcellular Location: Cytoplasm
EC: 1.15.1.1
|
Q9RU48 | MFRTLTVVPLLALGLSLSACADLGQPTVRADLLDQTGKVTGTATFSPSPIGTRVSIEVSGLKAGPHGLHIHENPNCNPGPDAQGQTIPFGAAGGHFDPGASHNHDGPHARNDQGHGGDLPMITVGEDGKGRLNFDTNRLKMTGPTGVLGRSIVIHADADDYQTNPAGNSGGRERCGVFQAIN | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Location Topology: Lipid-anchor
Sequence Mass (Da): 18787
Sequence Length: 182
Subcellular Location: Cell me... |
P61851 | MVVKAVCVINGDAKGTVFFEQESSGTPVKVSGEVCGLAKGLHGFHVHEFGDNTNGCMSSGPHFNPYGKEHGAPVDENRHLGDLGNIEATGDCPTKVNITDSKITLFGADSIIGRTVVVHADADDLGQGGHELSKSTGNAGARIGCGVIGIAKV | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15699
Sequence Length: 153
Subcellular Location: Cytoplasm
EC: 1.15.1.1
|
P22302 | KFELQPPPYPMDALEPHMSSRTFEFHWGKHHRAYVDNLNKQIDGTELDGKTLEDIILVTYNKGAPLPAFNNAAQAWNHQFFWESMKPNGGGEPSGELLELINRDFGSYDAFVKEFKAAAATQFGSGWAWLAYKPEEKKLALVKTPNAENPLVLGYTPLLTIDVWEHAYYLDFQNRRPDYISIFMEKLVSWEAVSSRLKAATA | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 23042
Sequence Length: 202
Subcellular Location: Plastid
EC: 1.15.1.1
|
Q8YSZ1 | MAFVQEPLPYDFNALEQYGMKGETFEYHYGKHHKAYVDNLNKLTDGTELADKSLEEVIQIAFKDASKAGIFNNAAQVWNHTFFWNSLKPAGGGAPTGEFAAKINQDFGSFDKLKEEFSNAAATQFGSGWAWLIDDGGTLKVTKTPNAENPLAHGQKALLTLDVWEHAYYIDFRNARPAFIKNYLDNLVNWDFAAANYAKA | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22384
Sequence Length: 200
EC: 1.15.1.1
|
P09213 | AFELPALPFAMNALEPHISQETLEYHYGKHHNTYVVKLNGLVEGTELAEKSLEEIIKTSTGGVFNNAAQVWNHTFYWNCLAPNAGGEPTGEVAAAIEKAFGSFAEFKAKFTDSAINNFGSSWTWLVKNANGSLAIVNTSNAGCPITEEGVTPLLTVDLWEHAYYIDYRNLRPSYMDGFWALVNWDFVSKNLAA | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 21342
Sequence Length: 193
EC: 1.15.1.1
|
Q8IAY6 | MVITLPKLKYALNALSPHISEETLNFHYNKHHAGYVNKLNTLIKDTPFAEKSLLDIVKESSGAIFNNAAQIWNHTFYWDSMGPDCGGEPHGEIKEKIQEDFGSFNNFKEQFSNILCGHFGSGWGWLALNNNNKLVILQTHDAGNPIKDNTGIPILTCDIWEHAYYIDYRNDRASYVKAWWNLVNWNFANENLKKAMQK | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22734
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 1.15.1.1
|
P19665 | MTHELISLPYAVDALAPVISKETVEFHHGKHLKTYVDNLNKLIIGTEFENADLNTIVQKSEGGIFNNAGQTLNHNLYFTQFRPGKGGAPKGKLGEAIDKQFGSFEKFKEEFNTAGTTLFGSGWVWLASDANGKLSIEKEPNAGNPVRKGLNPLLGFDVWEHAYYLTYQNRRADHLKDLWSIVDWDIVESRY | Cofactor: Binds 1 Mn(2+) or Fe(3+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal i... |
