entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
|
|---|---|---|---|---|
O13915
|
USB1_SCHPO
|
U6 snRNA phosphodiesterase 1 (3'-5' RNA exonuclease USB1) (EC 4.6.1.-) (Mutated in Poikiloderma with Neutropenia protein 1)
|
MSLVCYESSSSGEDDDETISDNPRMLKVPKLQESFHELYKKKPKTFDSPEFHEGRIRGQKHIEGLWFVQTYLEVDLSKKVKKGIREFLNSQSRFQSLLCSEHNVPRRLHLSISENYRINYSTKNQLVHKWEQYTNNLNYRTLKFRLGKMCLLFNDEKTRMFLAFECKFSDENYKDLISHASDCMKEFTNRNLREDFLLHISFASSLTNEDEYQNWVSQDRESHFFKTMNEIINTKIQKDQFSESFIVDSLKLSIGHLIFTFPFCK
|
3'-5' RNA exonuclease that trims the 3' end of oligo(U) tracts of the pre-U6 small nuclear RNA (snRNA) molecule, leading to the formation of a U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate.d. Participates in the U6 snRNA 3' end processing that prevents U6 snRNA degradation.
|
O13917
|
HPRT_SCHPO
|
Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (HGPRTase) (EC 2.4.2.8)
|
MDPVRLYYSYNDIHKMCAQQAEKILETFRPDVIIAIGGGGFIPARILRTFLKKKGSKNIPIQAIGLSLYEELVSDSPEEVPGLEVKRTQWLDFSTLGMVDLVGKNILIVDEVDDTRTTLHYALRELQRDVAEQAKKLNREGEKTTFGIFVVHNKVKPKNAQLDKEILDKYYFTGCNTPDCWIMYPWEAQDIEEHDSHVAKMGDLKP
|
Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity).
|
O13918
|
ZHF1_SCHPO
|
Zinc homeostasis factor 1
|
MFDLARQTRIILLLGIDVTFFFIEIITGYAIDSLALIADSFHMLNDIVSLLVALWATRLAHSTSHEPKYTYGWQRAEILGALSNGVFLIALCMFIFMEAIERFIEPPSVSNPTLMFFVGSLGLLSNFVGIFLFHDHGHDHPHTHTAQNYDFPEEDDIESVLPSTIVHRCNTSQQEVSHTHTQVADSATESSPLLSYTGNHNGAGTSKPVNNHGSIEQDAPKQTKKRNLNMHGVFLHVLGDALGNIGVISAALFIKYTDYSWRFLFDPCISILLTFIILFSAIPLCKSAALILLQVAPQSIKLDDVSNLINHLDGVESVHELHIWQLSDVKLIATVHVCVTLPDDKGESYTKLTTDIRNVLQSFGIYDVTIQPEFANHPLLCDQGSSS
|
Involved in zinc homeostasis, where it plays a role in its accumulation in the endoplasmic reticulum/nucleus. Also has a role in the sequestration of cadmium into the endoplasmic reticulum.
|
O13919
|
PST2_SCHPO
|
Paired amphipathic helix protein pst2 (SIN3 homolog 2)
|
MEQTLAILKNDNSTLVAEMQNQLVHDFSPNGTALPELDIKAFVQKLGQRLCHRPYVYSAFMDVVKALHNEIVDFPGFIERISVILRDYPDLLEYLNIFLPSSYKYLLSNSGANFTLQFTTPSGPVSTPSTYVATYNDLPCTYHRAIGFVSRVRRALLSNPEQFFKLQDSLRKFKNSECSLSELQTIVTSLLAEHPSLAHEFHNFLPSSIFFGSKPPLGSFPLRGIQSSQFTLSNISDLLSQSRPDNLSPFSHLSNESSDFFKNVKNVLTDVETYHEFLKLLNLYVQGIIDRNILVSRGFGFLKSNSGLWRSFLSLTSLSPEEFLSVYNSACSDFPECGPSYRLLPVEERNISCSGRDDFAWGILNDDWVSHPTWASEESGFIVQRKTPYEEAMTKLEEERYEFDRHIEATSWTIKSLKKIQNRINELPEEERETYTLEEGLGLPSKSIYKKTIKLVYTSEHAEEMFKALERMPCLTLPLVISRLEEKNEEWKSVKRSLQPGWRSIEFKNYDKSLDSQCVYFKARDKKNVSSKFLLAEADILRSQAKLHFPLRSRSAFEFSFVYDNEIVLFDTCYMVCTYIVCNSPSGLKKVEHFFKNILPLHFGLEKDKFSIFLDQVFRGPDYDVNAPNIVGNKPVRRKRSNSITQLTEFVKQPKINGQRESRSAAAARKKEESGNKSQSNSQNSLSDESGNVTPVSKKQLSQPAAAIKASLKYPSHPDSLLEHQDHAGDTENEMHDDVDKEQFGYSSMYVFFRLFNLLYERLYELQRLEDQVSIIQQRIIPNPVSQKQKIWRDRWNDLSDVPDEKTHYENTYVMILRLIYGIVDQSAFEDYLRFYYGNKAYKIYTIDKLVWSAAKQVHHIVSDGKYKFVTSLVEQNSSASPKKNYDDFLYRLEIEKLLNPDEILFRFCWINKFKSFGIKIMKRANLIVDQSLDTQRRVWKKYVQNYRIQKLTEEISYKNYRCPFLCRNIEKERTVEQLVSRLQTKLLRSAELVSGLQAKLCLDSFKLLYLPRTEDSYIDASYLRLRDTDFLDCQNKRKQRWRNRWESLLKSVRGTSDNTAEVNFDADINALFIP
|
Has a role in chromatin assembly and chromosome segregation. Involved in the deacetylation of histones.
|
O13924
|
HASP_SCHPO
|
Serine/threonine-protein kinase haspin homolog hrk1 (EC 2.7.11.1)
|
MESRSKVKTYGKNRRYINKDIEIWASLDERPCALKPRNIENFNNQERSDLEHIHSKPKKDSLLSWNILLKKGSYKENELLAKRNQNLVPTVIIPASPRDNASKSVVSKKEVVNLSSSVALSGKPANNSKLDPLHRLLQIVAQEDALPFSQFVKSQTFEIQKIGEASYSEVYQASNADDVPVVWKVIPFGEDGQAQYADVLNEVQISQWIKVDGFANLHQVVVVKGTYPSLLLEEWDRYLMQNGSENDRPDSYSSTQLYCVLCLDHSGTDLEHFELRSWRECWSVFYETLKILSLVETRYEFEHRDLHWGNILIRKADRSEEEVSFLLNEISLDDIESVDFPGSQDKADDFDNILQVTLIDFTLARASYSQGIISYNEFNDPDLFNGVDDYQFDIYRLMSRVTKGRWAQFFPITNVLWLHYLIHQLLHKKNLSSPLTETETLMRSRLKQIFRLIDPVKTMQFQQAEDSIRSKSTVTSATSLLNWVRQKY
|
Serine/threonine haspin-like protein kinase involved in cell cycle regulation. Acts in chromosomal passenger complex (CPC) targeting to centromeres by phosphorylating histone H3 at 'Thr3' (H3T3ph).
|
O13928
|
RHO3_SCHPO
|
GTP-binding protein rho3
|
MSSCFGSKKKPIYRKIVILGDGAAGKTSLLNVFTKGYFPQVYEPTIFENYIHDIFVDGNSIELSLWDTAGQEEYDQLRSLSYSDTHVIMICFAVDSRDSLENVITKWLPEVSSNCPGVKLVLVALKCDLRGADEEQVDHSKIIDYEEGLAAAKKINAVRYLECSAKLNRGVNEAFTEAARVALAAQPRGTKDGADESHGTGCIIA
|
Involved in controlling cell shape and septation. Regulates cell separation by modulating the function of the exocyst complex. Involved in post-Golgi vesicle transport. Involved in driving sexual development in a palmitoylation-dependent manner.
|
O13935
|
TRM4B_SCHPO
|
Multisite-specific tRNA:(cytosine-C(5))-methyltransferase trm4b (EC 2.1.1.-) (tRNA (cytosine-5-)-methyltransferase trm4b)
|
MGKRNKKVTQGKRAYNDKSEIVLENKQFEGYYKKQNLFRGKPNDEFDSFMEYMRKPLPTTFRICGYRHHAFELKNHFEKYYVPSLKNVVHEGQTIPPPTVLPWYPDGLAYIVDAQKDVIRKSPPLKRLQRFLVSENEAGNINRQEAVSMLPPLFLDVEPHHVILDMCAAPGSKTAQLIEAVYKKANIKDAAHDSKNLKSVEGLVIANDADPKRAQMLVHQINRLNSPNILVVNHDASTMPNIYVKGSSPSDGLNVIEEKKILKFDRILADVPCSGDGTFRKNLSLWREWSANSAFSLHPLQLRILIRGLQLLKVGGCLVYSTCSINPIENEAVVTAALKATGGAVSLVDVSKKLPLLKRDPGLLSWKVLDDSLNEFQSPAENTNDKIELTESMWPLPEEEMSKLHIERCARLYPHMQNTGGFFVAVLQKTDPINSRSFDPKKYTASMEILPPENKRQRTEKGVDEASNSTLTKSGNSYFDEEPFVYINPDDTSIKTIVDFYGIDPSFPRDQFFVRNQSGIPVRSIYFACSLFKEIIEANTNRVKFVHGGVRFFVKQEISQLLKDFSLKANKDICNFRIHSNGVNIISPFLNEKHFYDAGLKDLKILVKNEYPHVEQFSESGMLKKEFEKMPLGCNILRVDAQTKDGALMDMLILQPIWRSPTSCNLMLARKEKQNLSLELFGMDV
|
tRNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in tRNAs at position 49 and 50. Trm4a and trm4b methylate different sets of tRNAs. Also methylates cytosine to m5C at positions (60, 61 and 62) in tRNA(Asp).
|
O13936
|
SPT5_SCHPO
|
Transcription elongation factor spt5 (Chromatin elongation factor spt5)
|
MDTNSPKSIDKDANSTEVDAAEQDAASVKINSTRASPNGSDLLNDDSEAAKITTNEKQSSPVDSHNESPNDTTINKGEDGNENEVDNVNNNDKKEDEDNVEENEEEADANEEEEEDEEDDEEDEEDEDESGGGRRKRARHDRRNQFLDIEAEVDEDEEELEDEEDEIGREDGFIEEEVGADYVGDDRRHRELDRQRQELQSVDAERLAEEYREKYGRSQTVVGDTSNVPQRLLLPSVNDPNIWAVRCKIGKEKDIVFTIMRKAMDLQYTSSPLEIISAFQRDSLVGYIYVEARKQSHVLDALNGVLNVYTNNMILVPIKEMPDLLKVQKQVVELLPGAYVRIRRGKYAGDLAQVDNLSENGLTARVRIVPRIDYSDGLKRKNSATRPQARLFNESEAFKSNPSKFSKRGPRLFLFNNEEFEDGFLVKDIRISSLITEGVNPTLDEVSKFNPNNEDLDLSSLALSVKGGHAEFQPGDHVEVYVGEQTGVSGVVENVRGSVITMVSSDGLRLDVPSRGLRKRFRHGDYVKVIAGKYKDDTGMVVRISKDEVTFLSDTLMTELTVFSRDLGEASSAQAVNSAYELHDLVQLDVNTVACIFSVDRDTYKVIDQNGGVRTVLASQITMRHSNRRGVATDRNGAEIRIGDKVKEVGGEGKQGTILHIYRAFVFLHNRDIAENNGVFSARSRNVATIAAKGARISADLTKMNPALSNGPALPPVANLKRTIGRDKAIGATVRIRRGPMKGLLGVIKDTTDANARVELHTGNKMVTIPKENLLYTTKTGELISYTEFIERSRGIRPGSISTADGPNVPNWAQGARTPAVANGSRTPAWNTGSRTPAWNSGSKTPAWNSGSRTPAWNSGNKTPAWNAGSRTPAWNSGNKTPAWNVGNKTPAWNSGAKTPAWNAGNKTPSWNNGTKTPAWNANQTPMVANGTNTSWGQTPAYGGFSETNWDTEDNSKPYTAPTPGAWAAPTPGGWDDEEGDSPKYVPPSP
|
The spt4-spt5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene (By similarity). {ECO:0000250, ECO:0000269|PubMed:11893740}.
|
O13953
|
EAF3_SCHPO
|
Chromatin modification-related protein eaf3 (Altered polarity protein 13) (ESA1-associated factor 3)
|
MAVSYKVNERVLCFHGPLLYEAKIVDTEMKGDVTTYLIHYKGWKNSWDEWVEQDRILQWTEENLKTQKELKNAAISTRQKPTSKKSASSTSKHDSTGVKTSGKRSRESSTVTVDGDSHELPSRIKTQKSESPIPQQVKRDGTTDAKNEETTKPENNEKDDFEEEPPLPKHKISVPDVLKLWLVDDWENITKNQQLIAIPRNPTVRAAIAAFRESKISHLNNEIDVDVFEQAMAGLVIYFNKCLGNMLLYRFERQQYLEIRQQYPDTEMCDLYGVEHLIRLFVSLPELIDRTNMDSQSIECLLNYIEEFLKYLVLHKDEYFIKEYQNAPPNYRSLVGV
|
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity). Also involved in deacetylation of histones, chromatin assembly and chromosome segregation. May act as a transcriptional oscillator, directing histone deacetylases to specific chromosomal domains. {ECO:0000250, ECO:0000269|PubMed:12773392}.
|
O13958
|
SSN3_SCHPO
|
Serine/threonine-protein kinase srb10 (EC 2.7.11.22) (EC 2.7.11.23) (Cyclin-dependent kinase 8) (Suppressor of RNA polymerase B srb10)
|
MKDGYKIIGFISSGTYGKVYKAVSSNSNDKRLFAIKKFKAESKQVSSNAQQTGVSQSAIREMMLCREIQHENIVSLVQVLLKDGTISMVFEYAEHDLLQIIHFHSRSRTRQIPPSILKSILWQIINGVAYLHENWIMHRDLKPANIMITATGKVKIGDLGLGRLIRDPILPFYSSDRVVVTIWYRAPELLLGAHDYTPAIDVWAIGCIYGEMLALSPLFKGDEIKMEDKKVVPFQSTQMLRIMELLGTPTEERWPGLKNYPEYYQLSSFEVRYWNNLLPQWYQTVKNRDPQGLDLLMKMLQYDPKSRITAKQALEHVFFTSDKLWTTSPFLNQPIHYPERRISEDDSEVSSKRVLSTSLRSESKRFKGN
|
Catalytic component of the Cdk8 module/Srb8-11 module which is a regulatory module of the Mediator complex that regulates basal RNA polymerase II transcription. The Cdk8 module may sterically hinder the interaction between Mediator and RNA polymerase II leading to transcriptional repression of a subset of genes regulated by Mediator.
|
O13959
|
RBX1_SCHPO
|
RING-box protein pip1 (RING-box protein 1) (Pop-interacting protein 1)
|
MEDEMQIDKKEVEIEQKPPRFEIKKWNAVALWQWDIVVDNCAICRNHIMDLCIECQANTDSAAAQECTVAWGTCNHAFHFHCISRWLNTRNVCPLDNREWEFQRYGH
|
Component of E3 ubiquitin ligase SCF complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recruit the E2 ubiquitination enzyme, like UBC3/CDC34, to the complex and brings it into close proximity to the substrate. Component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.
|
O13961
|
NDC1_SCHPO
|
Nuclear envelope protein ndc1 (Cell untimely torn protein 11)
|
MVMLRTSFPSGSRTKAVRYHTLLRPILQQRFLRACFALLCLCCITSYWFSSGPFISLSFWFLSLVRGFVCFFFMFPYFVMLKSRMSTQKVTKQSLGAQLFYDFSPKSFFLVYLTFAVSVSCLCLFYIKGHASSIRLQWIASPNAYELPSLNERFVYMTYFSHILILALTVEHLYLQRDSPSRPVINVSFFNYIFQNLGWLIRFSFRKSIICCLFTPFSYAILRSYIWRFAALLTSCCRRIAYTKTPPKWPLSLRLLLHSFWMAFIVCLTFQIALLIFRVFLYSGPMIRGKLLSARSNDPNGTLVDGMKTKKKPLTECIATEELWFIAKRDPQRIKSIFQDIDRSVSIWQELYSITESRCKELATSLKILQSTGDFSAATSKKSGLTKKTNIPYSPNSNHEEINSIPLRNKNIFVPPSQGHSPLLEKIKKQGSLPSTTPVNEGGISDIIPKSLYDQVIRFISTFYKAPVFGIFRKTLRRQNEALLPNPWLFCVTVNSLTQLVLKSLKYDTYGVVARDISSILAVYCDTFDVLVSYKRSLVKNHSNSTNLDDDFKNLNSAANALHCGIIDITEKFQDFFTQLNLSPRIERRCWVLFREYKSNS
|
Component of the nuclear pore complex (NPC) and the spindle pole body (SPB), which plays a key role in de novo assembly and insertion of both structures in the nuclear envelope. Involved in the formation of the bipolar mitotic spindle. Anchors the spindle pole body in the nuclear envelope.
|
O13978
|
AT101_SCHPO
|
Autophagy-related protein 101 (Meiotically up-regulated gene protein 66)
|
MTNTVTIELKIGYKYAAEVVKAVLGVILFHRQFSTVPARTIDVLDITVPTLVGAELNEQLATKAAEFIDTIRNEAGANGQMILLLYERSPKKSWFGKGNTIPWEQWILHTTILEEGDSYQESSLSLEAAVEQIVQAVNLRSLSYLPPVAMDSGNYPYEIVTPTSTEGWGSLLKRMIIENVSGGD
|
Autophagy factor required for autophagosome formation. Component of the atg1 kinase complex in which it stabilizes atg13. Is also responsible for recruiting downstream factors to the autophagosome-formation site. Has a role in meiosis and sporulation.
|
O13983
|
HRQ1_SCHPO
|
ATP-dependent helicase hrq1 (EC 3.6.4.12) (Homologous to recQ protein 1)
|
MSQTPIKKEESNDQDDKFEFKKYINEGKLPLKADNPKKKPQLGTIQANQPIPSIFDNLFNLFKVINTTYTFLYLRNSLTITFPLLNSSVKQSLKKELTIGDLSQLREICPQIIELNYKSLASLALEINKNVYTDLNPELYTGSTVSQSSEYVLVIELLETQERSSKRRRREGPTMKANIQRQKLDFNNLKKAIELRNQKFLQGIKEYIKKCQLTELDPTQQLLTQSRKNQPVPPDSPSIPNDSIENCNLNTKACSIEELLNEIASESSYEGQIVQEALHTYPAVEAQYGALSRPLSQELINALYTSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSYMPTLKNIRVDTFDGDTPLESRESIIRSANIIFTNPDMLHQTILPNANRWYYFFKNLKLFVLDEAHVYNGIFGVHVAFVLRRMRRIAEYFGNSQYRFVSCSATIEDPLQHMKKIFGVDNIKLINYTSSPSGSKKFVMWNPPYVDPKHPDDGKKSAISEASKLLIKFAEKRVRTIVFCRVRKTCESLMRLVRQELKTKQKGDLLSKIQSYRAGYTVQERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRNKSSLAVYIVETFPVDQFYLKHPILIHTQPNAELTLDLTNEVLLASHLQCAAYELPINIRSDEKFFGNQIQDICEANLEMVEESYRPHPKYLPFPASQVRIRSVSEDMFTLVDVTNDKNVILELLEPFRVALTAYEGAVYVYQGKTFIIRLLNINKRIITAHQVDVEWSTLQRDFTDVDPVRSLMKKTMHGSTNIYFGAVKATLHVFGYFKVNKQKDILDVVDITDHPVEIDSRGFWIDVPWHIIEVLSLKKINGAASIHAAQHALLSLMPIFISNSGNDIRTECKAGEKEYKEAKSERRRPSRLIFYDNCGDSSGAGLCNKAYEHTDELITMAIERIESCDCKVREGCPGCITSSKFEGGVCSGEVLDKVGALILLKMLLCQHVNLDIYADGPEIDSYHALRTLIPSC
|
Helicase with 3'-5' helicase activity involved in genome stability. Functions in the nucleotide excision repair (NER) pathway and plays a critical role in DNA interstrand cross-link repair. Unwinds relatively long duplex DNA up to 120-bp and requires a long 3'-tail of at least 70 nucleotides for efficient unwinding of duplex DNA (By similarity). Shows both processive helicase and DNA strand annealing activities (By similarity). Affects telomere length by a non-catalytic mechanism, probably through inhibiting telomerase by competing with it for ssDNA binding (By similarity).
|
O13988
|
POT1_SCHPO
|
Protection of telomeres protein 1
|
MGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTSSARQNQTGLSYPSVSFSLLSQITPHQRCSFYAQVIKTWYSDKNFTLYVTDYTENELFFPMSPYTSSSRWRGPFGRFSIRCILWDEHDFYCRNYIKEGDYVVMKNVRTKIDHLGYLECILHGDSAKRYNMSIEKVDSEEPELNEIKSRKRLYVQNCQNGIEAVIEKLSQSQQSENPFIAHELKQTSVNEITAHVINEPASLKLTTISTILHAPLQNLLKPRKHRLRVQVVDFWPKSLTQFAVLSQPPSSYVWMFALLVRDVSNVTLPVIFFDSDAAELINSSKIQPCNLADHPQMTLQLKERLFLIWGNLEERIQHHISKGESPTLAAEDVETPWFDIYVKEYIPVIGNTKDHQSLTFLQKRWRGFGTKIV
|
Single-stranded telomeric DNA-binding protein that is required to protect the 3'-end telomeric overhang. It binds the consensus sequence 5'-GGTTAC-3'. Regulates telomerase and telomere length.
|
O13995
|
DAP1_SCHPO
|
Cytochrome P450 regulator dap1
|
MASTQVVFIVTLFLYLLITRWRRKNEKSFIASEEPKQPEWRDYTPAELKEYNGSKNSLVFLAIKGTVYNVTMGSKFYGPQGPYSAFAGHDASRGLAKNSFDDEFIPDSDAEELDDCSDLNDEERQALNDWKAFFDQKYQAVGRLISPREARAAATISETEEKVAHN
|
Required for sterol biosynthesis. Functions as a positive regulator of cytochrome P450 enzymes erg5 and erg11. Function requires bound heme.
|
O14003
|
RFC3_SCHPO
|
Replication factor C subunit 3 (Replication factor C3)
|
MSIEKGKGRAMDIDLPLGSESTLPWVEKYRPANLEDVVSHKDIISTLEKFISSNRVPHMLFYGPPGTGKTSTILACARKIYGPNYRNQLMELNASDDRGIDAVREQIKNFASTRQIFASTFKMIILDEADAMTLAAQNALRRVIEKYTKNVRFCIICNYINKISPAIQSRCTRFRFQPLPPKEIEKTVDHVIQSEHCNIDPDAKMAVLRLSKGDMRKALNILQACHAAYDHIDVSAIYNCVGHPHPSDIDYFLKSIMNDEFVIAFNTISSIKQQKGLALQDILTCIFEALDELEIKPNAKIFILDQLATIEHRMSFGCSEKIQLSAMIASIKTGVDLAAKVN
|
The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. Subunit 3 binds ATP. Also involved in replication and DNA damage checkpoint controls, probably functioning as a checkpoint sensor.
|
O14008
|
CAM2_SCHPO
|
Myosin 1 light chain cam2 (Calmodulin-2)
|
MPASKEQTDEMKEAFVLYDIDKDGLIPTSHVGSVLRSLGINVTDAELAKLSNELGDAIDEKKFMSFVSNKLRETESEEEYIKAFRVFDKDNSGYIETAKFADYMKTLGEKLSDNEVQLMVQEADPTNSGSFDYYDFVQRIMAK
|
Plays a role in meiosis and sporulation.
|
O14011
|
PRP19_SCHPO
|
Pre-mRNA-processing factor 19 (EC 2.3.2.27) (Complexed with cdc5 protein 8) (RING-type E3 ubiquitin transferase PRP19)
|
MFCSISGETPKEPVISRVSGNVYEKRLIEQVIRETSKDPVTQQECTLEDLVPVKVPDFVRPRPPSATSLPALLSLFQEEWDSVALEQFELRRNLTETKQELSTALYSLDAALRVISRLTKERDEAREALAKFSDNIGTVSSKTIEVQEVEMGESDDQLKTSLRSTVEKTFQELSSKRKRTKLQPKWATDDAVSQLLQATPSTILENLETESTTSFFPSPENSSFVLCLHKDELLCLDIQSNSTLKIFEGSALACCWLTSSKIAVATADAISIFEFPVSSSGLQSVGEPTSSIPIDEKVNFLQAHPSGEYLLAASNEKCYIFSLKSQVYNITVAQHITSLAVHPDGNLFVAGLENGELRFFETSSGNELTKFGPHSSPVKTLQFGENGYWLVVTTNDDSDIFIWDLRKSELVQKIPLQTKVAAVSLDITSQLLVSSDGETLYVHIYVKSSKSWRCMSQTHVSSISNLVWLNELHQLLFSTSNGAILRLG
|
Probable ubiquitin-protein ligase involved in pre-mRNA splicing (By similarity). May also function in DNA repair (By similarity).
|
O14014
|
RGA3_SCHPO
|
Probable Rho-type GTPase-activating protein 3
|
MIFRKSISKSPSSKGSTVCFRCGQAFQRRETPISFGGHMWHKDCFCCTKCDKGLEHSDQMLVQTSDGRPVCSSCAHTCTACRMRIKDYALMSGYDSYHRECFRCHDCRKQIIDSNFKRDNRTIFCNDCKQVRHPSRSSDESADYHNFEVDVTIKPTETKSSVESNKSLSIEIMSPQKPPLSPFGGSRDRLVSETPTNMSQAEGGNVPNDGQDSNLASNSADSLLPSAKNRSFSSFTSFESPMKYDDSFFPISPSISPLQKVNKQQQIESPTATFPLSKNTWKNRFHTFHKQSFTPVNDSSSSDSLKPTINEEALDDFAGSASPYKTMSLTDRAEPIVMNGHMRSLHNATSPFRPFSPSYRSSDTHSPRTRSPNVQTHKKTSSQPSDLSSFAQLLSPPQVLSPKPNGGGHKSFRHSHSLSETSQQTLVPSLGSNGEYHLPTNDHSSTPAQSERDSDVEELREQLENLTALTKKLSERLSSSTFDNSKFIRTEDKDTVRSAKLEICEKFFSFADVTDDPTLKDPKHQDLVAAANAYMAMLRESYGTEINNLLERRNELLDDYNNVQKILNESLEASVHLNTKNLELADLNNNLVKQIQHRVPPENQSNLEHTITTSSKNTTSSINPLTAVSSNSGQSSGRPGPLSPNLNVTTRIDIKGKKGSMHLQPRDVNRKVPFKSMHTKSKSADPVVGNEDRTQCDHVFHVNAIFKPSRCYICSESVWGSELRCFHCSISCHSRCLKRLFAESEHEKTMSETVSENSKWMPEMPTRMPPPGPSPTMFGRSLENQLKIEGSVLPQVIAMCVSCVDAHGLEVEGIYRISGSASQVRVLVDEFENGSIRMEHLTSDLFACTSVLKTYLHRLPEPVIPGTQYEELLEAEKIEKEEEKIERVVEVMKTLHPAHLSVFRFLIAHLGRVCKHAEKNLMNSKNVSTVFAPTLMRDKVNRFDLQHATKKSTALQFMLDNVDKILHNL
|
GTPase-activating protein for Rho-type proteins.
|
O14019
|
HAL4_SCHPO
|
Serine/threonine-protein kinase hal4 (EC 2.7.11.1) (Halotolerance protein 4) (Serine/threonine-protein kinase ppk10)
|
MGEKDKLHEISSKFASLGLGSLKSTPKARETTEPPPPSSQQPPSTPNGKEAASPSALKQNVRPSLNSVQQTPASIDAVASSSNVSLQSQQPLSKPVVSSKPNQTTAMPPPSNNPSRHVSSTSNKPAAVSPNPAAHHAELPSGSVPPSASVSRANSTATTTPHKAGVVSNPAAANVHVLSVAASPNPSTPSNGPAPVSTTATPSRNPVTRLQRIFSQNSVSRQNSRTGRGAAVANTEETNSTGGSETGGAANSSSTSNPSSAKWSRFTVYDDASHTHQLRPARRQEKLGKMLKDFLAGNSKKREEERIAKEAADAQHQLSLVQSWINGYGQEKLADKKDPAKVSASFVEKYGRCQEVIGRGAFGVVRIAHKVDPQNSGSETLYAVKEFRRKPAESQKKYTKRLTSEFCISSSLRHPNVIHTLDLIQDGKGDYCEVMELCSGGDLYTLIMAAGRLEPMEADCFFKQLMRGVDYLHDMGVAHRDLKPENLLLTVSGSLKITDFGNGECFRMAWEKEAHMTCGLCGSAPYIAPEEYTESEFDPRAVDVWACGVIYMAMRTGRHLWRVAKKSEDEYYSRYLMDRKNESGYEPIEMLERSRCRNTLYNILHPNPTYRLTAKQIMKSEWVRSITLCEAGNAGL
|
Promotes K(+) uptake, by the potassium transporter trk1-trk2, which leads to the subsequent cellular resistance to toxic cations such as Na(+), Li(+) and Ca(2+).
|
O14021
|
PRW1_SCHPO
|
RbAp48-related WD40 repeat-containing protein prw1
|
MAVSAVPHPSKQAQASEEGINQEKCINEEYKIWKKNSPFLYDLIITRALEWPCMSLQWYPEQQIFAEHGYTEQKMFLGVRADVGKYLLAVASIQLPYLNQTVPPTTMEGASAGDESSLRVNISNLYSHPESVCSAKLMPQDDSCVATVGNYHNDVLVFDKESFESYSSASESPLKPKYRLTKHTQPCTSVCWNFLSKGTLVSGSQDATLSCWDLNAYNESDSASVLKVHISSHEKQVSDVRFHYKHQDLLASVSYDQYLHVHDIRRPDASTKPARSVHAHSGPIHSVAFNPHNDFILATCSTDKTIALWDLRNLNQRLHTLEGHEDIVTKISFSPHEEPILASTSADRRTLVWDLSRIGEDQPAEEAQDGPPELLFMHGGHTSCTIDMDWCPNYNWTMATAAEDNILQIWTPSRSIWGNEQLEEDATAYLS
|
Has a role in chromatin assembly and chromosome segregation. Involved in the deacetylation of histones.
|
O14022
|
CTA5_SCHPO
|
Cation-transporting ATPase 5 (EC 7.2.2.-)
|
MDSIELKQLVPENDSEPGTPRQLLFQHYDISNEETIGIKPFKSIPAKVYILRVTEILTLGLLHLILTWLPEFRLKWIEAPCSNEDVEFVAISDPSGTSSIEKVSSICLKNDIQTSSFVLPSGKTRYFEYKKLRFYLEPLNLQWVLMPLETSAYSLVTSTPAYIQNGLDTFTIAKLRQVYGSNSLVSTKKSIVTILLNEVLHPFYLFQAVSVLIWLCDSFVFYSCCIVFISSYSIFLSVKESKESENRIHSIIGAPQPVTVIRNQVKQTVLADDLVIGDLLYFSNLDLKTCPVDGILFSSSCLLDESMVTGESVPARKFPLEDNSLDSWMIASCNIFSPHLIHAGTKFLKIDSTPSTPCLISVVRTGFRSNKGQLIRNLLYPNLRPSQLYLDSMSFLKTMAILSFVSIVFIAIYLNLYNASFGHVVLRSLDVLTILVPPALPATLSVGIANSIARLSRALIYTTSPESIHNAGCLSTFVFDKTGTLTENSVQLSCVYVKSGSNGLLKQVDADSLSLDSTKLNAHAYRVATCSQSLELVGNELVGDPLEVTLFTQFNGTFCATIRASNTPHPPLFSVSNSFDGPSQIFSIYKALEFDPVLRRMSVICSTSTERSLMLFTKGAPESILAISSQQSIPSNVQEVIHTLSSKGFRIIAFASKNLITPLQELIHLSRSTLESNVTFQGLFVLESPLRESSKDVISSLLRSKMEVSICSGDSLFTSVFVAKHCGALDSCNFIYTAELADSGDDCPQIHFEKIDLQTQNFQPIPDGFSLKDVILEKDSSLCMDGKLLQRLLTMLSFNEIKILLSKLRVLARMSPFDKATYVELCQKYGCKVGFCGDGANDCIALKQADVGVSLSDSEACAAASFVSKKKSIKDVFNVLLEGRCSLILSHRCFQYMVLCAIVQFSGVFFLYLKNYNFNDNQFLFMDLLIIFPLSAAMSYFDPAQNLTSNRPNSTLFGKGRVKDLGIQSVLIWLSHGLLTLILHELNWVELPEWQLEKSNTKNVLVTSIFLLSSLQYLGICIGINQSSEFLSPIWKKKTYVCLCTTIGLCNIYLCFANENHIISRCLQITRLPTLYRFIILFMGVISCCLTSILNM
|
Plays a role in regulating calcium and manganese homeostasis responsible for cell cycle progression.
|
O14023
|
ELP3_SCHPO
|
Elongator complex protein 3 (EC 2.3.1.-) (tRNA uridine(34) acetyltransferase)
|
MSTSSLAFLKAKACAEIVAELIASENQNKVINLNALKMRISKKHQLSESPRLTDIIAAIPPDAYLKESLMRKLRAKPVRTASGIAVVAVMCKPHRCPHIAMTGNVCVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPYEQARGRVEQLRSLGHTVDKVEYIIMGGTFMSLPESYRHTFIANLHNALSGATTEDLDEAVKFSEQSETKCVGITIETRPDYCLDQHLDEMLRYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCETFQLAKDTGYKVVTHMMPDLPNVGMERDIFQFQEYFENPAFRTDGLKLYPTLVIRGTGLYELWKTGRYKNYTPNALVDLIARILALVPPWTRIYRIQRDIPMPLVSSGVETGNLRELALNRMRDLGTKCRDIRAREVGMQEVHHKIHPEQVELLRRDYTANGGWETFLSYEDPKQDILIGLLRLRQCSDKTYRPEFTSQPTSLVRELHVYGSAVPVHSRDPKKFQHQGFGTLLLEEAERIAKYEHGSKKISVISGVGVRKYYQKLGYTLDGPYMSKWL
|
Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
|
O14026
|
SET2_SCHPO
|
Histone-lysine N-methyltransferase, H3 lysine-36 specific (EC 2.1.1.359) (Lysine N-methyltransferase 3) (SET domain-containing protein 2)
|
MQTASSLSVLTPLNEENVDRKSSWSKDTIAVQAVGSSPSSSSSHDFESKEDAEGMNKDESAPSPSTSSPSSASSRSQSKYVRKEALPPQLFHHLDSAKDKALTTFEEIQECQYASANIGKPPENEAMICDCRPHWVDGVNVACGHGSNCINRMTSIECTDEDNVCGPSCQNQRFQRHEFAKVDVFLTEKKGFGLRADANLPKDTFVYEYIGEVIPEQKFRKRMRQYDSEGIKHFYFMMLQKGEYIDATKRGSLARFCNHSCRPNCYVDKWMVGDKLRMGIFCKRDIIRGEELTFDYNVDRYGAQAQPCYCGEPCCVGYIGGKTQTEAQSKLPENVREALGIEDEEDSWENITARRQRRKKGIDETSKIIEEVQPTPLTSESATKVIGVLLQTKDDLLTRKLMERIFLTSDPSVCRSIIALRGYNIFGLMLKKFSIDIEFILRSIKTMLSWPRLTRNKIQDSNIEPVVQEFCDHENEEVKDHAKTLLKEWESLEIAYRIPRRKPGQVAPQSTNAEPSNNQSNPPLRDQEPQRGDKGDIKSAINNSTEDLSKKHPALHSSRPSDSRSRSKFGNDYQSHSKHNLFRKNSFPKRRRLSNSDTPSETTTPNNEQEQVSNQANKVDLNKIISAAMESVNQKNVLKAQKEEEERIAQQKREEKRRLAYEESLKRHAKKLHEKKTKSSQDATIDHHLTSHSPESIAFKAVLAKFFANKTARYQEKLGKAEFKLRVKKMTEIILKKHIQLVLSKKEKALPDELSDSQQRKLRVWAFRYLDTVVSRSGTATTTPTDSPSIGESPKKAA
|
Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3 (By similarity). Involved in transcription elongation as well as in transcription repression.
|
O14031
|
PGT1_SCHPO
|
Glutathione transporter 1
|
MTARNSASIPTSIRKTSENEVSGDETPAGVGNLSTKTASKTSLTFRQSSSDESTSSYSGNHHNINIQHHPNRPFRTNSSSFSPNDYSISESPSKSKKDGVHVSAVQLDNETDSEVESEVEELERELEAIEDSVYPEVRAAVNPTDDVNLPVNTWRTWVLTTIFVIVFAAVNQFFSLRYPALSISFIVAQLILFPLGKLLNLLPNWKIGYGRFSFYLNSSPFNVKEHAAITIAVSLTSSTAYATNILSAQTSFYKQNLSWGYKILIVLTSQMLGYGFAGLTRRWIVYPAAMIWPQTLVSTVLFRTLHGNSGNDIGVLKNNRISANGWTISRYRFFAYVMIGSFVFYWFPGFIFKGLSYFTVLCWIWPKNRVVNQLFGYNSGLGILPLTFDWQQVVYNSNPLASPWWVICNTFGSVVLIFWIVVPILYYKGVWFSNYLPMLSSSTFDHTGVSYNSSRVLNSDYSFNHTKYESYSPLYMPMSYSMSTALNFAAVTAIFTHCALYNGKDIWQRLWKESGKDECIHRKLMRNYKEAPQWWYATLFIVVFGLTIFTVRYYDTQCPVWALIVALLIFIVNFIPQGVLEGITNQHVGLNIITELIGGYILPGKPLANLMIKLYGFIPMRQGLEFSRDLKLAQYMKIPPRILFFVQLFATILGGITQVAVQEWMNYHIPGICTTSQSNGFTCPNGRSIYNASLIWGAIGPAKMFSKGKPYYPLIFFFLIGAVAPFITWGLRKRFPKSWIGKLNAPVLFTGPGNIPPATGINYSSWAIVGFIFNYVIRKRAIHWWRKYNYVLAAAMDSGVAVAGVVIFLCVSYPGGKITWWGNTVYTKTYDWKSVPYRSLGPNETFGYTNW
|
High-affinity glutathione transporter which plays a role in scavenging glutathione from the extracellular environment for the maintenance of sulfur homeostasis.
|
O14036
|
SMD2_SCHPO
|
Small nuclear ribonucleoprotein Sm D2 (Sm-D2) (Complexed with cdc5 protein 9) (snRNP core protein D2)
|
MADLVDKPRSELSEIELARLEEYEFSAGPLSVLQQAVKNHDQVLINCRNNKKLLARVKAFDRHSNMVLENVKEMWTEKKRTASGKKGKAINKDRFISKMFLRGDGVVLVVRIPSA
|
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity).
|
O14040
|
DI3L2_SCHPO
|
DIS3-like exonuclease 2 (EC 3.1.13.-)
|
MDLKPNIRRKEKRNLLKGEAALEKKGSIDRKTKNKAYPSTTHDPHQNDDSNIPGLGSGLLERIKDIVQRPTDTQLKGQDSNHKKASLTETKTEKAKVKPKAKKKNSKEKISKSSKQDEHKTDVHKESVSKLSKNLESRNNRDENSAKREKNNSHQVEADTNNATEMVSSNAKKSVYPLYYDSATVKKGLKSGTLFKGTLRILENHRSAFACMEDIPDFYVDGPIARNRAFHNDVVIVEPVMNNDSPTEKSNFLQNGVEKVKIKDHDDELGGAMEHLERLEIKSVASFKGDSRTRARVVAIEKRAEISKIVGILRAPGWSLKNVEYVSKKSSYAIFIPKDKRLPFITIHKNDLSDLSGENWIENILKHHDQLFSVEITRWSIYSRYPMGVLGEKLGNITDVEAYTNALLLENGISSSPFSDEVLNCLPPDDWIISHEEIKKRRDLRNELIITIDPETARDLDDAVSCRALDNGTYEVGVHIADVTHFVKPDSALDKEAASRATTVYLVQKAIPMLPPLLCERLCSLNPNVERLAFSVFWKLDSNGKEIGKRWFGKTVIKTCARLAYSEAQGVIEGKSWDDAVGKPIGGTHTPKDVETSILTLCEISRKLRKDRFAKGAVEINSTELKFQLDEYGMPNKCEVYEQTDANHLIEEFMLLANRSVAEHISKNFSNNSLLRRHASPKEKQINEFCHFLKSMNFDFDASSSAAFNASMVRLRSTFNEELVELFENMAVRSLNRAEYFCTGDFGEKTDWHHYALSFNHYTHFTSPIRRYPDIIVHRLLERSLKNTSPGIDKKNCSLVAAHCNEKKEKSTTVQEDSQQLFLSVYIAEYCKKHDKKSMPVQAFATRISGNSIDVYISEYGISNRVDLSSDDRIKSFIVAPDDSSVKITLFDDSQKTIALTDRFQVYLYSDYSRTFFSIRCSLVSLN
|
3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. {ECO:0000255|HAMAP-Rule:MF_03045, ECO:0000269|PubMed:23503588}.
|
O14050
|
MSY2_SCHPO
|
Mechanosensitive ion channel protein Msy2
|
MNEHRREPHRRSGYQDDSAFTNTEKLVDELDHNVEPEQLLEKNRTDFKLMYVIVKFYRWFNNLSFITRWITIWFPLAGALVIPLAVGVSPYPNAKLGGVRIFWIFVWLEVAWGGFWVSRVIARLLPYILYPLMGILPFTMYKYTVILTALEMPLAIFFCSIVCVCTFSPIMIGKGNFTSTTVTTTTSATATPTASASSNAVESVFVTKTAASVPSWIKVITKILGAAVVTSIVLLLEKIFLHFIGFHYHEVQYQYRITDNKRNTAVLAKLLTAALDAPYHDSPRVRRQDYLLGLIDTRSMSESKGSGNGKLRKVKKISKNAKRIFSKTRNAISTAFTDMLGKHAKDLTPEQEFILETIRSKKKCLALARKIWYSLVPEGEDCFQKEDLIGLIPDDEINDIFHILDNDYSRTVTLDEMEQFTREISIEFRSISSSLRDVDLALGKLDRVGLGVVGIIAVLTFISFLDTSFATILAAFGTTLLSLSFVFSTSAQELMSSIIFLFSKHPFDISDVVIVNNIKYEVVSLSLLFTVFRTMGGSTVQAPNSLLNTLFIENLRRSQPQSETITIVSPFATDFKQLERLRDLLLTFVKENERDFRPIIDLNVSDFSTLDSLKFTVTYYYKSNWQNVSLQCVRRNKFMCALKNAIATTNLPAVADPVRGSPDYPFVIEQYNLERPEYSKTASRPQFSDISSTASSNSLSNKPGFAHSESRNYHTHDEDNSSDDNHKREDRGHLPAQYLRQSVATWQIPNLISAIEAYDSQNESSQENATYTVVESNGNANGDNTATNSQGATDNGQTTTNTTQNNVDNTQATTDNTQANTDNMQVAIDYSQNMDGQIQY
|
Regulates intracellular calcium levels and cell volume for survival in response to hypo-osmotic shock. Involved in maintaining vacuole integrity and protecting the nuclear envelope upon hypo-osmotic shock.