P09223 | MAFELPPLPYAHDALQPHISKETLEFHHDKHHNTYVVNLNNLVPGTEFEGKTLEEIVKTSSGGIFNNAAQVWNHTFYWNCLAPNAGGQPTGALADAINAAFGSFDKFKEEFTKTSVGTFGSGWGWLVKKADGSLALASTIGAGCPLTSGDTPLLTCDVWEHAYYIDYRNLRPKYVEAFWNLVNWAFVAEQFEGKTFKA | Cofactor: Binds 1 Fe (3+) cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 21935
Sequence Length: 198
EC: 1.15.1.1
|
Q9XD74 | MAFELPNLPYDYDALAPYMSRETLEYHHDKHHLAYVTNGNKLAEEAGLSDLSLEDIVKKSYGTNQPLFNNAGQHYNHVHFWKWMKKGGGGTSLPGKLDAAIKSDLGGYDKFRADFSAAGAGQFGSGWAWLSVKNGKLEISKTPNGENPLVHGATPILGVDVWEHSYYIDYRNARPKYLEAFVDNLINWDYVLELYEAAAK | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22430
Sequence Length: 200
EC: 1.15.1.1
|
O30970 | MAFELPALPYAHDALASLGMSKETLEYHHDLHHKAYVDNGNKLIAGTEWEGKSVEEIVKGTYCAGAVAQSGIFNNASQHWNHAQFWEMMGPGEDKKMPGALEKALVESFGSVAKFKEDFAAAGAGQFGSGWAWLVKDSDGALKITKTENGVNPLCFGQTALLGCDVWEHSYYIDFRNKRPAYLTNFLDKLVNWENVASRM | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22122
Sequence Length: 200
EC: 1.15.1.1
|
P53652 | MPHALPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTPYAEQPVESLLRQLAGLPEKLRTPVVNNGGGHANHSLFWTVMSPQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTPQGSLLVESSGNQDSPLMNGNTPILGLDVWEHAYYLKYQNRRPEYIGAFYNVIDWREVARRYAQALA | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (Probable). Partially complements double sodA-sodB deletions in E.coli .
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da):... |
P77929 | MPHTLPALPYAYDALEPHIDAQTMEIHHTKHHQTYVNGLNAAIEGTEWAEWPVEKLVGAVKQLPESLRGAVTNHGGGHANHSLFWTVMSPQGGGEPHGQLAQAIASQLGGFDAFKEAFTKAALTRFGSGWAWLSVTPQKTLVVESSGNQDSPLMFGNTPIFGLDVWEHAYYLKYQNRRPEYIGAFYNVIDWAEVERRYLEALK | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22613
Sequence Length: 203
EC: 1.15.1.1
|
P22799 | MAYELPQLPYAYDALEPHIDAKTXEIHHSKHHNTYVTNLNAAVEGTEFADKDINDLIAMLDALPADKQTAVRNNGGGHANHTLFWEVIAPGGSNTPVGEVAKAIDAKFGSFDAFKEEFAKAATTRFGSGWAWLIVDGDSVAVTSTPNQDSPVMEGKTPVLGLDVWEHAYY | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 18468
Sequence Length: 170
EC: 1.15.1.1
|
P07895 | MLCRAACSAGRRLGPAASTAGSRHKHSLPDLPYDYGALEPHINAQIMQLHHSKHHATYVNNLNVTEEKYHEALAKGDVTTQVALQPALKFNGGGHINHSIFWTNLSPKGGGEPKGELLEAIKRDFGSFEKFKEKLTAVSVGVQGSGWGWLGFNKEQGRLQIAACSNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVSQRYIVCKK | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
PTM: Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity.