|
O14063
|
IMA1_SCHPO
|
Importin subunit alpha-1 (Cell untimely torn protein 15) (Karyopherin subunit alpha-1) (Serine-rich RNA polymerase I suppressor protein)
|
MSASSRFIPEHRRQNYKGKGTFQADELRRRRETQQIEIRKQKREENLNKRRNLVDVQEPAEETIPLEQDKENDLELELQLPDLLKALYSDDIEAQIQATAKFRKALSKETNPPIQKVIDAGVVPRFVEFLSHENNLLKFEASWALTNVASGSSNQTHVVVEANAVPVFVSLLSSSEQDVREQAVWALGNIAGDSPMCRDHVLQCGVLEPLLNIIESNRRLSMLRNSTWTLSNMCRGKNPQPDWNSISQVIPVLSKLIYTLDEDVLVDALWAISYLSDGANEKIQAIIDAGIPRRLVELLMHPSAQVQTPALRSVGNIVTGDDVQTQVIINCGALSALLSLLSSPRDGVRKEACWTISNITAGNSSQIQYVIEANIIPPLIHLLTTADFKIQKEACWAISNATSGGARRPDQIRYLVEQGAIKPLCNLLACQDNKIIQVALDGIENILRVGELDRANNPDKINLYAVYVEDAGGMDLIHECQNSSNSEIYQKAYNIIEKFFGEEDEIEELEPETVGDTFTFGTTQEPAGDFQFSATNAEDMAM
|
Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs. Has an essential role in mitotic chromosome condensation. Involved in nuclear protein import. Required for efficient nuclear import of both an SV40 nuclear localization signal-containing reporter protein and the pap1 component of the stress response MAP kinase pathway. Required for proper mitotic progression.
|
O14064
|
BIR1_SCHPO
|
Protein bir1 (Chromosome segregation protein cut17)
|
MKPITSSSKRRWNRFRREMCNYSKRLDTFQKKKWPRAKPTPETLATVGFYYNPISESNSEERLDNVTCYMCTKSFYDWEDDDDPLKEHITHSPSCPWAYILSSKNNPNQNPQAAALTKCREQTFVDKVWPYTNRPDYHCEPSVMAASGFVYNPTADAKDAAHCLYCDINLHDWEPDDDPYTEHKRRRADCVFFTWKDPNSLSPTKLSFLSTSNIDPEDLTEDNSILPVSPTRDSTKSHKTLNFSPSRKNNLNARPLTMSLYTNTSEEKDSQPTRAPQSPTKPVLLTAPRRKNKSPKKSKPAVFKPVKPIFSDEDEDDDDLTASQPFSKGICNDSMQVAKKNFTEEIPLKEDEKDNELEHLVSPATSVHTTVSDITGHQSVTDESDEQNNCMSTPPKIEIESKIEEEISVVSKSKEISSSVSSVGKEQNHTEKQVAIETPEQQKVEKEDEHLNLQGSFIEESTKQPISSKPSTSSPDMTDAATGGRVSSSSFRDKILQTNFSPRSTIDSFSNISKKRNSEEANDENDETNLKIPIPEKKRKFQEVLQSKNILVSSTEDSHEPVKVTEDSQTAIHVSKFEDLENKSMESEQSLQLLSESENDDKPLIDLIPLLAIKRKDNLVSGVLEKGKSTSTSKTKFDTSIVDFIEKPKTEISEVLPEEKRKAICDESQTVRVSIDRGVTKTRDVSSPVSDEKSENVNHEEANSGHTVMNVHSSLDPQPIVQPNELESGSYLKDLPDRNVGNSEKVTFQEDDINSPKLQSKNNQTVEAVNTETSDKLQEKEANHELENIEKIEEKLTEVDKVSLSDAFPDQEIKNSRTSVQNGTRSVSKNTPEKETKVDKIDNVSKKDVETSPGSCETSSAFAKTYAEKEVTSINLPSVRKPLDESYYDHSISPFDPLCQSSFLAPQTPVKSKHALPLVEANAPPWEPIDFSSLLESPVPNPVEPNKLSEKELDMTVEQWIKFMYAKCAKEFEEACEEKIEWLLEEGKRAEEYIQNL
|
Seems to act in the pleiotropic control of cell division. Has a role in chromosome segregation by recruiting condensin and ark1 kinase to appropriate sites as the cell progresses through mitosis. Ark1 activity depends upon bir1 function and phosphorylation. Ark1 with bir1 function is required for full-scale association with kinetochores and formation of a complex with mad3.
|
O14072
|
ATC4_SCHPO
|
Endoplasmic reticulum transmembrane helix translocase (EC 7.4.2.-) (P-type ATPase cta4) (P5A-type ATPase cta4) (Sporulation protein essential for vegetative growth 4)
|
MGSKALITSPDISSGQLYIKLPTFFHLYVWPFALFVYPYIGYVYQNKLYSEEVRYLTYIAVGTIHALFWLAGEWNTKVYCLMTCRKTDKVEQATHILVTPSKIGESSSVEPITKLVLPDSQTIQYSFSFQRKRFIYEPEKGCFANITFPMDEPSTIGTLKKSTGLTNIQSEIFLYRYGKNCFDIPIPTFGTLFKEHAVAPFFVFQIFCCVLWCLDDYWYFSLFSMFMIIALECSVVWQRQRTLTEFRTMSIKPYEIQVYRNKHWFPISTEDLLPNDVVSVLHNKEDSGLPCDLLLLSGSCVVNEAMLSGESTPLVKESIELRPEEAVIDVDELDKNAVLFGGTRVLQVTQSPFCKLKTPDNGVPAIVLRTGFETSQGSLVRTMVFSSEKVTANNRESLYFILFLLVFAIAASGYVWHVGSKTERSRYKLMLDCVMIITSVVPSELPMELSMAVNASLGALSKYYIYCTEPFRIPLSGHLDICCFDKTGTLTEEHMVVQGIAGVNRKDPYSLEKLSDASNDAILAIATAHTLVLLEQEGETPKVVGDPMEKATVENLGWSIEKKNFVSAPEGSVFYKGKVQIIRNFQFSSALKRQSSVSNVRVSGGSFKTFVSVKGAPEVIATMLREVPKDYEKIYKDYGRKGSRVLALGYKYFKNYIPENQVSDLSRESIESDLVFAGFLIFTSPLKEDARQTVQMLNNSSHRCMMITGDNPLTAVYVAEQVGIVEKPTLVLDIKHENEKILEWKSTDDTINLPMNPHKSLEASLYEKYDLCITGRALSQIINPDVIMSIFTHAWVYARVSPSQKEFMISTLKHNGYITLMCGDGTNDVGALKQAHVGVALLNASEEDMLEMQERARNQKLMGVYEKQIQLAKRFNLPTPPVPPALCHAFPPGPNNPHREKTQEGLNKVLEDLETKKASDVQLTEAEKAAERRANLANKMFDTLANASDDEAPKLKLGDASVAAPFTSKLAVVSSITNIVRQGRCTLVALVQMHKILALNCLITAYSLSVLHLDGIKFGDTQYTISGMLMSVCFYCVSRARPLETLSKERPQAGIFNTYIIGSVLGQFAIHIVTLIYITRVVYLYEDPLEKVDLEETFKPSLLNTAIYLLQLIQQVSTFAINYQGRPFREALSENKGMYYGLLGIAFVAIAGVTEFSPELNAKLQLVKMAYNFQIQLLATMVVDYAACWIIEELMKKYFRDNKPKEIVLRN
|
Endoplasmic reticulum translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Specifically binds mitochondrial tail-anchored transmembrane proteins: has an atypically large substrate-binding pocket that recognizes and binds moderately hydrophobic transmembranes with short hydrophilic lumenal domains (By similarity). Involved in controlling nuclear calcium ion levels. Required for cytokinesis and stabilizing microtubules. Required for assembly of the forespore membrane. Involved in calcium transport to the endoplasmic reticulum.
|
O14079
|
MDB1_SCHPO
|
DNA damage response protein Mdb1 (BRCT domain protein Mdb1) (Midzone and DNA break-localizing protein 1)
|
MEIQFGNQRCRMVNSGGFLATDGSHLKEMETDDVLVEFLNIEHQLFIRNIRAIVKIADTTVLPSASDKKLLYYVFDETRVRINDTPVIFSKLEEDNANVNEGSKMGVMTVPNTPQKPNLQQQKFEAINANEDQIDYSSNLEQNYNSLIRQGSDQVIPLSRFASEKSALELEKELFSERIPESQSAAEPVLKVENSENDLDEKLVLDGQHVEGDHSSDTEEEVVSEDQKQLNKTDDESTFIESHQIYIQGETKSPSSVSQSLSGDPSLKPAEVFDRKQSAEINSPIEKDVNPQQNISDSSIKNNSIHSDEVNPEVRPDLTPSNENEESKRSAPEIALKEKESTSQDESNREAEEAPISTNYSFPSSSLEDQPDKNVQSSAVENKNKHTNLVTSSFNLTKPMKSFIRRNGLRVQESVTDETDFVILGSPPLRRTHKFLLATSLGIPLVSSQYLTDCIKSGKVLDFRSYKYKDEEAEAKWGFRLDDIHRRTCFNGKRLYITKAIRDSMVGDSIHGLYSILETSGAEIVGDIKRAQEKDTIILAQPDNDQEGRNMSATGLNVYKIELVALSILRDRIDFDEFLIDYDADSPTKVIGKRNVSKASRTGQGRKRSSRSSWNKPSAKEQRT
|
Involved in DNA damage response (DDR) mediated through its interaction with phosphorylated H2A proteins hta1 and hta2 which mark the discrete foci of DNA damage.
|
O14089
|
IMB2_SCHPO
|
Importin subunit beta-2 (Importin-104) (Karyopherin subunit beta-2) (Karyopherin-104) (Transportin) (TRN)
|
MGDNPWVLQEQVLVELSEVIKNSLSENSQTRNAALNLLEKAKDIPDLNNYLTCILINATELSVSIRSAAGLLLKNNVRVSSLESGSGLQSLDYTKSTVIRGLCDPEQLIRGISGNVITTIISRWGISTWPEVLPQLMEMLSSPASTTQEGAFSALTKICEDSAQELDRDFNGTRPLDFMIPRFIELARHENPKIRTDALFCLNQFVLIQSQSLYAHIDTFLETCYALATDVSPNVRKNVCQALVYLLDVRPDKIAPSLGSIVEYMLYSTQDSDQNVALEACEFWLAIAEQPDLCSALGPYLDKIVPMLLQGMVYSDMDLLLLGNDADDYDVEDREEDIRPQHAKGKSRITLNTQGPITQQGSSNADADELEDEDEDDDEFDEDDDAFMDWNLRKCSAAALDVLSSFWKQRLLEIILPHLKQSLTSEDWKVQEAGVLAVGAIAEGCMDGMVQYLPELYPYFLSLLDSKKPLVRTITCWTLGRYSKWASCLESEEDRQKYFVPLLQGLLRMVVDNNKKVQEAGCSAFAILEEQAGPSLVPYLEPILTNLAFAFQKYQRKNVLILYDAVQTLADYVGSALNDKRYIELLITPLLQKWSMIPDDDPNLFPLFECLSSVAVALRDGFAPFAAETYARTFRILRNTLYLITTAQNDPTVDVPDRDFLVTTLDLVSGIIQALGSQVSPLLAQADPPLGQIIGICAKDEVPEVRQSAYALLGDMCMYCFDQIRPYCDALLVDMLPQMQLPLLHVSASNNAIWSAGEMALQLGKDMQQWVKPLLERLICILKSKKSNTTVLENVAITIGRLGVYNPELVAPHLELFYQPWFEIIKTVGENEEKDSAFRGFCNILACNPQALSYLLPMFVLCVAEYENPSAELRDMFQKILQGSVELFNGKASWQASPEVLAQIQAQYGV
|
Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for arginine/glycine-rich nuclear localization signals (rg-NLS) and PY-NLS in cargo substrates. Its predominant cargo substrate seems to be mRNA-binding proteins. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
|
O14092
|
HEM1_SCHPO
|
5-aminolevulinate synthase, mitochondrial (EC 2.3.1.37) (5-aminolevulinic acid synthase) (Delta-ALA synthase) (Delta-aminolevulinate synthase)
|
MERVVKLAAKHCPFVSKADPSALRRMAGAGLIRAGARCPVVRHALPVAAATGADVSRGFKSDSKQMAMEPSLDEIHLKAGVVNTGSRTCRHADAVKAAAEAATTTPVTKKHQMPKHYASDLNGVGPATTPRFDYDTFYREELDKKHRDKSYRYFNNINRLAKEYPLAHLADPNTRVEVWCSNDYLNMGGHKKIREAMHQCIETYGGGAGGTRNIAGHNQHAVRLEKSLADLHQKPAALVFGSCYVANDATLSTLGRKLPNCIFLSDEMNHASMINGIRNSRCEKIIFKHNDLVDLEAKLASLPLNRPKIIAFESVYSMSGNVAPISEICDLAKKYGAITFLDEVHAVGMYGPRGAGVAEETPGLLSRVDIITGTLAKSYGCVGGYIAASSTLVDMIRSLAPGFIFTTSLPPHVMVGALTAVEHLKVSNVEREQQRSAVRRVKQSLSEIGIPVLSNDTHIVPAMVGDAHLAKLASDSLLHDHNIYVQSINFPTVSVGTERLRITPTPAHNTEHYVQSLTNAMNDVWSKFNINRIDGWEKRGIDVGRLCKFPVLPFTTTH
|
Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
|
O14098
|
CTK1_SCHPO
|
CTD kinase subunit alpha (CTDK-I subunit alpha) (EC 2.7.11.23) (CTD kinase subunit 1) (Latrunculin sensitive kinase 1)
|
MSYSKSTIYRRQGTEPNSHFRRTVEEKSQLSGTNEESLGGHTLSSNAFKNNSSSISPSSSAKDPREQRKRTFPLNDTHSSRARQHERPFRSRKSRRRKGKKAFSPRPGSPPSPSFYRSGSQKRARNLTTKDYFAKRSESSSSASVSPISPSANRNDSKRQASSFRRSPPSSVHMKPSAFNGRKVSRRPSSSPPPIPSIPHETTSSDTQKKSSVSSGFPENKHGKFHFHIPNERRSRFDQPPSKRMALTSTARESVPAPLPSPPSGPIYTYTYPKPAYEKIDQIGEGTYGKVYKAINTVTGDLVALKRIRLEQEKDGFPITTVREVKILQRLRHKNIVRLLEIMVEKSSVYMVFEYMDHDLTGVLLNSQLHFTPGNIKHLSKQIFEALAYLHHRGVLHRDIKGSNILLNNNGDLKFADFGLARFNTSSKSANYTNRVITLWFRPPELLLGETAYDTAVDIWSAGCIVMELFTGKPFFQGRDEISQLEVIYDMMGTPDVHSWPEVKNLPWYELLKPVEEKKSRFVETFKEILSPAAIDLCQKLLALNPFCRPSAHETLMHEYFTSESPPPEPAVILKNMQGSWHEWESKKRKSKR
|
Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. Involved in RNA polymerase II transcriptional elongation and pre-mRNA 3'-end processing (By similarity). Together with ctk2/lsc1, required for the regulation of cytokinesis by phosphorylating 'Ser-2' residues found in the heptad repeats of the CTD. Required for nuclear localization of ctk2/lsc1. Positively regulates the septation initiation network (SIN) and promotes successful completion of cytokinesis in response to perturbation of the actomyosin ring. Acts in parallel to clp1 to promote actomyosin ring stability upon cytokinesis checkpoint activation. {ECO:0000250, ECO:0000269|PubMed:15537703, ECO:0000269|PubMed:17502918}.
|
O14111
|
PSD3_SCHPO
|
Phosphatidylserine decarboxylase proenzyme 3 (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 3 beta chain; Phosphatidylserine decarboxylase 3 alpha chain]
|
MPFTKSCRSANTLRKGIKNGKLILKIIVNDIDNVESCLSGDESNDSKKSSASFYMKLKYGSYRALADNILSTDENRKEDIAVFDVPLPNGLQIDTFTLCLYRKSKWKKQIVGEAYIGIQALLLSTNPDETCKYPVISPPSGRNKENQSPSHQICNLSLKWIIYDPEDADADSKTLAKAWLQQIKMNQTSIDPMSNISKSLKELEVDNVESDLEDSSFIAEPDSSIPPSESSVSISTDTGKETPPSKSKKSSNQPYVSIGEGNSDLLGFVFLEIISVSNLPPLKNVFRTGFDMDPFVITAFSKNIFRTKWLRHNLNPVYNEKFLFEVGAFESNYDLVFKVVDHDKMSLNDSIAVGSFNVQSIINSSAQVDPETGLYSFNIETSSPSQDTSSKAEDSPTVQKIADDFSSAVGKDLRTDIIEQIIPLTLCCKHDFSTPRDVKLSFKAMFFPIAALRQKFWRVMLAQYGDIEDGHIGKLGMYAVLDTLGSNIPNSMVDDIYTELSSKNHDDTSDSITVDEAVICLERLVDLVCHQDQQATQTPQSPSSNEESGPGTPTQTSDQYEDSEDSRNFPSKLYLVYLSNCPLCLKFKLSKVNQQKATVHLATCASHDWKRVDRLMMTSYVSLNQAQRRWFSKAFAKVVYGSSKVGSTSATTLVQNRQTGQIQEEKMNAYVRIGIRLLYRGIRNRRIEGSKVKKILRSLTLKQGMKYDSPISVKEIKPFIRFFDLNMNEVDMPVGGFKTFNEFFYRKLKPGSRPCAFPDNPDILVSPADSRIVAYECIEKATTYWIKGTEFTVERLLGYSNEAQRFVGGSICISRLAPQDYHRFHSPVNGCIGPITKIEGQYYTVNPMAIRSYLDVFGENVRVLIPIDSNEFGKVMLVAVGAMMVGSTVLTVDEGKIVQRSDELGYFKFGGSTVITLFEPNVTSFDEDLLRNSKTKIETLVKMGERIGQKIDPNKPTDAEDHSKSDS
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Together with psd1 and psd2, responsible for the majority of phosphatidylethanolamine synthesis. {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:19286980}.
|
O14113
|
SDE2_SCHPO
|
Splicing regulator sde2 (Silencing defective protein 2) (Telomere maintenance protein SDE2)
|
MECKTVFLNGDFLKNSVNVNLNRLATVETLLRHVLGDSYETVLERAYLTHQSRIVHPDIQLCKLEGKSTSAHLNLTLCTRVLGGKGGFGSQLRAAGGRMSKKRNEQENQDSCRDLDGNRLGTIRQAKELSEYLAKKPAETRAKKEAKKQKLNKVLAADSSSSRFDDHEYLEDLEQSVSNVRDAFQNSLLYRRGSTSASSFSSGSNGATTDEPAEKEARNNNSSINSWSRRMQASESSNEAEGEDSESQTSKSLYEWDDPLYGL
|
Plays a role in pre-mRNA splicing by facilitating excision of introns featuring relatively long (>21 nucleotides) spacing between the branchpoint and 3'-splice site (ss). Recruits cactin to the spliceosome which may enable folding of RNA between the branchpoint and 3'-ss, to guide the splice site towards the spliceosome's catalytic center. Required for proper chromatin organization by assisting splicing of components involved in genomic stability and telomere organization.
|
O14114
|
ATD2_SCHPO
|
ATPase histone chaperone abo1 (EC 3.6.1.-) (ATPase family AAA domain-containing protein abo1) (AAA-ATPase)
|
MKEEASEHGGSADETQELSPVSDSSDEMPNNAKRRRRSQSMIANKRIHQAFQEDEGDEDWEEEEHKPKAKRRYNTRSNESFSEGDDEPFEVSESSALEDELSDSEDSFIRSVRSKPKYKPGTRRSTRLRNRRSQDEEESEEEHRPILRERTSRINYSVPLAFPPVDEMDGDPSSQVNQSRSRKTHSELAITKLLRQQVSSFMPYIDSSGSESESDNTRIKKSSAKTIKALTDPANSGGPPDFGRIREKSDLADSDPLGVDSSLSFESVGGLDNYINQLKEMVMLPLLYPEIFQRFNMQPPRGVLFHGPPGTGKTLMARALAAACSSENKKVSFYMRKGADCLSKWVGEAERQLRLLFEEAKSTQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGMESRGQVIIIGATNRPDAVDPALRRPGRFDREFYFPLPDRDARKKIIEIHTRNWDPPVPEWLCSMLAEKSKGYGGADLRALCTEAALNSIKRTYPQLYRSTKRLQIDPKTIKVKVKDFVMSMKRMIPSSERSSISPSKPLSPELKPLLNEAFQDIEKTLQKLMPVASKLNPLEEVMYDDPKENDFEYQQRLETFETLRIYKPRFLICGRKGLGQTALGPAILQQYEGVHVQSFDMSTLLQDSTQSIETSIIHLFLEVRRHTPSIIYIPDIDNWLNVLPLTAITTFSSMLERLDFSDQILFLALSSSPLSELHPQLREWFSSKQSVYSLQYPTRDSIIAFFQPILELIKASPTELPGGIPRKRRVLPELPLAPDPPPFTSQKITLKQTKQADMRLLNKLKIKLNALLGSLRARYRKFKKPLIDFNDIYCVDPETGHSYRSREECHYEFVDDVVKQIGSDQKFSMMSLEEIEKRTWDNCYCTPKQFVHDIKLILRDALQLEDSETIKRAQEMYANVLLGVEDMEDDQFSQRCERMALREAERRKLRHGKLQKHLDETKADMQFTSEKPSVDESITEVDDAIKDGPPVLAETLTNSLMEDVGPENVDMDIEDNEIFTNQSTMSVPSMLVENEESPKPDEYIDQKDKVQSPLLNGKSPVGVPSEAALRVSTDVSTNISSNGRADIPVDTLITSPADVPNNAPTDAHNITSADGHIENIEQEVVFPDLVFDEDRLTPLKQLLIDSTTGFTVDQLLHLHSFLYQIIWNTKSEWNRNSVVDECERAVKEFMINALQ
|
ATPase histone chaperone which facilitates loading of histone H3-H4 onto DNA in an ATP-dependent manner. Plays a genome-wide role in nucleosome organization and establishment of chromatin. Also plays a role in heterochromatin assembly by stabilizing recruitment of the histone methyltransferase clr4 to methylated histone H3, to promote the transition from H3K9me2 to H3K9me3.
|
O14122
|
CUL4_SCHPO
|
Cullin-4 (Cul-4)
|
MPPEAKRIVVKGFDPRKSRQRQETYYVTMIDRLNMALQVVMAGLGLKTGYQELYSGVENLTRADQASRCFNILQHHMSSGIQLLKDSAESFIQLEGTETDTNACTVVVGCWNKWLERVEIVQNIFYYMDKTFLSHHPDYPTIEELSLSLFREKLMAVKNIQIPFLNSLLQSFENLHSSKSTDHAYLQDAMLMLHRTEMYSSVFVPMYLVMLSRFYDTESSQKIQELPLEEYLEYAMSSLEREDAYVEKFDIVRDKKSIRETVQRCLITSHLDTLTKGISQFIEKRDAHSCKLLYALLQFNHETEYLIQPWSDCLVDVGFKLVNDESKDDTLVQELLSFHKFLQVVVDESFLHDETLSYAMRKAFETFINGAKGSQREAPARLIAKYIDYLLRVGEQASGGKPLKEVFSEILDLFRYIASKDIFEAYYKLDIAKRLLLNKSASAQNELMLLDMLKKTCGSQFTHSLEGMFRDVNISKEFTSSFRHSKAAHNLHRDLYVNVLSQAYWPSYPESHIRLPDDMQQDLDCFEKFYLSKQVGKKISWYASLGHCIVKARFPLGNKELSISLFQACVLLQFNNCLGGEGISYQDLKKSTELSDIDLTRTLQSLSCARIRPLVMVPKSKKPSPDTMFYVNEKFTDKLYRVKINQIYLKEERQENSDVQEQVVRDRQFELQASIVRVMKQKEKMKHDDLVQYVINNVKDRGIPLVSDVKTAIEKLLEKEYLEREDNDIYTYVT
|
Required, indirectly, for activation of ribonucleotide reductase through the degradation of the protein spd1, thereby supplying deoxyribonucleotides for DNA replication and repair. Also has a role as a scaffold for assembling ubiquitin ligases. Component of the Clr4 methyltransferase complex (ClrC) which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me. ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 methyltransferase activity for the methylation of H3K9. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.
|
O14129
|
RAD55_SCHPO
|
DNA repair protein rhp55 (RAD55 homolog)
|
MLSSQHRLVTQPAIRAYEAFSAPGFGFNSKLLDDAFGGSGLKRGYISEVCGAPGMGKTSLALQITANALLSGSRVIWVETCQPIPMERLRQLLDNHVPSSQDEEEKCDTDELLNLLDVVYAPNLVNILAFLRNFDQEKHLKEIGLLIIDNLSMPIQLAYPTSPEDYAYLRLRRNTSKKSSLSDSSQKENTLTLNKENEFSSKDDSNFAFHNSSTKTTINRRKKAIGTISSLLSKITSSCYVAIFVTTQMTSKVVSGIGAKLIPLLSTNWLDNLSYRLILYSRHSTEESKDGQSRPSHQLLRYAFMAKQPPAHSAESELAFQLTSTGIQDYQSIPTNSSQRRKRSILECES
|
Required for radiation resistance and meiotic viability and acts in recombination and recombinational DNA repair pathways.
|
O14132
|
PIT1_SCHPO
|
Sporulation protein kinase pit1 (EC 2.7.11.1)
|
MKKYLWGTPTTNTVFTGKQPKYTKEVRKCISIDEVYNVVRKVGDGTFGSVYLATTKTPSKEVVAIKSMKKKLAKVSDATRLREVHSLLRLSENENIVNIFDLYIDQFRCLHIVMEFLDCNLYQLISTRKNDPLTLEQVQDIMRQIFKGLNHIHTNGFFHRDMKPENILISSNSDSSSFNVKIADFGLAREINSRPPYTEYVSTRWYRAPELLLRDSYYSFPVDIYAAGCMAFEIATLQPIFPGNDDFDQLYKMCEILGSPDEQSQNTGDKGGGIWDRAELLANKLGISLPKMAPLDFGDLFSPPWNLAFASMLSQLLKWDPAKRPTAEMCLDLEFCRVSAPADAVASKEEVNKNTDFRVSISYFPSSSSIPDECNTEEESRINPSTSKFLKQLNKGFNGFTKPFRKSRKQSKNRKNKSSVATQFSEESEDIADSITSSTFFPVLPQIRPSTPLNLKLRNFIISSSEDSTSPKAKEFDRPLPSTEFLVAINKSQEALLNNSPNSKSGSTQLSASTCLSDLISPQLSILSHEDKRENQSVNSESSKYSPRSSNHSPTLHSKDLHRDMATVNNYAKSPPSFHATQDLLRKTLAYTNSSGTSTVLSNDSSAISSTFLDRDFPDFGITSLAGSLTLPDSKIIDRSKTHVSTQLLP
|
Protein kinase which is essential for spore formation.
|
O14139
|
HRP3_SCHPO
|
Chromodomain helicase hrp3 (EC 3.6.4.-) (ATP-dependent helicase hrp3)
|
MSTSAIALALSSSKAIEQLDHVQTETPNLKQEMSESPSNSGVASKRKLQSTEWLDPELYGLRRSGRTRSNPGRYVDTDDQEDVFPSKHRKGTRNGSSFSRHRTIRDLDDEAESVTSEESESDDSSYGGTPKKRSRQKKSNTYVQDEIRFSSRNSKGVNYNEDAYFESFEEEEEEEMYEYATEVSEEPEDTRAIDVVLDHRLIEGHDGSTPSEDYEFLIKWVNFSHLHCTWEPYNNISMIRGSKKVDNHIKQVILLDREIREDPTTTREDIEAMDIEKERKRENYEEYKQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPIAATEIQAFQEREESALSPSRGTNYGNSRPKYRKLEQQPSYITGGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCISYLGNTTSRQVIRDYEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRRLKKDVEKSLPSKSERILRVELSDLQMYWYKNILTRNYRVLTQSISSGSQISLLNIVVELKKASNHPYLFDGVEESWMQKINSQGRRDEVLKGLIMNSGKMVLLDKLLSRLRRDGHRVLIFSQMVRMLDILGDYLSLRGYPHQRLDGTVPAAVRRTSIDHFNAPNSPDFVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLLSKDTIEEDVLERARRKMILEYAIISLGVTDKQKNSKNDKFSAEELSAILKFGASNMFKAENNQKKLEDMNLDEILEHAEDHDTSNDVGGASMGGEEFLKQFEVTDYKADVSWDDIIPLTEREKFEEEDRLREEEEALKQEIELSSRRGNRPYPSSAVESPSYSGTSERKSKKQMLKDEVLLEKEIRLLYRAMIRYGSLEHRYNDIVKYADLTTQDAHVIKKIAADLVTASRKAVSAAEKDLSNDQSNNKSSRKALLITFKGVKNINAETLVQRLNDLDILYDAMPTSGYSNFQIPMHVRSVHGWSCQWGPREDSMLLSGICKHGFGAWLEIRDDPELKMKDKIFLEDTKQTDNSVPKDKENKEKKVPSAVHLVRRGEYLLSALREHHQNFGIKSSPAISTNGKTQPKKQTANRRQSGKPNVKSAQKIESATRTPSPAISESRKKPSSKDTKIETPSREQSRSQTASPVKSEKDDGNVSLNAEQKARCKELMYPVRKHMKRLRKDSSGLGRAELVKLLTECLTTIGKHIEKTVNDTPSEEKATVRKNLWMFACYFWPKEEVKYTSLISMYEKMK
|
Involved in heterochromatin silencing. Required for transcriptional repression at the silence loci of mat3, where it has a direct role as a chromatin remodeling factor.
|
O14140
|
SEM1_SCHPO
|
26S proteasome complex subunit rpn15 (mRNA export factor dss1)
|
MSRAALPSLENLEDDDEFEDFATENWPMKDTELDTGDDTLWENNWDDEDIGDDDFSVQLQAELKKKGVAAN
|
Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Acts as a ubiquitin receptor of the 26S proteasome, by interacting with ubiquitin chains linked by 'Lys-63' and 'Lys-48'. Involved in nuclear export of specific sets of mRNAs. Links the mRNA adapter mlo3 to rae1 for targeting mRNA-protein complex to the proteins of the nucleoporin complex (NPC). Involved in recombinational repair of DNA. Plays a critical role in linking repair and checkpoint factors to damaged DNA sites by specifically recruiting rad24 and cdc25 to the DSBs.
|
O14148
|
INO80_SCHPO
|
Chromatin-remodeling ATPase INO80 (EC 3.6.4.-)
|
MDPSRETFDGSTRDSYKPPNGAEMMGQSELNTQNRIPYNTSANNRNWQIPLYWQQRGNEFQASPPPPLGYVTPEYGATGTPVNANNASRVDYATTAANVPEEYANDYSSELAYIHNVNDMPHVDGLSNHSPATQPDLFETPAQSDPILFSSYPHAAQARVDPSISKDLYNMVPRPDANTVSPHAARSASSLPVPKEASETPFRDASTDLFDEHAHAAPMHSSISISTLLSDSDRYEPHVSLTENISPVMAPSIDARLSQTILRGLPPAQKLSPNSSQSQITHNRRKHKLPLNATTNNSVVLTPDTSPLLDSDEVVSDDDSNEQQTMMMKFNYLQHLRNKRDEAVHAEKRRLLDIRGSIHDRLVCRYENRYNKLHASEYNHHHDWAVRQAIREEVAAVEAAKIRADEEKKKKEREEQVRLLQESADKDAEMNEASTATSENEDLKDDLSLADLSSKKTANSQATENNNTPSKAKVKAESKVRSKAKSDKSRAKLSSDTNKDSEKNDNNDASLQSAGVASDGESSPETPLTKASKSKKAKASKLANDTSKNANGETKSTPKKSKKKTSKAQQEANSTTAEGKEKLSGDSTETGNSTNKEASTEDTKANATASAPNKKKKTVETLQQQVIKEIARKEIPRVYKIIQQNQYNRSTNARKTSQLCGREARRWQFRTIKNNKDMQTKAKRAMRETMVFWKRNERVERDLRKKAEREALDRAKKEEELRESRRQARKLDFLITQTELYSHFVGRKMDREQDLPSATNTASVSEINFDSDEEEDIRRLAVESAQEAVQKAREHSQLFDANRQQSPNNSSSDMNEGEMNFQNPTLVNAFEVKQPKMLMCKLKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSISVMAYLAETHNIWGPFLVIAPASTLHNWQQEITRFVPKLKCIPYWGSTKDRKILRKFWCRKNMTYDENSPFHVVVTSYQLVVLDAQYFQSVKWQYMILDEAQAIKSSSSSRWKSLLAFKCRNRLLLTGTPIQNTMQELWALLHFIMPSLFDSHNEFSEWFSKDIESHAQSNTQLNEQQLKRLHMILKPFMLRRVKKNVQSELGEKIEKEVYCDLTQRQKILYQALRRQISIAELLEKAILGGDDTVASIMNLVMQFRKVCNHPDLFEREDVRSPLSLATWSKSIYINREGNFLDVPYNTRNFITFSIPRLLYEQGGILSVPGLNTSRGFETKYLYNLMNIWNPEYTNDSIKSNPEGSPFSWLRFVDESPQTLFQTFQNPVVHYLDEAEASSSLKEEQLCRQEFCYGKDYSNVRKMLLLPKSITKVDVLGSDFKEDSPFYHLTHVLEESDSQLDLTLLDSVLVQRASAPPIDIYCPGSRQFTVLQSRFQRDHLWSHYLYQPLKGEEDLIINNQAVSKLPIPRKPLLPSFGIAKGSYSNVRIPSMLRFIADSGKLSKLDKLLVELKANDHRVLIYFQMTRMIDLMEEYLTFRQYKYLRLDGSSKISQRRDMVTEWQTRPELFVFLLSTRAGGLGINLTAADTVIFYDSDWNPSIDSQAMDRAHRIGQQKQVTVYRFITRGTIEERIVIRAKEKEEVQKVVISGGETRPTKQMDLKGNSREMVSWLLEE
|
ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair. {ECO:0000255|PROSITE-ProRule:PRU00746}.
|
O14156
|
PP2C4_SCHPO
|
Protein phosphatase 2C homolog 4 (PP2C-4) (EC 3.1.3.16)
|
MSIRFLKRLRAPLYIQNAYCSKNYFYRSFIQYYSPSNGPYLKISMNKAPQSLGLCTARGDSPTNQDRMAYGYLNNLKDTTNRDSPFFYGLFDGHGGTECSEFLSTNLGKIIENQDLNDTEKILKEVHSVGGYMAGLKPPFSLRTVLQSRDEDLLWRARLYYSFLQADMDYLTNYARPSPDSAVPGAVGTVAIITSKNNLSYWESDSYIIHLAHVGDTRALLCDSRTGRAHRLTFQHHPADVEEARRLRRYNMGFSRDSFGQKRFAWVANTRSFGDGYKLKKLGVVAEPQLTSIHSLRDDWSFLTLLSDGITDVVSDDEVVDIIKLSESPQDAANNIIRYAQNVGAVDDITCLVVRLPGWKKRTINDFTKNLRLEKSAYHPRRS
|
Has a role in the regulation of vacuole fusion.
|
O14157
|
MYO3_SCHPO
|
Myosin type-2 heavy chain 2 (Myosin type II heavy chain 2)
|
MSYLSKNGSNDNNNIIKKLVDAEKHCNAVKDASFDERTWIWIPDSKESFVKAWIVEDLGEKYRVKLERDGSERIVDGFDAEKVNPPKFDMVDDMAALTCLNEPSVVNNLTQRYEKDLIYTYSGLFLVAVNPYCHLPIYGDDVVRKYQSKQFKETKPHIFGTADAAYRSLLERRINQSILVTGESGAGKTETTKKVIQYLTSVTDASTSDSQQLEKKILETNPVLEAFGNAQTVRNNNSSRFGKFIRIEFSNNGSIVGANLDWYLLEKSRVIHPSSNERNYHVFYQLLRGADGSLLESLFLDRYVDHYSYLKNGLKHINGVDDGKEFQKLCFGLRTLGFDNNEIHSLFLIIASILHIGNIEVASDRSGQARFPSLTQIDQLCHLLEIPVDGFVNAALHPKSKAGREWIVTARTREQVVHTLQSLAKGLYERNFAHLVKRLNQTMYYSQSEHDGFIGVLDIAGFEIFTFNSFEQLCINFTNEKLQQFFNHYMFVLEQEEYTQERIEWDFIDYGNDLQPTIDAIEKSEPIGIFSCLDEDCVMPMATDATFTEKLHLLFKGKSDIYRPKKFSSEGFVLKHYAGDVEYDTKDWLEKNKDPLNACLAALMFKSTNSHVSSLFDDYSSNASGRDNIEKKGIFRTVSQRHRRQLSSLMHQLEATQPHFVRCIIPNNLKQPHNLDKSLVLHQLRCNGVLEGIRIAQTGFPNKLFYTEFRARYGILSQSLKRGYVEAKKATITIINELKLPSTVYRLGETKVFFKASVLGSLEDRRNALLRVIFNSFSARIRGFLTRRRLYRFNHRQDAAILLQHNLRQLKLLKPHPWWNLFLHLKPLLGTTQTDEYLRRKDALINNLQNQLESTKEVANELTITKERVLQLTNDLQEEQALAHEKDILVERANSRVEVVHERLSSLENQVTIADEKYEFLYAEKQSIEEDLANKQTEISYLSDLSSTLEKKLSSIKKDEQTISSKYKELEKDYLNIMADYQHSSQHLSNLEKAINEKNLNIRELNEKLMRLDDELLLKQRSYDTKVQELREENASLKDQCRTYESQLASLVSKYSETESELNKKEAELVIFQKEITEYRDQLHKAFQNPEKTHNINDVKSGPLNSDENIYSTSSTTLSILKDVQELKSLHTKEANQLSERIKEISEMLEQSIATEEKLRRKNSELCDIIEALKYQIQDQETEIISLNADNLDLKDTNGVLEKNASDFIDFQGIKSRYEHKISDLLNQLQKERCKVGLLKQKTENRSVTQHTLDGNSPHPSFEEKHSGDPLKRIDGNNDDRKIDNKLLKTISKSLDALQLTVEEELSNLYSLSKDLSFTDISGHIPNSIRKLEKGLSTLSELKERLNASNSDRPSPDIFKDTQAIMNSRKLLSNPNSDAQSGLISSLQKKLYNPESNMEFTGLKPLSPSKISNLPSSQPGSPSKRSGKMEALIRNFDQNSSIPDPFIVNQRNSVLQTEFEKINLKLKEATKSGILDNKDLSKFSELIQSLLKENEELKNLTTSNLGSDDKMLDFAPLLEDVPNNTRNQIKGFVEKAISSKRAIAKLYSASEEKLFSTEKALREITKERDRLLHGLQGPSVPTSPLKAPTASQLIIPNFDGSITNYSGEEETEWLQEEVNIMKIKELTSTVNKYREQLAMVQSLNEHAESSLSKAERSKNYLTGRLQEVEELARGFQTTNADLQNELADAVVKQKEYEVLYVEKSNDYNTLLLQKEKLMKQIDEFHVIRVQDLEEREKKDQLLFQRYQKELNGFKVQLEEEREKNLRIRQDNRHMHAEIGDIRTKFDELVLEKTNLLKENSILQADLQSLSRVNNSSSTAQQNAQSQLLSLTAQLQEVREANQTLRKDQDTLLRENRNLERKLHEVSEQLNKKFDSSARPFDEIEMEKEVLTLKSNLAQKDDLLSSLVERIKQIEMFALKTQKDSNNHREENLQLHRQLGVLQKEKKDLELKLFDLDLKTYPISTSKDVRMLQKQISDLEASFAASDIERIKGIDECRNRDRTIRQLEAQISKFDDDKKRIQSSVSRLEERNAQLRNQLEDVQASETQWKFALRRTEHALQEERERVKSLETDFDKYRSLLEGQRVKRSESRLSMRSNRSPSVLR
|
Stabilizes the F-actin cables forming the F-actin ring that surrounds the nucleus during interphase. May work in conjunction with myo2.
|
O14164
|
EIF3C_SCHPO
|
Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 93 kDa subunit homolog) (eIF3 p93) (Translation initiation factor eIF3, p93 subunit homolog)
|
MSRFFKGGSSDSDAESVDSSEENRLTSSRLKKQDDSSSEEESSEEESASSSESESSEEESESEESEVEVPKKKAVAASEDSESDSESSEEEEETESEEDSEVSDESESESESESESEEESESEEESDESERSGPSSFLKKPEKEEAKPAGLKFLRGESSEESSDEEEGRRVVKSAKDKRYEEFISCMETIKNAMSSNNWIVVSNEFDHLNKVSQKCKEAGRNPPPYIEFLSALDQKLESADKAFIKSLDAANGRAFNALKQRVRKNNRQFQSDIDRYRKDPEGFMKPAELNEIPKPAGKAGQDEVIVDGVATRGIVAPTEGLGKPEEITPADIFKYLRAIFEARGKKSTDRSEQIRLLEKLSTIAVTDYQRLRVKVALLAVRFDINTGSGQYMPIDQWNAALTELHSILDIFDANPKIVIVEQVEDENEEEEEAIAAAENNNGVIQVQGSVVSFLERLDDEFTRSLQMIDPHTPEYIDRLKDETSLYTLLVRSQGYLERIGVVENTARLIMRRLDRVYYKPEQVIRANEEVAWRSFPPTFDLTITPRATTTTPDILIHSLCVYLYNNGVSLLRTRAMLCHIYHEALQNRFYKARDMLLMSHLQDSVHAADIATQILHNRTMVQIGLCAFRNGMVQETQYALQDISTTGRVKELLGQGIQAPKFGQFTPDQDRLDKQLVLPFHMHINLELLECVYLTCSMLMEIPAMAAASSTASDSRKRVISRPFRRMLEYIDRQLFVGPPENTREYIMQASKALADGEWRRCEEFIHAIKIWSLMPDADKIKQMLSEKIREEGLRTYLLAYAAFYDSVSLEFLATTFDLPVQRVTVIVSRLLSKREIHAALDQVHGAIIFERVEINKLESLTVSLSEKTAQLNEANEKLYEQKTQHTNPQENRRRDKGGSVKRRNERTENRNRSDMN
|
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. {ECO:0000255|HAMAP-Rule:MF_03002}.