Catalytic Activity: 2 H(+) + 2 superoxide... |
Q9UQX0 | MLRFLSKNSVAAIRNVSIARGVHTKATLPPLPYAYNALEPALSETIMKLHHDKHHQTYVNNLNAAQEKLADPNLDLEGEVALQAAIKFNGGGHINHSLFWKILAPQKEGGGKPVTSGSLHKAITSKWGSLEDFQKEMNAALASIQGSGWAWLIVDKDGSLRITTTANQDTIVKSKPIIGIDAWEHAYYPQYENRKAEYFKAIWNVINWKEAESRYSNR | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 24347
Sequence Length: 218
Subcellular Location: Mitochondrion matrix
E... |
P29082 | MPKPYVAINMAELKNEPKTFEMFASVGPKVCMVTARHPGFVGFQNHIQIGILPFGNRYGGAKMDMTKESSTVRVLQYTFWKDWKDHEEMHRQNWSYLFRLCYSCASQMIWGPWEPIYEIIYANMPINTEMTDFTAVVGKKFAEGKPLDIPVISQPYGKRVVAFAEHSVIPGKEKQFEDAIVRTLEMLKKAPGFLGAMVLKEIGVSGIGSMQFGAKGFHQVLENPGSLEPDPNNVMYSVPEAKNTPQQYIVHVEWANTDALMFGMGRVLLYPELRQVHDEVLDTLVYGPYIRILNPMMEGTFWREYLNEQ | Cofactor: Binds 1 Fe cation per subunit.
Function: Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products.
Catalytic Activity: 4 H2O + O2 + 4 sulfur = 6 H(+) + 2 hydrogen sulfide + 2 sulfite
Sequence Mass (Da): 35318
Sequence Lengt... |
O29903 | MELFQTADWKKEKHVPVIEVLRAEGGVVEVKVSVGKEIPHPNTTEHHIAWIELVFQPEGSKFPYVVGRAEFAAHGASVDGPNTSGVYTDPVAVFAFKAEKSGKLTAFSYCNIHGLWMGEATLSLE | Function: Uses electrons from reduced NADP, by way of rubredoxin and an oxidoreductase, to catalyze the reduction of superoxide to hydrogen peroxide.
Catalytic Activity: 2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized [rubredoxin]
Sequence Mass (Da): 13696
Sequence Length: 125
EC: 1.15.1.2
|
Q58151 | MTHYCGINRMKEGTDFEKKHTPFIECKDRVKANDYFEVKISTGIPHPMEDNHFIHWIELYMGDLYLARVDFTQFMKPEVKLMVKAPSKEHEKFILRALMRCNLHGVWEYEKEILLE | Function: Uses electrons from reduced NADP, by way of rubredoxin and an oxidoreductase, to catalyze the reduction of superoxide to hydrogen peroxide.
Catalytic Activity: 2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized [rubredoxin]
Sequence Mass (Da): 13950
Sequence Length: 116
EC: 1.15.1.2
|
P82385 | MISETIRSGDWKGEKHVPVIEYEREGELVKVKVQVGKEIPHPNTTEHHIRYIELYFLPEGENFVYQVGRVEFTAHGESVNGPNTSDVYTEPIAYFVLKTKKKGKLYALSYCNIHGLWENEVTLE | Function: Uses electrons from reduced NADP, by way of rubredoxin and an oxidoreductase, to catalyze the reduction of superoxide to hydrogen peroxide.
Catalytic Activity: 2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized [rubredoxin]
Sequence Mass (Da): 14324
Sequence Length: 124
EC: 1.15.1.2
|
O58810 | MLKETIRSGDWKGEKHVPVIEYEREGDLVKVEVSVGKEIPHPNTPEHHIAWIELYFHPEGGQFPILVGRVEFTNHSDPLTEPRAVFFFKTSKKGKLYALSYCNIHGLWENEVQLE | Function: Uses electrons from reduced NADP, by way of rubredoxin and an oxidoreductase, to catalyze the reduction of superoxide to hydrogen peroxide.
Catalytic Activity: 2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized [rubredoxin]
Sequence Mass (Da): 13326
Sequence Length: 115
EC: 1.15.1.2
|
Q9WZC6 | MKLSDFIKTEDFKKEKHVPVIEAPEKVKKDEKVQIVVTVGKEIPHPNTTEHHIRWIKVFFQPDGDPYVYEVGRYEFNAHGESVQGPNIGAVYTEPTVTTVVKLNRSGTIIALSYCNIHGLWESSQKITVEE | Function: Uses electrons from reduced NADP, by way of rubredoxin and an oxidoreductase, to catalyze the reduction of superoxide to hydrogen peroxide.