|
O14170
|
POP2_SCHPO
|
WD repeat-containing protein pop2 (Proteolysis factor sud1)
|
MSLSRCPTDNSSSRINSSVPLINSSSPATPPESFDPQVFPSSLIHGDNLLPQDDQIASDPRSESNSCNGNTSSSLPCTDSYQYPLKHSCTPSFLRKFNESIENVSYKCLDHSPPDSVPGDFSISLVPQRNFLYSHSSLPPKIISIDRNNRIKLDNSISSNSDNFPPSPKVDTSNTVSPGSKPISEDLEDLNLQSIVQTFEDLPEGIQSYAFFQLLRSCNRQSMRLLLNECEPLLKKDILSNLPFSIVQSILLNLDIHSFLSCRLVSPTWNRILDVHTSYWKHMFSLFGFQINENDWKYANPNLNRPPFLHNDQISDDYFPEIFKRHFLNRKRWLFPSIPPSHLSFPIHVPNFMITSLLLHKDRIITTSGSGTIQIHNAITGVLEARLEGHKEGVWAVKIHENTLVSGSIDKTVRVWNIEKAKCTHIFRGHISIIRCLEILVPSRLIRHGVEIVEPDQPYIVSGSRDHTLRVWKLPKNTDPPYLPDNTNSIDRWEKNPYFVHTLIGHTDSVRTISGYGDILVSGSYDSSIRIWRVSTGECLYHLRGHSLRIYSVLYEPERNICISGSMDKSIRVWDLSTGTCKYVLEGHDAFVTLLNVFQNRLISGSADSTIRIWDLNTGKPLMVLPSNSGYISSFVSDEHKIISGNDGSVKLWDVRTGKLLRFLLTDLTKIWHVDFDAMRCVAAVQRDDQAYLEVINFSGSRP
|
Involved in maintenance of ploidy through proteasome dependent degradation of CDK inhibitor rum1 and S-phase initiator cdc18. Functions as a recognition factor for rum1 and cdc18, which are subsequently ubiquitinated and targeted to the 26S proteasome for degradation. Together with pop1, required for cig2 instability during G2 and M phase and cig2 degradation in exponentially growing cells.
|
O14174
|
SPT20_SCHPO
|
SAGA complex subunit spt20
|
MERNNGLGDYTYRYHGKELSLDDFQNKQGIESSDDAFLSKIYENVSNFNVPRKLHDIEHKFSKEEPSLILHIHKFHFRFEQQDGAFTYNGPVKSILQYIRMELIPPDCLEVFRNSDVKFYDGCLTVRIIDHRQSPSADQTVQPQPGSTNQQQQNNTNPINNQPEDTKPNTNSPPVYHTVLRPTPETLWQDLCLLSESFANSLSDEAVLTLESNILLASEAPLFLTPAKSKAEMIQFMNQLADSAPPCTRKKPQGSAQLADEEAERLEKENLLLLMDDQRKRDFQPTFQRLQFIENVRRKRAILQQRQMQMQQQQKAQQQQSPKAQQPPAHLVQSAPVQRKTTPKIQRLPPSSIQIPPPKPMQKFPANAASSESPPNATGNFLPSGPVPANEPMLKRESVDLIKIRQLAILFQQRASQLKARGATREQITEILNRQAIAAGTDLATVMTVARNLHFQQLQMRQQQQQQQMKAER
|
Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs).
|
O14187
|
SPP42_SCHPO
|
Pre-mRNA-splicing factor spp42 (Complexed with cdc5 protein 6)
|
MASLPPGNPPPPPPPPGFEPPSQPPPPPPPGYVKKRKNKTPAQSGNLEKQLNERARKWRASQKSKFGVKRKQGYVQTEKADLPPEHLRKIMKDRGDMSSRKFRADKRSYLGALKYLPHAVLKLLENMPMPWEEYREVKVLYHVTGAITFVNESPRVIEPHFIAQWGTMWMMMRREKRDRKNFKRLRFPPFDDEEPPFSIDQLLDLEPLEAIRMDLDEEDDAPVMDWFYENKALEDTPHVNGPTYRRWKLNLPQMANLHRLGYQLLSDLRDDNYFYLFNDNSFFTAKALNVAIPGGPKFEPLYKDEAPEMEDWNEFNDIYKLIIRHPIKTEYRIAFPYLYNSRARSVALSEYHQPSNVFVPPEDPDLPAFFWDPIINPITSRQLTLHELDTSPEDSAIEEDPNFEIPFDPFFHSEDIEFEHTASALILLWAPHPFNKRSGATKRAQDVPLIKHWYLEHCPPNQPVKVRVSYQKLLKSHVMNKLHMAHPKSHTNRSLLRQLKNTKFFQSTSIDWVEAGLQVCRQGYNMLQLLIHRKGLTYLHLDYNCNLKPTKTLTTKERKKSRFGNAFHLMREILRLTKLIVDSHVQYRLGNIDAYQLADGLHYIFNHVGQLTGMYRYKYRLMRQIRACKDFKHLIYYRFNTGPVGKGPGCGFWAPSWRVWLFFLRGIVPLLERWLGNLLARQFEGRHSTGVAKQITKQRVDSHQDLELRAAVMNDILDMIPEGIRQGKSKTILQHLSEAWRCWKANIPWKVPGLPAPIENMILRYVKSKADWWTSVAHFNRERIRRGATVDKTVAKKNLGRLTRLWLKAEQERQHNYLKDGPYVTADEAVAIYTTFVHWLESRRFQPIPFPPLSYKHDTKLLVLALERLKEAYSVKGRLNQSQREELALVEQAYDNPHEMLSQIKRRLLTMRTFKEVGIEFMDMYSHLIPVYSVDPMEKICDAYLDQYLWFEADRRHLFPSWVKPSDSEPPPLLVYKWCQGINNLTDVWETSNGECNVLMETRLSKVFEKVDLTLLNRLMSLLMDTNLASYASAKNNVVLSYKDMSHTNSYGLVRGLQFSSFIWQFYGLVLDLLILGLQRATEIAGPADAPNDFLHFKDQATETSHPIRLYTRYIDKVYIMFRFTDEESRDLIQRFLNENPDPTNSNVVNYSKGKKNCWPRDARMRLMKHDVNLGRAVFWEIRNRLPRSLTTLEWEDTFPSVYSKDNPNLLFSMTGFEVRILPKIRQNEEFSLKDGVWNLTDNRTKQRTAQAFIRVTEDGINQFGNRIRQILMSSGSTTFTKIANKWNTALIALMTYYREAAISTPELLDLLVKCESKIQTRVKISLNSKMPSRFPPAVFYSPKELGGLGMLSMGHVLIPQSDLRWSKQTDTGITHFRSGMTTNGEHLIPNLYRYIQPWESEFIDSQRVWAEYAMKRQEALQQNRRLTLEDLEDSWDRGIPRINTLFQKDRHTLAYDKGWRVRTEFKQYQLLKNNPFWWTSQRHDGKLWQLNNYRVDVIQALGGVEGILEHTMFKATGFPSWEGLFWEKASGFEESMKFKKLTNAQRSGLNQIPNRRFTLWWSPTINRANVYVGFQVQLDLTGIMMHGKIPTLKISLIQIFRSHLWQKIHESVVWDLCQVLDQELESLQIETVQKETIHPRKSYKMNSSCADILLLAAYKWNVSRPSLLNDNRDVLDNTTTNKYWIDVQLRFGDYDSHDIERYTRAKFLDYSTDAQSMYPSPTGVLIGIDLCYNMHSAYGNWIPGMKPLIQQSMNKIMKANPALYVLRERIRKGLQLYASEPQEQYLSSSNYAELFSNQIQLFVDDTNVYRVTIHKTFEGNLTTKPINGAIFIFNPRTGQLFLKVIHTSVWAGQKRLGQLAKWKTAEEVAALIRSLPVEEQPRQIIVTRKGMLDPLEVHLLDFPNITIKGSELQLPFQAIIKLDKINDLILRATEPQMVLFNLYDDWLQSVSSYTAFSRLILILRALNVNTEKTKLILRPDKSIITKENHVWPNLDDQQWLDVEPKLRDLILADYAKKNNINVASLTNSEVRDIILGMTITAPSLQRQQIAEIEKQGRENAQVTAVTTKTTNVHGDEMVVTTTSAYENEKFSSKTEWRNRAISSISLPLRTKNIYVNSDNISETFPYTYILPQNLLRKFVTISDLRTQVAGYMYGKSPSDNPQIKEIRCIALVPQLGSIRNVQLPSKLPHDLQPSILEDLEPLGWIHTQSSELPYLSSVDVTTHAKILSSHPEWDTKAVTLTVSYIPGSISLAAYTVSKEGIEWGSKNMDINSDEAIGYEPSMAEKCQLLLSDRIQGFFLVPEEGVWNYNFNGASFSPKMTYSLKLDVPLPFFALEHRPTHVISYTELETNDRLEEDMPDAFA
|
Involved in pre-mRNA splicing. May be involved in endoplasmic reticulum-associated protein degradation (ERAD) and required for growth at low and high temperatures (By similarity). Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U5. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region. {ECO:0000250, ECO:0000269|PubMed:16133344}.
|
O14188
|
IQG1_SCHPO
|
Ras GTPase-activating-like protein rng2 (Ring assembly protein 2)
|
MDVNVGLSRLQSQAGAPVGTKGSNTRLAAKQRETLQAYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPPLIKSDENLSFTDEDVSIIVRRLRQSNVILPNFKALSADFMLRASPVSSRTPSPTRFPKHARFQTLNSSDSASIYSSPYTSPTLEFSKKDASARSDILKMHRRTKSATPSLEQFNEPYKQTLPSHSIEFEDSFFQPPSQKGHMQRSFLTTFSAPTRRREALFSTTSGLSQRSPVDEKIVNAIQACGRGVLVRLRLVDMLQSLVEQSSSVVLLQAVIRGYISRNTYRIRKKAYDELVNWVTSIQSISRAYLIRAQYRKVVLQEEATKSIQTLQSIIRGGFYRRKYHSLIERLDLFTPSFVLIQSSALGFLTRHAIVNMLDNLYNYIPLFNRMQSILRANMFRNEWSNFLDSVQSFPVSFHSICKGRLIRDSINRLNGSLLGELDNFIKLQNLSRGFMIRRAFKEKLEKLKASTSSFIALQAIVRAFLLRKNLESIYDSFQKSHLSVIKAQSLYRGFITRTKIDYCNDYLLKRLPDIVFMQSAVRAILLRDDVNYTEVQLDSFIPEIVLLQSLIRGYLSRNKFSRKLQNFHKNMENPIVAKSIFRGRQEGLAYRELATAKNPPVMTVKNFVHLLDDTNFDFEEEVLLEKMRKEIVQQVRDNEEIEVHINELDVKIALLVKNKISLDDVLKHHNKYKFGKQSTEYLKINTLSMKSLNNSSRKFLELYQCFFYVLQTNEMYLANYFQALKTEGTSSVKIRHAVYLVLQIFGHGSNRREEVLLLRFISQVIKLEAALVNSSQDLLSDDCVWKLLFTGYRGDVREVKLWKTILGRIHKVLVADNHLDFEINPLTLFKSFNPEVASQTDSPKLTLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVDGSITALQRKNLYTLSSILSEIFSIESCDSKQLGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPPDVNDPLRAVVNSLGPVSEQDNDFVQDETDVKLELNPKFCTIENPVAQERTLIVQTKRYILFIIRIQNGLNLLEILVKPVTDSDEAAWQNLLAEESEKNARNYDLFDDSIFSMSFAELKYTALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYIEQAMETLQSKKGKKKLIPFSKQYFHMRDLRKSGRVPRFGSFKYPALKLYDRGVLVSISHMPQKEKLYITISADEVGKFILEATSPTVKVSSPRCELHLDDLLSAQYNKVLTLDVLDGRLKLNTNMFLHLIFSKFYS
|
Component of the contractile F-actin ring required for its construction following assembly of F-actin at the division site.
|
O14194
|
GGT2_SCHPO
|
Glutathione hydrolase proenzyme 2 (EC 3.4.19.13) (Gamma-glutamyltransferase 2) (Gamma-glutamyltranspeptidase 2) (EC 2.3.2.2) [Cleaved into: Glutathione hydrolase 2 heavy chain; Glutathione hydrolase 2 light chain]
|
MSPTDTTPLLYSWDDQSRHQDPDWHKLRNYHGAWYRRISRRRFSQFIFAFGLMTLFVLVYSISSNLHTPTQFTGHKVRGRRGAVASEVPVCSDIGVSMLADGGNAVDAAIASTFCIGVVNFFSSGIGGGGFMLIKHPNETAQSLTFREIAPGNVSKHMFDKNPMLAQVGPLSIAIPGELAGLYEAWKSHGLLDWSKLLEPNVKLAREGFPVTRAMERVLKLPEMAHLLKDPIWQPILMPNGKVLRAGDKMFRPAYAKTLEIIANKGIEPFYRGELTNSMVKFIQDNGGIVTVEDFGNYSTVFADALHTSYRGHDVYTCTLPTSGPALIEGLNILDGYPLNTPSLAFPKRLHLEVEAMKWLSAGRTQFGDPDFLPLDHLDVVSKLLSKEFASQIRNNISLSKTYPWEHYNPSYDLPISHGTTHVSTVDSNNLAVSITSTVNLLFGSQLMDPVTGVVFNDQMDDFSIPGASNAFNLSPSPWNFIEPFKRPQSSSAPTILTDINGDFEMALGASGGSRIVTAVLDSIIKRIDMDYDIESMVASARPHHQLLPDILILESGFSKSVATRMKKYGHKVWRLKQHDTPLSQIQAVTRHHSEYYGMSDPRKYGQAAAY
|
Catalyzes the transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH. Plays a role in the turnover of the vacuolar GSH, serving as an alternative nitrogen source during nitrogen starvation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15920625}.
|
O14213
|
EPR1_SCHPO
|
ER-phagy receptor 1 (Meiotically up-regulated gene 185 protein)
|
MNNPFKDMDCYEILQVNHDSDLQEIKANYRKLALQYHPDRNPGIEDYNEIFSQINAAYNILSNDDKRKWHEKDYLRNQYSVQIEDVLQHLQTIEKIPFESTSAFVERLRQDEKIAGSTDDLPTLGDTTWLWTYAKPIYQKWLRFSTKKSFEWEALYNEEEESDAATRRLMKRQNQRQIQYCIQRYNELVRDLIGKACDLDPRRKNVVKLSDGERYNSLQEASRKQSERDRRQYQETFKNQSIASWTIIDQEETSSDDESLSKEIVNSNPIMCMVCNKNFRSQNQLENHENSKKHKKNLRKMNQEIKKHAKEAQKNAESNKQPEDAPSESPYSNKVSSSDFYTRSFEEIEKTFTFVEISDNEFYTASEDGFLNEDDKLDQD
|
Reticulophagy receptor required for autophagosomal sequestration of endoplasmic reticulum (ER) membranes during ER stress (Ref.5). Confers resistance to ER stress by promoting the autophagic degradation of the ER (ER-phagy or reticulophagy) (Ref.5). Acts as a bridging molecule to mediate the association between atg8 on the autophagic membrane and the vesicle-associated membrane protein-associated proteins (VAPs) scs2 and scs22 on the ER (Ref.5). May play a role in meiosis.
|
O14214
|
TRM10_SCHPO
|
tRNA (guanine(9)-N1)-methyltransferase (EC 2.1.1.221) (tRNA methyltransferase 10) (tRNA(m1G9)-methyltransferase) (tRNA(m1G9)MTase)
|
MENKDALDIGKDDTNTSEADVSKNETQEQPVLSKSALKRLKRQQEWDAGREKRAEMRREKKRLRKEERKRKIEAGEVVKSQKKRIRLGKVVPSSIRIVLDCAFDDLMNDKEINSLCQQVTRCHSANRTALHPVELFATNFGGRLKTRQDFVLKGQQNNWKRYNPTTKSYLEEFESQKEKLVYLSADSDNTITELDEDKIYIIGAIVDKNRYKNLCQNKASEQGIKTAKLPIDEYIKITDRKILTVNQVFEILSLWLEYRDWEKAFMEVIPKRKGILLKSDESFDVSEDTRSQSNQSDSELEKEN
|
S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
|
O14215
|
PRI1_SCHPO
|
DNA primase small subunit (EC 2.7.7.102) (DNA primase 1)
|
MTVQIDELDDKDLDEIIANGTLDGAKQGAVDSETMIQYYRHLFPWKYLFQWLNHGPVVTNDFAHREFAFTLPNDAYIRYLSFSNWEELKKEALNLCPSRFEVGPVYSANPRDRKTIRKSTFHPLKKELVFDIDMTDYDDVRTCCSKTNICEKCWPFITIAVQVLDICFHEDFGFKHILWVYSGRRGIHAWICDEIACSLDDRSRRMIASYLQVVVGNPQGGVRLINNLKRPLHPHLTRSLNILKSAFVKIVLEDQDPWASKEGAENLLKLLPDKDLASALRKKWEVDPERSSKNKWSDIDTVLASGSIASISPSVIAIAKQDIVLTYLYPRLDVEVSRHLNHLLKSPFCVHPGTSRVCVPIDIERMDSFNPLKVPTVNDLLQELDKNSQNDNGHGPTMETNTTENQKDNARGQSNKGHGFSTSLNPYTLYFKSFSSQLFKETVGNKRKHENLEF
|
Catalytic subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex - primosome/replisome) which play an essential role in the initiation of DNA synthesis (By similarity). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit pol1, an accessory subunit spb70/pol12 and two primase subunits, the catalytic subunit spp1/pri1 and the regulatory subunit spp2/pri2) is recruited to DNA at the replicative forks (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands (By similarity).
|
O14216
|
SLD2_SCHPO
|
DNA replication regulator sld2 (DNA replication and checkpoint protein 1)
|
MHDESRTKQISSIKALLKKWEHEYVHTNNCKPSKEDVKKQPEIALLYKQYYELKRESSITPKKAKTKVDFKFQTPTKQRAETEANESPKAPRNDYLQVTPKTVDKSLLGPTPQLSRRVLNLLEDMSPIADSHVDQISDIKHNTSEISSTMIPTTPSKNPEPVAQHTPTVLETPSSYRLQVYTSPNLLRVNAPCRKSLSEMLRELKDIEDDYGSNEEKILQEFESFSSSSSESLVDRDISQPMKKKIKRQNRLVKLPPSMNLSKSHLEGLPEIDEDAENGIDDNEDTTASKDSSPFLDLQSERQNKKIMRNGLVIGKQVSQNYSSYKLKKRKFRRHRS
|
Has a role in the initiation of DNA replication. Required at S-phase checkpoint.
|
O14222
|
FSV1_SCHPO
|
Syntaxin-like protein fsv1
|
MSNLLLIIDSVSQKIRDRRKLEEFGQNPDEEIESSLKDVRQELQKLNEEQSRLEKNAQIPEYRVRESEAFLIRMQRRLESAEEEFEKQRRASSIPADGTSAFSANPQVASTNNKLTPLPSLQKTTSSSEGSDIEMEAMYPVDGNDPDPINVNVLAQMHQQMLNEQEESLGGIEASVQRQKRMGYAMNTELSEQNVLLDNMNNDADRIERRFDHAKNRLNKVSRKAKQYPRCFIILLLCALLLLVASI
|
Involved in vesicle-mediated protein transport between the Golgi and the vacuole.
|
O14227
|
RDP1_SCHPO
|
RNA-dependent RNA polymerase 1 (Protein rdp1) (EC 2.7.7.48)
|
MAVSLNDFISVKLKRYSRESPWERLRVPYRNKKQKKWASVHNNEAQLHSANKRNDNCLIQRSSTWRLGDMITLVIKDIPVTWLSNEGGKLYNLWEPLHDYGTIEFMKINEPLNGQTSTTAIVQFAPPPKVPFWEPNGKINVKGVDLAVQIDITAHRSHISRQVFSKNSFRSDQLVKIPLSSFKLGQVYDERIVPLFGVDCGITVTESNLLVYFNFKKLCVLFDASFDKQIETFRLDFDFHSIIGDVGTDYYDDHISLVFRFRFSPLIFRKSKNATESRVQTFWTASHLWRRHYDILPFNVSPTTASPIELLNCHNAPIGRCNVLVLSFSIRDESDKDDIAFLLHNLEKFNLKSQLDKVVFHLVPDYKHRCSLINDKEIEEEIAYLLQACLSKNLLSEIDLPIILANLKKLSKERAKKFLRLILTSKTALINPSELDFTKSFVFYDLSSASSIHIKKLYVTPTTLRIVEDSLEAGNRVIRNFKDFANRFMRVQITDEYYKQKIRGGSDGFRNEKLYSRIQQLLTYGIKVGNQIYEFLAFGNSQLREHGAYFFASGSDLNAKQIREWMGDFSEINSVSKYAARMGQCFSTTKEINRFCVDISLQDDIVRNNHCFTDGVGMASLSVIRRLSLEVKNHDMFPSAFQFRMGGYKGVLSLAPPTKLEYHQGNLVFPRRSQDKFKSFHSTLEVIKISRFSNAHLNMQLITLLEGLGVEKTVFLELTRSQLSKMNESINSKQKSILMLRDNVDEYHSTLIIADFIQAGFLERDDAFTENLLNLYYEWVLRLIKEKQKVSVPKGAYLLGVADETGTLKGHYDDAVLSVPEIFIQITDTSTSFGSYSTGKLKTRVIVGLCIVARNPSLHPGDVRVCKAVRCDELMHLKNVIVFPTTGDRSIPAMCSGGDLDGDEYTVIWDQRLLPKIVNYPPLLESSPKKSIDFLEGKPLIDSVKEFFVNYIKYDSLGLISNAWKAWAHDHDNNPEGIFGNVCLELAEMHSKAVDFAKSGVACKMQAKYHPKRYPDFMQKTKTRSFRSETAVGKIFRYAARFQRESGRPATYNPIMNTVYDPCMKLPRFKTEYLNVAEEVKKHYDNDLRSIMARFDISTEYEVYTAFILFKDDLAKTVNEYGLREEVSFQFDLLKKKYTQEYLEKCALSNQSAFDSSEYEERINSAVAATYDVTYDQRVKSVGNGTTEVLISFPYLFSSRLCQLSRKAMLTANNF
|
Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation, accurate chromosome segregation, centromere cohesion and telomere function during mitosis and meiosis. Required for both post-transcriptional and transcriptional gene silencing. Required for silencing at the centromeres and for initiation of transcriptionally silent heterochromatin at the mating type locus. Promotes histone H3 'Lys-10' methylation necessary for centromere function. Required for recruitment of swi6 and cohesin to an ectopic dg repeat. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediates their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA. Its RNA-dependent RNA polymerase activity is critical in siRNA production necessary for heterochromatin formation.
|
O14230
|
ERG20_SCHPO
|
Farnesyl pyrophosphate synthase (FPP synthase) (FPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Geranyltranstransferase)
|
MSAVDKRAKFESALPVFVDEIVNYLKTINIPDDVTEWYKNSLFHNTLGGKYNRGLSVIDSYEILLGHPLDEAAYMKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMPGVGNIAINDAFMVESAIYFLLKKHFRQESCYVDLIELFHDVTFQTELGQQLDLLTAPEDSVDLSKFSLQKHSFIVIYKTAFYSFYLPVALAMHLAGVATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGKIGTDILDNKCSWIINLALAKCTPEQRVILDDNYGRKDSESEKRVKAVFEELNIRGEFENYEESEVSEIKKLIDGVDESTGLKKSIFTTFLGKIYKRNK
|
Farnesyl pyrophosphate synthase part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway. Fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8. The diphosphomevalonate decarboxylase mvd1 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
|
O14232
|
MTR4_SCHPO
|
ATP-dependent RNA helicase mtr4 (EC 3.6.4.-)
|
MFGGELDDAFGVFEGKVPKSLKEESKNSQNSQNSQKIKRTLTDKNASNQEQGTKKLESSVGEQESATKRAKIENLKDNQDLIPNNDVNGIHINNSAVADTKHKPKIGDIAADDISNEVSIKNEGDTIPEATVADSFEQEASLQVAGKVGMTEAKSSTEEVVELRHQVRHQVSIPPNYDYVPISKHKSPIPPARTYPFTLDPFQAVSIACIERQESVLVSAHTSAGKTVVAEYAVAQSLRDKQRVIYTSPIKALSNQKYRELLAEFGDVGLMTGDVTINPDATCLVMTTEILRSMLYRGSEVMREVAWVIFDEIHYMRDKERGVVWEETIILLPDKSHFVFLSATIPNAMQFAEWITKIHRQPCHVVYTDFRPTPLQHYLFPSGSDGIHLVVDEKSNFREENFQRAMSALMEKQGDDPAAMATKGNAKKGKTGKGGVKGPSDIYKIVKMIMVKNYNPVIVFSFSKRECEALALQMSKLDMNDQTERDLVTTIFNNAVNQLSEKDRELPQIEHILPLLRRGIGIHHSGLLPILKEVIEILFQEGLLKVLFATETFSIGLNMPAKTVVFTNVRKFDGKTFRWISGGEYIQMSGRAGRRGLDDRGIVILMIDEKMDPPVAKSMLKGEADRLDSAFHLSYNMILNLLRVEGISPEFMLERCFFQFQNSLEVPKLEAKLEESQQHYDSFTILDERPLEEYHTLKTQLERYRTDVRTVVNHPNFCLSFLQGGRLVRVKVGNEDFDWGVVVNVSKRPLPKGQSNEYLPQESYIVHTLVMVASDTGPLRIRSGHLPEVHPPAAEDKGKFEVVPFLLSSLDGIAHIRVFLPNDLKSQGQKLTVGKALSEVKRRFPEGITLLDPVENMNIKEPTFIKLMKKVNILESRLLSNPLHNFSELEEKYAEYLRKLALLEEVKDLKKKLSKARSIMQLDELNSRKRVLRRLGFTTSDDVIEVKGRVACEISSGDGLLLTELIFNGMFNDLTPEQCAALLSCLVFQEKSEVENQRMKEELAGPLKILQEMARRIAKVSKESKQELNEEEYVNSFKPSLMEVVYAWAHGASFAQICKMTDVYEGSLIRMFRRLEELIRQMVDAAKVIGNTSLQQKMEDTIACIHRDIVFSASLYL
|
Component of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates (By similarity). Required for heterochromatic gene silencing at centromeric repeats by either exosome- or RNAi-mediated degradation of heterochromatic transcripts.
|
O14243
|
SNX4_SCHPO
|
Sorting nexin-4 (Autophagy-related protein 24)
|
MSDSVNLDEPSTNSTHFLQCLVTEPRKELQGSRDTHVSYLIITKTNLSIFTRAECKVRRRFSDFVKLQEILSRMNEDCVVPPLPAKHKLEYIKGGRFSDNFINRRAKLLNRYITRCALHPVLHQSPHFIAFLENPNWNNYVRFFIQPKLNNTSKLDEISDSLLNAFSKLKEEPTEFDIQRDHVQQFMFGISNLEGSIQKLLRLEKALESDYEDVSIQFDRLASLDQALDVPIESIQNALQQTGTEYANLTEKLTLLLDTIKDVESYAHSLKELLKRRDQKQQDVEALQEYSAKLSLERDKISSGGSNGFSLSKTLDDLRGIDHNDTRLKRLEHVQSELQAVEQAIQEASAVHDAFNQRVREESKLFDSVRQSEMLSAISDYANVHVEFFTNIRDLWIRVKQ
|
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.
|
O14246
|
TPZ1_SCHPO
|
Protection of telomeres protein tpz1 (Meiotically up-regulated gene 169 protein)
|
MSNCLKHPWLENGLLNLIKNADVLPIRVFKCQPLQIFEYIRYEHPIRCKLSDTEFYIEAEFSSQSISDLNNFTEKRITSLRGGIVTLGNFLIHLIPSQSGIIPWIQVESFNFQGCEGAVFGNPKAITTSALFNALLQSPYLAALANEFNRSIKEGSSYQEASLSQQEKPNDNTSNSRDIKNNIQFHWKNMTSLSIEECIIPKGQQLILEKESEENTTHGIYLEERKMAQGLHNSVSETPEVKQEDNDEDLDAYSWSSSTDSAGEIPSLPTNRKILEKIAEKPPPFESPLEDDETPDQTNEHEANQVNVSQLPLNPRGSGISGRPVESTEQLNSSLTIERSQSIQSTDSKQRVETQSHRRSKIEIFDAQDELFDRSICTTIDDSTGKLLNAEETPIKTGDLHSTSASSVISCTPPAINFTSDICNEQIELEYKRKPIPDYDFMKGLETTLQELYVEHQSKKRRLELFQLTNNHQKNSEACEMCRLGLPHGSFFELLRDWKKIEEFRNKS
|
Telomeric DNA-binding protein that is required to protect the 3'-end telomeric overhang and involved in telomere length regulation. recruits poz1 and ccq1 to telomeres, regulating telomere length negatively and positively respectively.
|
O14261
|
ATG11_SCHPO
|
Taz1-interacting factor 1 (Protein taf1) (Autophagy-related protein 11) (Cytoplasm to vacuole targeting protein 9)
|
MRFRLNDSFSGKSWTIDNVQWTPQNLVAWIMELNIGLSDEAKLLLPNGMSLNETVLNSESDVVIYVLDQNLLTFTYDGDKIPSIPSLKGQPISNVLTGIIADSSSDQWKDKISKCLSLLSDILESSSKIHNQLSVCHDEYSTSIVSPEVAMNYLQRRQSGMKDLLFVFYERLDRVSVSDLLHDFLALPTGSLPITPLKILSTNWTKLDSWLNSISARYAEAQKRVQQCIGAANSIIVSPFKEVPSIKEGDDAYYHLRSVAQDAANILQEILKIESTSTTSQIKPKCNYETEITDCMEKLQSNLSELKSSRKSSLISLKSFWLSFYKVSLRYDALYEYLRQIAEELDRSKFVLSQSRNIFSLYIDILMEALRRTEWQESYNVSHDSSLPLDQEKELSLRKSWLSHFSNLLFNHGQLKYLPVLTRDEISNYLLNIQAHPNYQTFHQMLSNRLSEYLGFPGSPREAVSNTVQANNSLHEKLAMYQNRCNNLEAMLSHQNGFNYNINNDGLSPNAPHPPINEQSNSSQPFYRVSPSIVPLNVIRKLTNRKTSFTDSHILRLQDEVNQLRNELDLVNKRNEDLLIELQGKEEKIQYLETENEEVLQKYENLQEELSSTRKLLTKNEAAVAEQQSNEEMHSNEPNILNLYSVFEGKVDSLQELYNAFKLQLTSLKQKGEYATLAKDAEAVQHIIEERDYALAEKADLLKLSENRKEQCKILTQKLYTIVFRCNELQSVLRECVTQPGFDSDNERDGHASIPDRQIEFNSKDLQYLYWMDGEDADRNFQEFLNRMSSLDFDSFHNFVVSVLTQAHNHELRWKREFQSNRDKALKAILDSQSKVSLRNFKQGSLVLFLPTRRTAGNKKVWAAFNVNAPHYYLNTQPHLKLESRDWMLGRVTSIEDRTADDSTDKWLRLPSGTIWHLVEAIDERF
|
Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the preautophagosome (PAS), the site of vesicle/autophagosome formation. Required for atg9 anterograde transport from the mitochondria to the PAS (By similarity). Required for nitrogen starvation-induced sexual development and for entering the dormant G0 state (By similarity). {ECO:0000250, ECO:0000269|PubMed:11270572}.
|
O14283
|
PRR1_SCHPO
|
Transcription factor prr1 (Pombe response regulator 1)
|
MPSSNGSSDFVRKLFNMLEEPEYRHILRWSDSGDSFIVLDTNEFTKTILPRHFKHSNFASFVRQLNKYDFHKVRHEEGAPSIYGEGAWEFRHDDFQLHHKDLLDNIKRKAPSKRNLANENTAPVIENLKQQVDSILDFQKLLDRNLSGLATSYQTILLKMFELKRGIESRDLLMSSIISYLCDLEGSTQRQANPGAMFVPSHPLQELLNAYQALAKGQVATTSPQQIPNQIQQASAATTASSKMTVDTNLGTAQPSLYNTPSSDYELANQEKPADSMASAASLNTPLSSNDHSLNPHAHGSYPMYEKFQPIQHPNPGSFTTHLDSNASMAKSFSQISNDSLAKASSVATSMSQMGAAVPTTGLWKRQPRILLVEDDELSRRMTIKFLTSFDCQVDVAVDGIGAVNKANAGGFDLILMDFILPNLDGLSVTCLIRQYDHNTPILAITSNISMNDAVTYFNHGVTDLLVKPFTKLTLLQLLKKQLLNLLQADNSINMSDVPSTKEAKDDKAPVTFYLENDAPMYPQQMLQDPIQADLQHPH
|
Involved in oxidative stress. Transcription factor that acts upon trr1 and ctt1.
|
O14285
|
SPC34_SCHPO
|
DASH complex subunit spc34 (Outer kinetochore protein spc34)
|
MSDLLNYLQSIAATSEKLLEPENPNAARFTDAVLHTHAITDLIRDTQKEELIAAEFKSLPKDWSERLASENPADYVACIEELLDIYPMQGGREYLETLVEKYNLHMSGIENLENVLLEQKEQLQQLEKRQTDQVSARENILQRETSEIQRLEREIEKVKQLIQS
|
Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore.
|
O14295
|
PLR1_SCHPO
|
Pyridoxal reductase (PL reductase) (PL-red) (EC 1.1.1.65)
|
MPIVSGFKVGPIGFGLMGLTWKPKQTPDEEAFEVMNYALSQGSNYWDAGEFYGVDPPTSNLDLLARYFEKYPENANKVFLSVKGGLDFKTLVPDGNPDFVSKSVENVIAHLRGTKKLDLFQCARVDPNVPIETTMKTLKGFVDSGKISCVGLSEVSAETIKRAHAVVPIAAVEVEYSLFSRDIETNGIMDICRKLSIPIIAYSPFCRGLLTGRIKTVEDLKEFAKSFPFLEYLDRFSPDVFAKNLPFLQAVEQLAKKFGMTMPEFSLLFIMASGNGLVIPIPGSTSVSRTKSNLNALNKSLSPEQFKEAKEVLSKYPIYGLRYNEQLAGTLSV
|
Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
|
O14299
|
WIS4_SCHPO
|
MAP kinase kinase kinase wis4 (EC 2.7.11.25) (MAP kinase kinase kinase wak1) (MAP kinase kinase kinase wik1)
|
MGLEHTFYPAEDRFEPLLEHSEPVNFVPKENAKSYVRQGFASPHQSLMDNLVDSTESTKRSENFVSHIPLTPSHSGQSEKLMSTRTSHSPYISPTMSYTNHSPANLTRNSSFNHQHYSTTLRSPPSMRGRGIDVNSSHYPHISRPRTSSDSQKMYTRAPVDYYYIQENPYFNNIDQDSISDKSLPSTNQSLHHSEEDTESDNDFSESIHPEFDIDVFYKVSNILYDESDLQDPEKRERLEWHSMLSSVLKGDVMQTEKRRLRLTEPDGHSGTYISEVWLGLQAWLHGRLNADQAEVIRKSREGVEPVLREVIDFQIQDEETTKPPLEQVTEILEKVEQCKQFYISSREMEENVPLSASKEFNYKLNALISWSNVMESIQVETLVLQKWVGNDEFDLTMRTPQFNYDGVENTSSFVERIFRQSGLQRTFEQRTLTTLNRIIHQAKQTISENAQAFEEMKLPTYEDKLLPLVRFPIKLLEEALRLRLAYAKKIKGPNFLIVDSMLDDFKIALSVAVRIKREYIKIASPSPGWSLPTNVDEDYDNVLLDSLKFYFKLLTLKLSSGNKNLYFKEIDFLENEWAFLNEHIYWINGGDIHMAGQFSYLSNSLLLNVHRYVESHLNGPTERTAASLTNWYSTLLKNTQIRFRKILRFSETLNSRFENASDFVISEGHLPDLVNRLSTTGHFLAYTANLERDGVFVIADHTLSENPEALKALLFSKDISNLETIQQNCSYVLILCPVHPIVWKGRIEKVDVPDFSVDLKTNRVRIIASNKREHLQAAKSVFQSISGDLVTLAVECRSSITRVYKEFIRLSKLCMRISSTVVDCVSAVREACSGVNCHDLIYHVFSFAAEFGQRILRFLSFDSYWQTKLKRKITSLAVEWISFICDECDLMDRKTFRWGVGALEFLMLMIRGNNILLIDDAMFLKIREKVGKSMAFLLTHFDVLGAKSKVAAKLQRESTEVSSSPRLTSFGDVEEEALSIQLLQKETMLRIDELEIERNNTLLERLAIGHVLDDSVFRNRDFIKLASSFSNITIRWQQGHFVRSGMFGDVYTGVNMETGDLLAVKEIKLQDSRTFRSTVDQIHNEMTVLERLNHPNVVTYYGVEVHREKVYIFMEFCQGGSLADLLAHGRIEDENVLKVYVVQLLEGLAYIHSQHILHRDIKPANILLDHRGMIKYSDFGSALYVSPPTDPEVRYEDIQPELQHLAGTPMYMAPEIILGTKKGDFGAMDIWSLGCVILEMMTGSTPWSEMDNEWAIMYHVAAMHTPSIPQNEKISSLARDFIEQCFERDPEQRPRAVDLLTHPWITDFRKKTIITMPPATITKKTSLSHTITEEKTAQLLAGRHDDSKAETDSLAASYKEESALPVASNVGLRQPNELRIDSINLPPAIVTPDTINYSVD
|
Involved in a signal transduction pathway that is activated in under conditions of heat shock, oxidative stress or limited nutrition. Unlike win1, it is not activated by changes in the osmolarity of the extracellular environment. Activates the wis1 MAP kinase kinase by phosphorylation.
|
O14302
|
CYK3_SCHPO
|
cytokinesis protein 3
|
MSIPKQLPCMVRALYAWPGEREGDLKFTEGDLIECLSIGDGKWWIGRHINTNTQGIFPSNFVHCLDIPTVRPGSSMSRTSASSFRYSSPQKSSIDTPITSSDQGLTPDLVGSSNALNKPTRESDSLKHQKSHPMLNSLGSSLSLKKSVSRPPSSMSRTNLDVSSRWDNTADNDSQIDAQDLSRSTPSPLRSAMENVLQSLNAMGKKSFSRANSPLLRLTKSTTTSKETDFIPVPPAHGSTSMTSRSKLDDSTDNSSKPRTSLQPGESPMKSSRDISRKPSMASSVLSPSDYFPQHRRFQSAPAPIPRPVSTLIPLTQVRTTASNVIKPRPQTTERPSTAQSFRKGGGFLKKTFKKLLRRGSSKRKPSLQPTPPVSYPAHNVPQKGVRPASPHTLKSVKDDLKRTKTYTKAEFAAKREEIFNKLSMPVYEPLKDLSECIGNVLADGEPVQFSVGTNIHNMNFSAIDKQIRSIIPQRVQVSPAVLAKNYLAPGQTTALAQMRAVFIYISERITFTNQTLDNDELRTSTQVISEGQGTPFEVALLVKEMLQALDLWCEVIEGYLKSPDDIYYTRDININHAWNVVTFDNEVRLIDASFASPTHPQQALKSSSSNDFYFLMKPNECIFTHVPENPDQQFIMPDLSMPIVMALPWVSSVYFTLGLKLRKFNTSILHLNDLEVLQIEFLAPKDIECVAEVDALSALAPTADVSQCYKYTLTQAFWETPDIRVMRVKAVMPANNRAAVLRIYAGRLGVSSPVRTAPHPMAMSLPFVHHGKNKALEFVTRHPVPHCPSVDLYINSPQCGTLHSGVEYKFNVSAYACQPSTSISNTRLAIQTPTGNIVRLREERSGNGVIFFSLSLTINETGEYRALILAEKIGRWVVYATWQAV
|
Involved in cytokinesis.
|
O14305
|
SID1_SCHPO
|
Serine/threonine-protein kinase sid1 (EC 2.7.11.1) (STE20-like kinase sid1)
|
MYPLNANSYTLLRKLGSGSFGVVWKARENVSGDIIAIKQIDLETGIDDITDIEQEVFMLSNCNSSNVIQYYGCFVDGYTLWILMEHMDGGSVSGLLKMGRLNEQVISIILREVLYGLNYLHGQNKIHRDIKAANILLSSSTGNVKLADFGVAAQLSNAASRRHTFVGTPFWMAPEVIQQTSYGLAADIWSLGITAIEMANGIPPRATMHPMRVIFEIPQSEPPKLDDHFSPTFRDFVSCCLDLNPNMRWSAKELLQHPFIKSAGTVKDIIPLLVQKENKLFDDSDQSVLEETINNTLKPFEEPIAEGNADIEDWTFETVKKSDSTVLGNTSIPKNSIISSQNKEELPSSIKYLEKTIMSDQATPHPFSKSLSEKGSSYHKSLTSDFAMKHYIKSTIRSMLLNDKLSATQRSSLESFYTSFISLDKNLSSKFVNQITPDNRLHHKKQKRSPISQLLFSRWLEETEKRRSLNG
|
Has a role in the septation initiation network (SIN) required for cytokinesis.
|
O14310
|
NP106_SCHPO
|
Nucleoporin npp106 (Nuclear pore protein npp106)
|
MESKEAKEKGVNTSDSKGSQIESSISDLREKSQHLFGVLLEPQVPVIQYGLNQLEEKARNLESKVLLTRDGDTKAHYLLAESGMNAEQTRQKIYSIHIHSPWDQLELDKKSLYEQPHTKLYNGQNVVASIENGYQSNVYEFQLRLMKNNGIAWENTKTEFMEDVGKLLHSKDNSGLGTSISMSLRPNLARPLLTASSVKSQSVRSLREVGSNLPIPTGSLTKIDGLNNQLSNDLTRSQTTNIFGFAEKASSFAAAVHKLNEARIRNQACHVWSLFASVSQMVNTEVIQLFDAWSLLAHMIDETRYGMGDFEARHLALDSSSAALAVEKNCIEGSLKYLENQFLSLIDLHLSDAGHITTVNSVEKVIAYSKLRFYKNGSWIKSTVSVVNDVPLWVVLFYLMRSGQLDAALQFVNTYSDDFEKLGRSFPLYFYSYAKNPSLPLPKQLRDRLQAEYGQLMKYAPEDPFKHAIYKLLGNCEPHRVSLPEVCVTSEDYMWIQLMFCRVNQNDVIDSNGGQSTNSLFNLYQLEKKIVAFGPRYFNPKNNTPTNYFLALLMCGEFERAISFLHTNYPVEATHFAVAMAYYGLLRTKNYEKNENILIYEADDVKINFPQLIIAYLKHLEYVDAAVYLDYIACIPLVPAYQACSINLTKILLLQSHEFSKFLGDIKPDTERTTGLLDLYLRLIPFDHDSLQKLYLEGAREADDDGRFGDSIILYHLLGDYDTVIGVAIKNLSQSIVSRGLWSIDSKESKNMHISSNVVASEAPDALAANLLAMYESNPKKSAKVSATNKKALKVLLKVVKVQKLYGQEKWDEVLQLIEHLDLLPINEVQAEFEPNEQIPPISARLRRRAFEFSTFQDEVLSVIPSLMYISMSSIKALYRTISKLPVVNEESKKKLQRLQFKGSMLVMFSTMIESRLSPQILEYLQAEQLTLL
|
Has a role in promoting mRNA export from the nucleus.
|
O14313
|
PMP20_SCHPO
|
Peroxisomal membrane associated protein 20 (Peroxiredoxin homolog pmp20) (Prx)
|
MVAVGSTLPKVTLWENKPEEVVEFPSQGKFIIVGVPGAFTPPCSSQVPGYIANEKQFAAKGISGIYVVAVNDVFVTKAWKKSFDGGEQSGVHFVADWNGEFTKAFDAGFDASGLLGPLRSKRYAAVVENGKVVKVFIENEVTDVDISSADKVLSSL
|
May act as a chaperone rather than a peroxidase. Has no thioredoxin-dependent peroxidase activity. Shows weak chaperone activity.