Catalytic Activity: 2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized [rubredoxin]
Sequence Mass (Da): 14935
Sequence Length: 131
EC: 1.15.1.2
|
Q9BQ15 | MTTETFVKDIKPGLKNLNLIFIVLETGRVTKTKDGHEVRTCKVADKTGSINISVWDDVGNLIQPGDIIRLTKGYASVFKGCLTLYTGRGGDLQKIGEFCMVYSEVPNFSEPNPEYSTQQAPNKAVQNDSNPSASQPTTGPSAASPASENQNGNGLSAPPGPGGGPHPPHTPSHPPSTRITRSQPNHTPAGPPGPSSNPVSNGKETRRSSKR | Function: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint . In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA ... |
Q8R2Y9 | MTTETFVKDIKPGLKNLNLIFIVLETGRVTKTKDGHEVRTCKVADKTGSINISVWDDVGNLIQPGDIIRLTKGYASVFKGCLTLYTGRGGDLQKIGEFCMVYSEVPNFSEPNPEYNTQQAPNKSVQNNDNSPTAPQATTGPPAASPASENQNGNGLSTQLGPVGGPHPSHTPSHPPSTRITRSQPNHTPSGPPGPSSNPVSNGKETRRSSKR | Function: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA l... |
Q9SJA7 | MEYSDDGRFDVIVVGAGVMGSSAAYQLAKRGQKTLLLEQFDFLHHRGSSHGESRTIRATYPEDYYYSMVSESTRLWAAAQSEIGYKVHFPTQQFDMGPADQQSLLSVVATCQKHGLAHRVMDSHAVSEHFSGRISIPENWIGVSTELGGIIKPTKAVSMFQTLAIGHGAILRDNTKVANIKRDGESGEGVIVCTVKGDKFYGKKCIVTAGAWISKLVKTVAGIDFPVEPLETTVCYWRIKEGHEEKFTIDGEFPTFASYGAPYVYGTPSLEYPGLIKVAVHGGYWCDPDKRPWGPGVKLEELKEWIKERFGGMVDSEGPV... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H2O + O2 + sarcosine = formaldehyde + glycine + H2O2
Sequence Mass (Da): 45702
Sequence Length: 416
EC: 1.5.3.1
|
Q29RU9 | MAAQRELYDAIVIGAGIQGCFTAYHLAKHSKKVLLLEQFFLPHSRGSSHGQSRIIRRAYPEDFYTQMMAECYSLWAQLEHEAGTQLYRQTGLLLLGMKENPELKIIQATLSRQGVEHQCLSSEELKQRFPNIRLARGEVGLLEVSGGVLYADKALRALQDAIRQLGGIVHDGEKVVEIKSGLPVMVKTTSRSYQAKSLIITAGPWTNRLLRPLGAELPLQTLRINVCYWQEKVPGSYSVSQAFPCFMGLGLSLAPHHIYGLPSREYPGLMKVCYHHGNNADPEERDCPAAFSDIQDVHILSGFVRDHLPDLQPEPAVMEH... | Cofactor: Binds 1 FAD per subunit.
Function: Metabolizes sarcosine, L-pipecolic acid and L-proline.
Catalytic Activity: H2O + O2 + sarcosine = formaldehyde + glycine + H2O2
Sequence Mass (Da): 43820
Sequence Length: 392
Subcellular Location: Peroxisome
EC: 1.5.3.1
|
Q18006 | MSTDYDVVVVGAGIFGSCTAYNCQKIGLKTLLLEQFELGHKNGSSHGKSRITRYAHTEVEYVDLVGDAYNQIFELERIRGEKLWKKTGLLWVSTGNEVEKIHTNLKLKGIKHEVIKGTEVGKRYPQFKFDDSWNGLIDPMGGVIYADKWLNAFRDEFKKIGGIIHDREIVLSHSEISNNLFVTTNKSRYSSKKIIFTVGCWITKFLPDLKFNIEPISISVCYWKTKNESDSHLLNEDHYPVVIAQEMDLQVFHYSLPDTDYPGSMKFCYHFGDALTQDLAHPAQRSQRCIDLPAKFIQKYMPVVDGSAPTRIDKCIYTNS... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H2O + O2 + sarcosine = formaldehyde + glycine + H2O2
Sequence Mass (Da): 43123
Sequence Length: 384
EC: 1.5.3.1
|
Q9P0Z9 | MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYLEDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCLSSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINPGLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVSQAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSSFVRDHLPDLKPEPAVIESCM... | Cofactor: Binds 1 FAD per subunit.
Function: Metabolizes sarcosine and L-pipecolic acid.
Catalytic Activity: H2O + O2 + sarcosine = formaldehyde + glycine + H2O2
Sequence Mass (Da): 44066
Sequence Length: 390
Subcellular Location: Peroxisome
EC: 1.5.3.1
|
Q10721 | AYTGQTGAPWGLA | Function: Serine protease. Degrades fibrinogen.
PTM: Not glycosylated.
Sequence Mass (Da): 1292
Sequence Length: 13
Subcellular Location: Secreted
EC: 3.4.21.-
|
P52928 | MEKIKVCLVDDNKELVSMLESYVAAQDDMEVIGTAYNGQECLNLLKDKQPDVLVLDIIMPHLDGLAVLEKMRHIERLRQPSVIMLTAFGQEDVTKKAVDLGASYFILKPFDMENLTSHIRQVSGKANATIKRPLPSFRSATTVDGKPKNLDASITSIIHEIGVPAHIKGYMYLREAISMVYNDIELLGSITKVLYPDIAKKYNTTASRVERAIRHAIEVAWSRGNIDSISSLFGYTVSMSKAKPTNSEFIAMVADKLRLEHKAS | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of s... |
P52930 | LAVLEKMRHIERLKQPSVIMLTAFGQEDVTKKAVDLGASYFILKPFDMENLPSHIRQVSGKANTMIKRPLPSFRSATTVDGKPKNLDASITSIIHEIGVPAHIKGYMYLREAISMVYNDIELLGSITKVLYPDIAKKYNTTASRVERAIR | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of s... |
P52933 | LAVLERLRENNEMTKQPSVIMLTAFGQEDVTKKAVDLGASYFILKPFDMENLVGHIRQVSGNGTQVTHRSSSIQNSVLRNKPPEPKRKNLDASITTIIHEIGVPAHIKGYLYLREAISMVYNDIELLGSITKVLYPDIAKKFNTTASRVERAIRHAIEVAWSRGNIDSISSLFGYTVSMSKAKPTNSEFIA | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of s... |
P06534 | MEKIKVCVADDNRELVSLLSEYIEGQEDMEVIGVAYNGQECLSLFKEKDPDVLVLDIIMPHLDGLAVLERLRESDLKKQPNVIMLTAFGQEDVTKKAVDLGASYFILKPFDMENLVGHIRQVSGNASSVTHRAPSSQSSIIRSSQPEPKKKNLDASITSIIHEIGVPAHIKGYLYLREAISMVYNDIELLGSITKVLYPDIAKKFNTTASRVERAIRHAIEVAWSRGNIDSISSLFGYTVSMTKAKPTNSEFIAMVADKLRLEHKAS | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of s... |
P10728 | MKNEMHLEFSALSQNESFARVTVASFIAQLDPTMDELTEIKTVVSEAVTNAIIHGYEENCEGKVYISVTLEDHVVYMTIRDEGLGITDLEEARQPLFTTKPELERSGMGFTIMENFMDDVSIDSSPEMGTTIRLTKHLSKSKALCN | Function: Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
Catalytic Activity: ATP + L-sery... |
Q8RAA8 | MEYNNMMELKFLSKSQNESFARTVVAAFAAQLDPTIEEIADIKTAVSEAVTNCIIHAYENKIGIITIRAFILDNKITIEVIDEGKGIEDVEKAMQPLFTTRLEEERAGMGFTVMQTFMDELEVESTPGKGTLVRMTKYIGRNR | Function: Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
Catalytic Activity: ATP + L-sery... |
Q97GQ9 | MLENKMELKFLAKSENESFARVTVASFASELDPTLEEIDDVKMAVSEAVTNAIIHGYENKGGVVTICAVIEDRELTIEVMDEGIGIENIEKAMEPLYTSRPDLERSGMGFTVMESFMDNIKVESEKGKGTKIIMKKKFALIED | Function: Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