|
O14333
|
PSD1_SCHPO
|
Phosphatidylserine decarboxylase proenzyme 1, mitochondrial (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 1 beta chain; Phosphatidylserine decarboxylase 1 alpha chain]
|
MLKFHRNVKPQFGAFARYSSLGKHNSRKRVGIIRLAYGLTGIGLVGLAGFAWAQDRHEKTYQKKGVQVEGPWQFYVLTTLPLRTLSRWWGYVNRIEIPLWMRVPAFGLYSKIFGCNLTEADPDDVRQYKNLAEFFTRKLKPGARVIDPDAPIVIPADGKILNYGVIEGGQLEQVKGITYSLDALLGDEKLARLKRSHAIPSPDHIPHIRQEEFAKLNGIHYSLQDLMGHDHGERPSHVKDASAQHIDLLSSTKVAAKSQFTLFGSRETNCLYYAVIYLAPGDYHRFHSPTDWVVERRRHFSGELFSVSPFMARRLGNLFILNERVALMGRYKYGFMSMIPVGATNVGSIRIKFDKDLCTNQFGKLGPVGTFDEAVYTSSSSILHGHPLLRGDEVGNFELGSTVVLVFEAPADFEFLVKQGQKVRVGLPLGRVVPSSH
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Together with psd2 and psd3, responsible for the majority of phosphatidylethanolamine synthesis. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:19286980}.
|
O14343
|
KLP5_SCHPO
|
Kinesin-like protein 5
|
MSRQSSITVTVRVRPFSTAESANLIASSDRLSFGTSSSLRNPGSGRQIRRVVKVLDGRVLVFDPPDETTATLSATNRRLSTSQQSLARLSRKSNNSAGFGRDLRYAFDRVFDETATQQQVYERTARPLLDNILDGFNATIFAYGATGCGKTHTISGTMQDPGLIYLTLKELFERMDHLRDEKIFDLRLSYLEIYNETIRDLLVSPTPNQAKPLNLREDADRRITVPGLTSLSPESLEEIIDIIMKGNANRTMSPTEANAASSRSHAVLQVTLIQKPRTAGINEDHTLATLSIIDLAGSERATATKLRGSRLFEGANINKSLLALGNCINALCDPHRRAHVPYRDSKLTRLLKFSLGGNCRTVMIVCVSPSSVHYEETHNTLKYANRAKNIKTEVLRNMISVDRHVSQYVKAIVELREQISELENRLAQIDLSSQSNGSDQDAVTQSFAHESKLAEARNLLRMTFEETLPLQNDTINKVEKVKHFDDSIRVLKYWLSCYERILPNSADERVFLVRSKLESLLTRRAEIIADIDPELVYQKFQRSVSHIINTYKQEGATMYADVLQDEVDLLKSIIENQVLDAQNKVDEFTPVLESLLRSSFKASSLLKEGGMQELFSILEKWLLGIGLGEKPNISVLSESYKLNSTSDDSRTINRDRVHSFPTQPLLNNNLPRMFFVKSPKKPVVFSKRSPKKRVRFDDSMSTSDSGASAYNSPIQTSKLKNMNFFNTMHMPSTPAHKRPENKNQIDVEINLTSPVSPMLEDKPEPGLLIKSPLEKKQEVNSESTQLDQLLAEDSSTDDVSLPHLDTIDLDGSPVPKVPDLNFSRANMDSPTFILNNEAIHNFDFSKPKTRQSLSSLTTLHLSNPANIIRKSLSMAENEEEKAT
|
Has a role in establishing metaphase during mitosis. Required for chromosome segregation where it generates tension during kinetochore capturing.
|
O14350
|
SWI3_SCHPO
|
Swi1-interacting protein swi3 (Replication fork protection complex subunit swi3)
|
MSTAASDSGVEKLVEENKREEVKKNEEEKEFDLGLEENPDSVKKPRKRLAKFDEERLISENGIPKLRKMMRKVKLKGKGHEAKDLKQLLGMYHIWTHELYPRATFDDSISYLKTLGKHRSVKVRRRGWINEIAVENGSDSNASLFTGPSSNSLVNLTSGDPYVQDTADDAFVAQDNDTQLE
|
Forms a fork protection complex (FPC) with swi1. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. It is required for programmed fork-pausing which is necessary for mating-type switching. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors. It is involved in termination at the mat1-proximal polar-terminator of replication (RTS1) and also required for activation of the Rad53-like checkpoint kinase cds1.
|
O14352
|
LSM4_SCHPO
|
Probable U6 snRNA-associated Sm-like protein LSm4
|
MLPLTLLNATQGRPILVELKNGETFNGHLENCDNYMNLTLREVIRTMPDGDKFFRLPECYIRGNNIKYLRIQDEVLSQVAKQQAQQRENRGSRFRGRGQRGRGNYGHTAPNRRGRGRGGHM
|
Binds specifically to the 3'-terminal U-tract of U6 snRNA.
|
O14356
|
TOR1_SCHPO
|
Serine/threonine-protein kinase tor1 (EC 2.7.11.1) (Phosphatidylinositol kinase homolog tor1) (Target of rapamycin kinase 1)
|
MEYFSDLKNKNESIQLAAADQLKEFVHSSTKELSGESLARFNNDINRRIFELIHSHDSHERFGGILAIGKLIEFESEGDVTNLSRYANYLRMTLPSTDWHSMELSAKVLGHLAASGGTLAAEFVEFEVQRAFEWLQGDRQEQKRMAAILIIKALAQNSPTLVYLYISEIFQNLWTGLRDPKPLIRETAADALGASLDVVCQREAKVQLQCFNEVLLQAEHGLRQSSVEYLHGSLLAYKELFEKSGSFIREHYTEFCDLALRLREHRDNSIRRCIVFLLPTLSEYNPKKFQQRYLDSFMVYLLSHIRKDKEKSLAFEAIGRIAMAVNEAMIPYLQNILKVIRDTLTAKVREKTQYEKPVFECIGMLAAAVKLELLEDSRSLLGLIFSCELSVHLRQALVKMAENIPPLLAPIQERLLNMVSQILTGKNFEIRTNDTYTPSFTNIYSAREPDQRSKSTESIILALETLGTFNFTGYSLISFIQESVLSYLENDNSEIRIAAARTCCQVFARDPICRKTNPLAVESVAEVLEKLLTLGIADSDPKIRETVLSLLDERFDRHLAHPDNIRCLFIALNDEVFSIREIAIIIIGRLALYNPAHVMPSLRKTIIQLLSDMEYSGNSRQKEESAQLLKLLVSKARTLIKPYIQSIIHVILPKAADTSPGVSSAIISALGELASVEGEDMPVDVRGSFMKLILVNLQDQSSTLKRLASLKCLRKLCGRSGYVIQPYLDYPPLLGALIGILQSEQPTPIRREVLRTLGVLGALDPYTYLTTEEVSDDLQSSHNNAHGVPQISAAQYPSLENYAMVAVVTLIGILKDSSLSMHHSSVVQAVMHICSQMGSKSTVFLPQVVPTFLQVMQSLSASSAEFYFQQLTTLTSIIGPNIRDYVSDIFNLSKVFWESTTSLLLVILELIDAIAIALQDEFKFYLPQILSCMLKAFSLDNTSSRSVSYKVLQSFVIFGSNIEEYMHLVLPVIIRSFERDTIPLGFRKSALKCIAQLFQSVNFSDHASRIIHPLVRMLGKSNGDLRAVIMDTLCAIVSQLGYDYSIFIPMVNKVLVSHKISHPAYELLVSRLLKGEPLPKDVVVKEFKPRPSTKPFSTQDEVLTKLPVDQASLKAAWESSQKLTRDDWQDWIRRISIELLKESPSSALRSCSTLAGIYHPLARDLFNVSFLSCWDELTESNKKNLVKSIELAMNAPNISVEILQTLLNLAEYMEREDHTLPIPIKVISAHASKCNVYAKALHYTELQFVQETKEEVSISTIESLITINNHLQQSDAAVGMLQYTKEHKQFSLKETWYEKLHRWDDALAAYEHREREGDSSFEINIGKLRCYYALGDWDHLSELAQKAWVTSEQEHREAIAPLAAAAAWGLGQWNLISEYVSAMDRDPQDKEFFSAISAVHLGQYNKAYGHIERHRDILVNDLSSIIGESYNRAYGIMVKSQMLSELEEIIDYKKNMQYENNLDSLKKTWRKRLEGCQKNVDVWHNTLRFRALVLSPQDSPEMWIKLADLCRRSDRLKLSNQCLTYLMGRDPSNAYPLDSLKLLNPHVVYTYLKYLWATDQKNIAVSELEEFTSYLSSKHGYKMGDSSKLVDILASSSVSSEERSFLARCFHKLGKWKKSLQDSVNQESVRDILNCYFYATLFDKSWYKAWHSWALANFEVVGYYEQTEHGVTQDMYEQYIVPAIKGFFHSSVLNQKNSLQDILRLLNLWFKFGEHSDVAAAIVEGFSNVPMDTWLEVIPQLIARIHTSSSSVRASVHQLLSDIGRVHPQALVYSLTVSSKSTNPQQKHSAKSIMDSMLSHSDTLVRQALLVSQELIRVAILWHELWYEGLEEASQAYFSDHDISLMIDIVKPLHETLEKGPSTLSEISFAQTFGYDLRKARSYWQKFLQDGDPTELNQSWDLYYQVFRRIQKQLPRIKHLELQYVSPKLLDACDLELAVPGTYGHNKPVIRISHFHHTFEVISSKQRPRRLTIHGSDGKDYQYVLKGHEDLRQDERVMQLFGLCNTLLTTDSETFKRRLNIERYTVIPLSPNSGLLGWVPHSDTLHFLIKEFRSKRNILLNLEHRMMLQMAPDCDSLTLLQKLEVFEYVMANTDGYDLYHVLWLKSRSSEAWLDRRTSYTQSLAVMSMVGYILGLGDRHPSNLMMDRYSGKIIHIDFGDCFEVAMHREKFPEKIPFRLTRMLINAMEVSGIQGTYKITCELVMRVLRSNTESLMAVLEAFVYDPLINWRLMTKSSFGASTTLRPTSSSVEEKGRSYTHRARHADYAALSETNGVNAEGLNERSIQVLKRVSNKLTGKDFDLKEQLPVKAQVEKLIQQATAPENLCRCYVGWCSFW
|
Phosphatidylinositol 3-kinase homolog, component of TORC2, which regulates multiple cellular processes to control cell growth in response to environmental signals. TORC2 is required for cell survival under various stress conditions. TORC2 positively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Positively regulates amino acid uptake through the control of expression of amino acid permeases. Responsible for the phosphorylation of AGC kinase gad8 at 'Ser-527' and 'Ser-546', activating gad8 kinase activity and promoting sexual development.
|
O14370
|
BCA1_SCHPO
|
Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT) (EC 2.6.1.42)
|
MSLMFLRRAGNIKGRNIRFALQRGSVGYSQQSSEACKNFLNTTQLRTMVQTAALHGPKPMDSSHIKVTNVKELKPLPEWKSLKFGENFTDHMLIMKWNREKGWSTPEIVPFGKLCFHPASSVFHYGFECFEGMKAFRDEKGVPRLFRPIKNAERMLSTGTRISLPSFDPAELAEIIRKFVAHENRWVPDQRGYSLYIRPTFIGTDEALGVHHCDNAMLYVIASPVGPYYSSGFKAVKLCCSEESVRAWPGGTGHYKLGGNYAPSVLPQKEAAKKGYAQILWLYGDEDYITEVGTMNCFTVWINKNGEKEIITAPLDGMILPGVTRDSILEICRERLAPKGWKITEGKYSMKEVAQASKEGRLLEVFGAGTAALVSPVKAINYKGTEYEIPMPEGQEAGPITSEISKWILDIQYGKEPNNPWSVPALP
|
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
|
O14405
|
GUN4_HYPJE
|
Endoglucanase-4 (EC 3.2.1.4) (Cellulase IV) (Cellulase-61A) (Cel61A) (Endo-1,4-beta-glucanase IV) (EGIV) (Endoglucanase IV) (Endoglucanase-61A)
|
MIQKLSNLLVTALAVATGVVGHGHINDIVINGVWYQAYDPTTFPYESNPPIVVGWTAADLDNGFVSPDAYQNPDIICHKNATNAKGHASVKAGDTILFQWVPVPWPHPGPIVDYLANCNGDCETVDKTTLEFFKIDGVGLLSGGDPGTWASDVLISNNNTWVVKIPDNLAPGNYVLRHEIIALHSAGQANGAQNYPQCFNIAVSGSGSLQPSGVLGTDLYHATDPGVLINIYTSPLNYIIPGPTVVSGLPTSVAQGSSAATATASATVPGGGSGPTSRTTTTARTTQASSRPSSTPPATTSAPAGGPTQTLYGQCGGSGYSGPTRCAPPATCSTLNPYYAQCLN
|
Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. May be involved in the degradation of complex natural cellulosic substrates.
|
O14417
|
MAD2_SCHPO
|
Mitotic spindle checkpoint component mad2
|
MSSVPIRTNFSLKGSSKLVSEFFEYAVNSILFQRGIYPAEDFKVVRKYGLNMLVSVDEEVKTYIRKIVSQLHKWMFAKKIQKLILVITSKCSGEDLERWQFNVEMVDTADQFQNIGNKEDELRVQKEIQALIRQITATVTFLPQLEEQCTFNVLVYADKDSEVPTDWVDSDPRILRDAEQVQLRSFSTSMHKIDCQVAYRVNP
|
Feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. It interacts with the anaphase promoting complex/cyclosome (APC/C) thereby inhibiting APC/C-dependent proteolysis, a step required for exit from mitosis.
|
O14434
|
ARP1_ASPFU
|
Scytalone dehydratase arp1 (EC 4.2.1.94) (Conidial pigment biosynthesis oxidase arp1)
|
MVEKKPNLTLEFHDYLALKKVLFDWADSYDAKDWDRLRSIIAPTLTVDYRQIGLRKWDDMPAEDYMAMISDMDFLGDPTVKTQHLLGESWWEKISDTEVIGHHQLRAAHQVYTDSTLQTVKLKGHGHATNEHYYRKVDGVWKFAGLKPTVRWNEYQFEDVFRAAKPSV
|
Scytalone dehydratase part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall. The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA. The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening. 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone. The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN. 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone. Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN. Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin. DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize. DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins. DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses. DHN-melanin protects also conidia against amoeba predation.
|
O14442
|
CP51_UNCNE
|
Eburicol 14-alpha-demethylase (EC 1.14.14.154) (CYPLI) (Cytochrome P450 51) (Cytochrome P450-14DM) (Cytochrome P450-LIA1) (Sterol 14-alpha demethylase)
|
MYIADILSDLLTQQTTRYGWIFMVTSIAFSIILLAVGLNVLSQLLFRRPYEPPVVFHWFPIIGSTISYGIDPYKFYFDCRAKYGDIFTFILLGKKVTVYLGLQGNNFILNGKLKDVNAEEIYTNLTTPVFGRDVVYDCPNSKLMEQKKFMKTALTIEAFHSYVTIIQNEVEAYINNCVSFQGESGTVNISKVMAEITIYTASHALQGEEVRENFDSSFAALYHDLDMGFTPINFTFYWAPLPWNRARDHAQRTVARTYMNIIQARREEKRSGENKHDIMWELMRSTYKDGTPVPDREIAHMMIALLMAGQHSSSSTSSWIMLWLAARPDIMEELYEEQLRIFGSEKPFPPLQYEDLSKLQLHQNVLKEVLRLHAPIHSIMRKVKNPMIVPGTKYVIPTSHVLISSPGCTSQDATFFPDPLKWDPHRWDIGSGKVLGNDAVDEKYDYGYGLTSTGASSPYLPFGAGRHRCIGEQFATLQLVTIMATMVRFFRFRNIDGKQGVVKTDYSSLFSMPLAPALIGWEKR
|
Sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (By similarity). Can also use susbtrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity).
|
O14463
|
TRX1_SCHPO
|
Thioredoxin-1 (TR-1) (Trx-1)
|
MVKQVSDSSEFKSIVCQDKLVVVDFFATWCGPCKAIAPKFEQFSNTYSDATFIKVDVDQLSEIAAEAGVHAMPSFFLYKNGEKIEEIVGANPAKLEASIKANL
|
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
|
O14467
|
MBF1_YEAST
|
Multiprotein-bridging factor 1 (Suppressor of frameshift mutations protein 13)
|
MSDWDTNTIIGSRARAGGSGPRANVARSQGQINAARRQGLVVSVDKKYGSTNTRGDNEGQRLTKVDRETDIVKPKKLDPNVGRAISRARTDKKMSQKDLATKINEKPTVVNDYEAARAIPNQQVLSKLERALGVKLRGNNIGSPLGAPKKK
|
Transcriptional coactivator that stimulates GCN4-dependent transcriptional activity by bridging the DNA-binding region of GCN4 and TBP (SPT15), thereby recruiting TBP to GCN4-bound promoters. Involved in induction of the ribosome quality control (RQC) pathway a pathway that degrades nascent peptide chains during problematic translation. Required to prevent stalled ribosomes from frameshifting.
|
O14470
|
SSR2_SCHPO
|
SWI/SNF and RSC complexes subunit ssr2
|
MTLDQVRIPFLVEQTYPIIVPSYAGWFDMSKIHDIERRSNPEFFNGKSPLKTPSIYKDYRDFMINSYRLEPNEYLTVTACRRNLVGDVCAIIRVHAFLEQWGLINYQIDPETRPAFRLPPISGHVQAISNTPIVTQEMLAQHPPPSTVGGSSSQEFVKLEEKHYSPSLNAMEQTSPKEEDEKSDKVPRVDKVCFTCGVNCSQTWYHNLKNKKYDICPNCYKQGRFSSSFNSSDFLCMDAIDFNHDEEKPWSNQETLLLLEAIETYGDDWNQIALHVGSRTKEQCLIHFLQIPIEDPYRQKLQGDFSPFKKGFLPFDENENPVLSTLTYLASIVQQGMKERKQNESVKQGETSFGNSEFKNPLERVAYYALKSAAQKAKLIAAFENRQLRRLVFSLIQAQLEKLQLKMKVLEQLEKMCSLELSELDLRGKNLLLSRLSTKKMLLAFNKKLEEAVNLGGEDGLKIIDDLMSTEHAEALLTFEMPTATTVSPLSKQYPDKFRTIAL
|
Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
|
O14490
|
DLGP1_HUMAN
|
Disks large-associated protein 1 (DAP-1) (Guanylate kinase-associated protein) (hGKAP) (PSD-95/SAP90-binding protein 1) (SAP90/PSD-95-associated protein 1) (SAPAP1)
|
MKGLSGSRSHHHGVTCDSACDSLSHHSDRKPYLLSPVEHHPADHPYYTQRNSFQAECVGPFSDPLASSTFPRRHYTSQQELKDECALVPRTLATKANRIPANLLDQFERQLPLSRDGYHTLQYKRTAVEHRSDSPGRIRHLVHSVQKLFTKSHSLEGPSKGSVNGGKASPDEAQAARYGKRSKSKERRAEPKARPSTSPGWWSSDDNLDGDMCIYHAPSGVMTMGRCPDRSASQYFLEAYNTISEQAVKASRSNNDVKCSTCANLPVSLDTPLLKKSAWSSTLTVSRAREVYQKASVNMDQAMVKSESCQQERSCQYLQVPQDEWTGYTPRGKDDEIPCRRMRSGSYIKAMGDEDSGDSDTSPKPSPKVAARRESYLKATQPSLTELTTLKISNEHSPKLQIRSHSYLRAVSEVSINRSLDSLDPAGLLTSPKFRSRNESYMRAMSTISQVSEMEVNGQFESVCESVFSELESQAVEALDLPMPGCFRMRSHSYVRAIEKGCSQDDECVSLRSSSPPRTTTTVRTIQSSTVSSCITTYKKTPPPVPPRTTTKPFISITAQSSTESAQDAYMDGQGQRGDIISQSGLSNSTESLDSMKALTAAIEAANAQIHGPASQHMGNNTATVTTTTTIATVTTEDRKKDHFKKNRCLSIGIQVDDAEEPDKTGENKAPSKFQSVGVQVEEEKCFRRFTRSNSVTTAVQADLDFHDNLENSLESIEDNSCPGPMARQFSRDASTSTVSIQGSGNHYHACAADDDFDTDFDPSILPPPDPWIDSITEDPLEAVQRSVCHRDGHWFLKLLQAERDRMEGWCQQMEREERENNLPEDILGKIRTAVGSAQLLMAQKFYQFRELCEENLNPNAHPRPTSQDLAGFWDMLQLSIENISMKFDELHQLKANNWKQMDPLDKKERRAPPPVPKKPAKGPAPLIRERSLESSQRQEARKRLMAAKRAASVRQNSATESAESIEIYIPEAQTRL
|
Part of the postsynaptic scaffold in neuronal cells.