Catalytic Activity: ATP + L-sery... |
P41028 | MKNGWTNFVIGTVRIRIVGKGIERFLNNCVRQQIMISNVHKVDGQLATATILLKDVKKIRILIRNADCKIYFIRGRGFPFLTKRVIKNSGFALGFLSFFIILGLLSNMVWKVEISGAEPQTEHQMTKQLAKIGVKRGEFQFLLESPEKIQRYLTDNMNNITWVGVEVRGTSYHFQVVEKNEPKPQQKTPYQHLIAKKKAIITNLFVEKGQPLVKVNDFVNEGEVLVSGIIGNEKNKKVVAAKGKVYGETWYKSEVEVPLKTDFQVLTGNGYTKHYLDFQAFKMPLWAFNKEKYTSKVTEKVEHPLYFFKWKLPLSYEKVA... | Function: May have a role in completing stage IV of sporulation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45378
Sequence Length: 395
Subcellular Location: Membrane
|
Q00758 | MAKQTFLKGTLILIAAGMVTRMLGFVNRVVIARFIGEEGVGLYMMAAPTFFLATTLTQFGLPVAISKLVAEASARGDHQKTKNILVMSLTITGVLSLIFTPLFLFFAPVMAETMLTDKRTLYPLLAITPVVPIIAISSVLRGYFQGKQNMNPLAMSQVLEQVVRISLVAVCTTIFLPYGIEYAAAGAMLSSVAGELASLLYLFVCFKYKKTIKIRKHFLQSIKNGKQTFTQLMSVSLPTTGSRFIGNLSWFFEPIVVAQSLAIAGVATVAATKQYGELTGFAMTLLTLPSFITYSLSTALVPAISEGMEQKKLQVVEYRL... | Function: Involved, directly or indirectly, in spore cortex biosynthesis. Affects only indirectly the expression of late sporulation genes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56079
Sequence Length: 518
Subcellular Location: Cell membrane
|
Q03524 | MRVSNVTVRKRLLFVLLFGVIVFLIIDTRLGYVQFVMGEKLTSLAKDSWSRNLPFEPERGEILDRNGVKLATNKSAPTVFVVPRQVQNPMKTSKQLAAVLNMSEEKVYKHVTKKASIEKITPEGRKISNEKAKEIKALDLKGVYVAEDSIRHYPFGSFLSHVLGFAGIDNQGLLGLEAYYDDDLKGEKGSVKFYTDAKGKKMPDEADDYTPPKDGLDMKLTVDSKVQTIMERELDNAEAKYHPDGMIAVAMNPKNGEILGMSSRPDFDPADYQSVDPSVYNRNLPVWSTYEPGSTFKIITLAAALEEQKVNLKRDQFYDK... | Function: Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Spore cortex formation is determined primarily by the mother cell.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. A... |
P07373 | MTTKKTSPDLLLVIITLLLLTIGLIMVYSASAVWADYKFDDSFFFAKRQLLFAGIGVIAMFFIMNVDYWTWRTWSKLLMVICFFLLVLVLIPGVGMVRNGSRSWIGVGAFSIQPSEFMKLAMIAFLAKFLSEKQKNITSFRRGFVPALGIVFSAFLIIMCQPDLGTGTVMVGTCIVMIFVAGARIAHFVFLGLIGLSGFVGLVLSAPYRIKRITSYLNPWEDPLGSGFQIIQSLYAVGPGGLFGMGLGQSRQKFFYLPEPQTDFIFAILSEELGFIGGTLILLLFSVLLWRGIRIALGAPDLYGSFVAVGIISMIAIQVM... | Function: May play an essential role not only during sporulation, but also during vegetative growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40132
Sequence Length: 366
Subcellular Location: Cell membrane
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.