|
O14492
|
SH2B2_HUMAN
|
SH2B adapter protein 2 (Adapter protein with pleckstrin homology and Src homology 2 domains) (SH2 and PH domain-containing adapter protein APS)
|
MNGAGPGPAAAAPVPVPVPVPDWRQFCELHAQAAAVDFAHKFCRFLRDNPAYDTPDAGASFSRHFAANFLDVFGEEVRRVLVAGPTTRGAAVSAEAMEPELADTSALKAAPYGHSRSSEDVSTHAATKARVRKGFSLRNMSLCVVDGVRDMWHRRASPEPDAAAAPRTAEPRDKWTRRLRLSRTLAAKVELVDIQREGALRFMVADDAAAGSGGSAQWQKCRLLLRRAVAEERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVDPGDSEEDTELSCTRGGCLASRVASCSCELLTDAVDLPRPPETTAVGAVVTAPHSRGRDAVRESLIHVPLETFLQTLESPGGSGSDSNNTGEQGAETDPEAEPELELSDYPWFHGTLSRVKAAQLVLAGGPRNHGLFVIRQSETRPGEYVLTFNFQGKAKHLRLSLNGHGQCHVQHLWFQSVLDMLRHFHTHPIPLESGGSADITLRSYVRAQDPPPEPGPTPPAAPASPACWSDSPGQHYFSSLAAAACPPASPSDAAGASSSSASSSSAASGPAPPRPVEGQLSARSRSNSAERLLEAVAATAAEEPPEAAPGRARAVENQYSFY
|
Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. May be involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis. May induce cytoskeletal reorganization via interaction with VAV3.
|
O14493
|
CLD4_HUMAN
|
Claudin-4 (Clostridium perfringens enterotoxin receptor) (CPE-R) (CPE-receptor) (Williams-Beuren syndrome chromosomal region 8 protein)
|
MASMGLQVMGIALAVLGWLAVMLCCALPMWRVTAFIGSNIVTSQTIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALVIISIIVAALGVLLSVVGGKCTNCLEDESAKAKTMIVAGVVFLLAGLMVIVPVSWTAHNIIQDFYNPLVASGQKREMGASLYVGWAASGLLLLGGGLLCCNCPPRTDKPYSAKYSAARSAAASNYV
|
Channel-forming tight junction protein that mediates paracellular chloride transport in the kidney. Plays a critical role in the paracellular reabsorption of filtered chloride in the kidney collecting ducts. Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
|
O14494
|
PLPP1_HUMAN
|
Phospholipid phosphatase 1 (EC 3.1.3.-) (EC 3.1.3.106) (EC 3.1.3.4) (EC 3.6.1.75) (Lipid phosphate phosphohydrolase 1) (PAP2-alpha) (Phosphatidate phosphohydrolase type 2a) (Phosphatidic acid phosphatase 2a) (PAP-2a) (PAP2a)
|
MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLGGIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAKYSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAILVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP
|
Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound. Through its extracellular phosphatase activity allows both the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes. It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P. Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes. May also have an intracellular activity to regulate phospholipid-mediated signaling pathways (By similarity).
|
O14495
|
PLPP3_HUMAN
|
Phospholipid phosphatase 3 (EC 3.1.3.-) (EC 3.1.3.4) (Lipid phosphate phosphohydrolase 3) (PAP2-beta) (Phosphatidate phosphohydrolase type 2b) (Phosphatidic acid phosphatase 2b) (PAP-2b) (PAP2b) (Vascular endothelial growth factor and type I collagen-inducible protein) (VCIP)
|
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIKPYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQNPYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYRCRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVDIIDRNNHHNMM
|
Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound. Has both an extracellular and an intracellular phosphatase activity, allowing the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes. Through the dephosphorylation of extracellular sphingosine-1-phosphate and the regulation of its extra- and intracellular availability, plays a role in vascular homeostasis, regulating endothelial cell migration, adhesion, survival, proliferation and the production of pro-inflammatory cytokines. By maintaining the appropriate levels of this lipid in the cerebellum, also ensure its proper development and function (By similarity). Through its intracellular lipid phosphatase activity may act in early compartments of the secretory pathway, regulating the formation of Golgi to endoplasmic reticulum retrograde transport carriers. Independently of this phosphatase activity may also function in the Wnt signaling pathway and the stabilization of beta-catenin/CTNNB1, thereby regulating cell proliferation, migration and differentiation in angiogenesis or yet in tumor growth. Also plays a role in integrin-mediated cell-cell adhesion in angiogenesis.
|
O14497
|
ARI1A_HUMAN
|
AT-rich interactive domain-containing protein 1A (ARID domain-containing protein 1A) (B120) (BRG1-associated factor 250) (BAF250) (BRG1-associated factor 250a) (BAF250A) (Osa homolog 1) (hOSA1) (SWI-like protein) (SWI/SNF complex protein p270) (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1) (hELD)
|
MAAQVAPAAASSLGNPPPPPPSELKKAEQQQREEAGGEAAAAAAAERGEMKAAAGQESEGPAVGPPQPLGKELQDGAESNGGGGGGGAGSGGGPGAEPDLKNSNGNAGPRPALNNNLTEPPGGGGGGSSDGVGAPPHSAAAALPPPAYGFGQPYGRSPSAVAAAAAAVFHQQHGGQQSPGLAALQSGGGGGLEPYAGPQQNSHDHGFPNHQYNSYYPNRSAYPPPAPAYALSSPRGGTPGSGAAAAAGSKPPPSSSASASSSSSSFAQQRFGAMGGGGPSAAGGGTPQPTATPTLNQLLTSPSSARGYQGYPGGDYSGGPQDGGAGKGPADMASQCWGAAAAAAAAAAASGGAQQRSHHAPMSPGSSGGGGQPLARTPQPSSPMDQMGKMRPQPYGGTNPYSQQQGPPSGPQQGHGYPGQPYGSQTPQRYPMTMQGRAQSAMGGLSYTQQIPPYGQQGPSGYGQQGQTPYYNQQSPHPQQQQPPYSQQPPSQTPHAQPSYQQQPQSQPPQLQSSQPPYSQQPSQPPHQQSPAPYPSQQSTTQQHPQSQPPYSQPQAQSPYQQQQPQQPAPSTLSQQAAYPQPQSQQSQQTAYSQQRFPPPQELSQDSFGSQASSAPSMTSSKGGQEDMNLSLQSRPSSLPDLSGSIDDLPMGTEGALSPGVSTSGISSSQGEQSNPAQSPFSPHTSPHLPGIRGPSPSPVGSPASVAQSRSGPLSPAAVPGNQMPPRPPSGQSDSIMHPSMNQSSIAQDRGYMQRNPQMPQYSSPQPGSALSPRQPSGGQIHTGMGSYQQNSMGSYGPQGGQYGPQGGYPRQPNYNALPNANYPSAGMAGGINPMGAGGQMHGQPGIPPYGTLPPGRMSHASMGNRPYGPNMANMPPQVGSGMCPPPGGMNRKTQETAVAMHVAANSIQNRPPGYPNMNQGGMMGTGPPYGQGINSMAGMINPQGPPYSMGGTMANNSAGMAASPEMMGLGDVKLTPATKMNNKADGTPKTESKSKKSSSSTTTNEKITKLYELGGEPERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQCLYAFECKIERGEDPPPDIFAAADSKKSQPKIQPPSPAGSGSMQGPQTPQSTSSSMAEGGDLKPPTPASTPHSQIPPLPGMSRSNSVGIQDAFNDGSDSTFQKRNSMTPNPGYQPSMNTSDMMGRMSYEPNKDPYGSMRKAPGSDPFMSSGQGPNGGMGDPYSRAAGPGLGNVAMGPRQHYPYGGPYDRVRTEPGIGPEGNMSTGAPQPNLMPSNPDSGMYSPSRYPPQQQQQQQQRHDSYGNQFSTQGTPSGSPFPSQQTTMYQQQQQNYKRPMDGTYGPPAKRHEGEMYSVPYSTGQGQPQQQQLPPAQPQPASQQQAAQPSPQQDVYNQYGNAYPATATAATERRPAGGPQNQFPFQFGRDRVSAPPGTNAQQNMPPQMMGGPIQASAEVAQQGTMWQGRNDMTYNYANRQSTGSAPQGPAYHGVNRTDEMLHTDQRANHEGSWPSHGTRQPPYGPSAPVPPMTRPPPSNYQPPPSMQNHIPQVSSPAPLPRPMENRTSPSKSPFLHSGMKMQKAGPPVPASHIAPAPVQPPMIRRDITFPPGSVEATQPVLKQRRRLTMKDIGTPEAWRVMMSLKSGLLAESTWALDTINILLYDDNSIMTFNLSQLPGLLELLVEYFRRCLIEIFGILKEYEVGDPGQRTLLDPGRFSKVSSPAPMEGGEEEEELLGPKLEEEEEEEVVENDEEIAFSGKDKPASENSEEKLISKFDKLPVKIVQKNDPFVVDCSDKLGRVQEFDSGLLHWRIGGGDTTEHIQTHFESKTELLPSRPHAPCPPAPRKHVTTAEGTPGTTDQEGPPPDGPPEKRITATMDDMLSTRSSTLTEDGAKSSEAIKESSKFPFGISPAQSHRNIKILEDEPHSKDETPLCTLLDWQDSLAKRCVCVSNTIRSLSFVPGNDFEMSKHPGLLLILGKLILLHHKHPERKQAPLTYEKEEEQDQGVSCNKVEWWWDCLEMLRENTLVTLANISGQLDLSPYPESICLPVLDGLLHWAVCPSAEAQDPFSTLGPNAVLSPQRLVLETLSKLSIQDNNVDLILATPPFSRLEKLYSTMVRFLSDRKNPVCREMAVVLLANLAQGDSLAARAIAVQKGSIGNLLGFLEDSLAATQFQQSQASLLHMQNPPFEPTSVDMMRRAARALLALAKVDENHSEFTLYESRLLDISVSPLMNSLVSQVICDVLFLIGQS
|
Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Binds DNA non-specifically. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity).
|
O14503
|
BHE40_HUMAN
|
Class E basic helix-loop-helix protein 40 (bHLHe40) (Class B basic helix-loop-helix protein 2) (bHLHb2) (Differentially expressed in chondrocytes protein 1) (DEC1) (Enhancer-of-split and hairy-related protein 2) (SHARP-2) (Stimulated by retinoic acid gene 13 protein)
|
MERIPSAQPPPACLPKAPGLEHGDLPGMYPAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGELSGRNVETGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGTSRKPSDPAPKVMDFKEKPSSPAKGSEGPGKNCVPVIQRTFAHSSGEQSGSDTDTDSGYGGESEKGDLRSEQPCFKSDHGRRFTMGERIGAIKQESEEPPTKKNRMQLSDDEGHFTSSDLISSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNASAAALSSFMNPDKISAPLLMPQRLPSPLPAHPSVDSSVLLQALKPIPPLNLETKD
|
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. Represses the transcription of NR0B2 and attentuates the transactivation of NR0B2 by the CLOCK-BMAL1 complex. Drives the circadian rhythm of blood pressure through transcriptional repression of ATP1B1 in the cardiovascular system.
|
O14508
|
SOCS2_HUMAN
|
Suppressor of cytokine signaling 2 (SOCS-2) (Cytokine-inducible SH2 protein 2) (CIS-2) (STAT-induced STAT inhibitor 2) (SSI-2)
|
MTLRCLEPSGNGGEGTRSQWGTAGSAEEPSPQAARLAKALRELGQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVHLYLTKPLYTSAPSLQHLCRLTINKCTGAIWGLPLPTRLKDYLEEYKFQV
|
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-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
|
O14511
|
NRG2_HUMAN
|
Pro-neuregulin-2, membrane-bound isoform (Pro-NRG2) [Cleaved into: Neuregulin-2 (NRG-2) (Divergent of neuregulin-1) (DON-1) (Neural- and thymus-derived activator for ERBB kinases) (NTAK)]
|
MRQVCCSALPPPPLEKGRCSSYSDSSSSSSERSSSSSSSSSESGSSSRSSSNNSSISRPAAPPEPRPQQQPQPRSPAARRAAARSRAAAAGGMRRDPAPGFSMLLFGVSLACYSPSLKSVQDQAYKAPVVVEGKVQGLVPAGGSSSNSTREPPASGRVALVKVLDKWPLRSGGLQREQVISVGSCVPLERNQRYIFFLEPTEQPLVFKTAFAPLDTNGKNLKKEVGKILCTDCATRPKLKKMKSQTGQVGEKQSLKCEAAAGNPQPSYRWFKDGKELNRSRDIRIKYGNGRKNSRLQFNKVKVEDAGEYVCEAENILGKDTVRGRLYVNSVSTTLSSWSGHARKCNETAKSYCVNGGVCYYIEGINQLSCKCPNGFFGQRCLEKLPLRLYMPDPKQKAEELYQKRVLTITGICVALLVVGIVCVVAYCKTKKQRKQMHNHLRQNMCPAHQNRSLANGPSHPRLDPEEIQMADYISKNVPATDHVIRRETETTFSGSHSCSPSHHCSTATPTSSHRHESHTWSLERSESLTSDSQSGIMLSSVGTSKCNSPACVEARARRAAAYNLEERRRATAPPYHDSVDSLRDSPHSERYVSALTTPARLSPVDFHYSLATQVPTFEITSPNSAHAVSLPPAAPISYRLAEQQPLLRHPAPPGPGPGPGPGPGPGADMQRSYDSYYYPAAGPGPRRGTCALGGSLGSLPASPFRIPEDDEYETTQECAPPPPPRPRARGASRRTSAGPRRWRRSRLNGLAAQRARAARDSLSLSSGSGGGSASASDDDADDADGALAAESTPFLGLRGAHDALRSDSPPLCPAADSRTYYSLDSHSTRASSRHSRGPPPRAKQDSAPL
|
Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. May also promote the heterodimerization with the EGF receptor.
|
O14512
|
SOCS7_HUMAN
|
Suppressor of cytokine signaling 7 (SOCS-7) (Nck, Ash and phospholipase C gamma-binding protein) (Nck-associated protein 4) (NAP-4)
|
MVFRNVGRPPEEEDVEAAPEPGPSELLCPRHRCALDPKALPPGLALERTWGPAAGLEAQLAALGLGQPAGPGVKTVGGGCCPCPCPPQPPPPQPQPPAAAPQAGEDPTETSDALLVLEGLESEAESLETNSCSEEELSSPGRGGGGGGRLLLQPPGPELPPVPFPLQDLVPLGRLSRGEQQQQQQQQPPPPPPPPGPLRPLAGPSRKGSFKIRLSRLFRTKSCNGGSGGGDGTGKRPSGELAASAASLTDMGGSAGRELDAGRKPKLTRTQSAFSPVSFSPLFTGETVSLVDVDISQRGLTSPHPPTPPPPPRRSLSLLDDISGTLPTSVLVAPMGSSLQSFPLPPPPPPHAPDAFPRIAPIRAAESLHSQPPQHLQCPLYRPDSSSFAASLRELEKCGWYWGPMNWEDAEMKLKGKPDGSFLVRDSSDPRYILSLSFRSQGITHHTRMEHYRGTFSLWCHPKFEDRCQSVVEFIKRAIMHSKNGKFLYFLRSRVPGLPPTPVQLLYPVSRFSNVKSLQHLCRFRIRQLVRIDHIPDLPLPKPLISYIRKFYYYDPQEEVYLSLKEAQLISKQKQEVEPST
|
Regulates signaling cascades probably through protein ubiquitination and/or sequestration. Functions in insulin signaling and glucose homeostasis through IRS1 ubiquitination and subsequent proteasomal degradation. Inhibits also prolactin, growth hormone and leptin signaling by preventing STAT3 and STAT5 activation, sequestering them in the cytoplasm and reducing their binding to DNA. May be a substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:15677474, ECO:0000269|PubMed:16127460}.
|
O14514
|
AGRB1_HUMAN
|
Adhesion G protein-coupled receptor B1 (Brain-specific angiogenesis inhibitor 1) [Cleaved into: Vasculostatin-40 (Vstat40); Vasculostatin-120 (Vstat120)]
|
MRGQAAAPGPVWILAPLLLLLLLLGRRARAAAGADAGPGPEPCATLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPVPCSGPGRVRTYQFDSFLESTRTYLGVESFDEVLRLCDPSAPLAFLQASKQFLQMRRQQPPQHDGLRPRAGPPGPTDDFSVEYLVVGNRNPSRAACQMLCRWLDACLAGSRSSHPCGIMQTPCACLGGEAGGPAAGPLAPRGDVCLRDAVAGGPENCLTSLTQDRGGHGATGGWKLWSLWGECTRDCGGGLQTRTRTCLPAPGVEGGGCEGVLEEGRQCNREACGPAGRTSSRSQSLRSTDARRREELGDELQQFGFPAPQTGDPAAEEWSPWSVCSSTCGEGWQTRTRFCVSSSYSTQCSGPLREQRLCNNSAVCPVHGAWDEWSPWSLCSSTCGRGFRDRTRTCRPPQFGGNPCEGPEKQTKFCNIALCPGRAVDGNWNEWSSWSACSASCSQGRQQRTRECNGPSYGGAECQGHWVETRDCFLQQCPVDGKWQAWASWGSCSVTCGAGSQRRERVCSGPFFGGAACQGPQDEYRQCGTQRCPEPHEICDEDNFGAVIWKETPAGEVAAVRCPRNATGLILRRCELDEEGIAYWEPPTYIRCVSIDYRNIQMMTREHLAKAQRGLPGEGVSEVIQTLVEISQDGTSYSGDLLSTIDVLRNMTEIFRRAYYSPTPGDVQNFVQILSNLLAEENRDKWEEAQLAGPNAKELFRLVEDFVDVIGFRMKDLRDAYQVTDNLVLSIHKLPASGATDISFPMKGWRATGDWAKVPEDRVTVSKSVFSTGLTEADEASVFVVGTVLYRNLGSFLALQRNTTVLNSKVISVTVKPPPRSLRTPLEIEFAHMYNGTTNQTCILWDETDVPSSSAPPQLGPWSWRGCRTVPLDALRTRCLCDRLSTFAILAQLSADANMEKATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAGASLWSSCVVLPLLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVDRQEEGNGDSGGSFQNGHAQLMTDFEKDVDLACRSVLNKDIAACRTATITGTLKRPSLPEEEKLKLAHAKGPPTNFNSLPANVSKLHLHGSPRYPGGPLPDFPNHSLTLKRDKAPKSSFVGDGDIFKKLDSELSRAQEKALDTSYVILPTATATLRPKPKEEPKYSIHIDQMPQTRLIHLSTAPEASLPARSPPSRQPPSGGPPEAPPAQPPPPPPPPPPPPQQPLPPPPNLEPAPPSLGDPGEPAAHPGPSTGPSTKNENVATLSVSSLERRKSRYAELDFEKIMHTRKRHQDMFQDLNRKLQHAAEKDKEVLGPDSKPEKQQTPNKRPWESLRKAHGTPTWVKKELEPLQPSPLELRSVEWERSGATIPLVGQDIIDLQTEV
|
Phosphatidylserine receptor which enhances the engulfment of apoptotic cells. Also mediates the binding and engulfment of Gram-negative bacteria. Stimulates production of reactive oxygen species by macrophages in response to Gram-negative bacteria, resulting in enhanced microbicidal macrophage activity. In the gastric mucosa, required for recognition and engulfment of apoptotic gastric epithelial cells. Promotes myoblast fusion (By similarity). Activates the Rho pathway in a G-protein-dependent manner. Inhibits MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity (By similarity). Required for the formation of dendritic spines by ensuring the correct localization of PARD3 and TIAM1 (By similarity). Potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53/TP53 signal in suppression of glioblastoma.
|
O14519
|
CDKA1_HUMAN
|
Cyclin-dependent kinase 2-associated protein 1 (CDK2-associated protein 1) (Deleted in oral cancer 1) (DOC-1) (Putative oral cancer suppressor)
|
MSYKPNLAAHMPAAALNAAGSVHSPSTSMATSSQYRQLLSDYGPPSLGYTQGTGNSQVPQSKYAELLAIIEELGKEIRPTYAGSKSAMERLKRGIIHARGLVRECLAETERNARS
|
Inhibitor of cyclin-dependent kinase CDK2 (By similarity). Also acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin.
|
O14520
|
AQP7_HUMAN
|
Aquaporin-7 (AQP-7) (Aquaglyceroporin-7) (Aquaporin adipose) (AQPap) (Aquaporin-7-like)
|
MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF
|
Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH. The channel is also permeable to urea. Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export from adipocytes. After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia. Required for normal glycerol reabsorption in the kidney (By similarity).
|
O14521
|
DHSD_HUMAN
|
Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial (CybS) (CII-4) (QPs3) (Succinate dehydrogenase complex subunit D) (Succinate-ubiquinone oxidoreductase cytochrome b small subunit) (Succinate-ubiquinone reductase membrane anchor subunit)
|
MAVLWRLSAVCGALGGRALLLRTPVVRPAHISAFLQDRPIPEWCGVQHIHLSPSHHSGSKAASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGLGQVVTDYVHGDALQKAAKAGLLALSALTFAGLCYFNYHDVGICKAVAMLWKL
|
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
|
O14522
|
PTPRT_HUMAN
|
Receptor-type tyrosine-protein phosphatase T (R-PTP-T) (EC 3.1.3.48) (Receptor-type tyrosine-protein phosphatase rho) (RPTP-rho)
|
MASLAALALSLLLRLQLPPLPGARAQSAAGGCSFDEHYSNCGYSVALGTNGFTWEQINTWEKPMLDQAVPTGSFMMVNSSGRASGQKAHLLLPTLKENDTHCIDFHYYFSSRDRSSPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTFWPHFYQVIFESVSLKGHPGYIAVDEVRVLAHPCRKAPHFLRLQNVEVNVGQNATFQCIAGGKWSQHDKLWLQQWNGRDTALMVTRVVNHRRFSATVSVADTAQRSVSKYRCVIRSDGGSGVSNYAELIVKEPPTPIAPPELLAVGATYLWIKPNANSIIGDGPIILKEVEYRTTTGTWAETHIVDSPNYKLWHLDPDVEYEIRVLLTRPGEGGTGPPGPPLTTRTKCADPVHGPQNVEIVDIRARQLTLQWEPFGYAVTRCHSYNLTVQYQYVFNQQQYEAEEVIQTSSHYTLRGLRPFMTIRLRLLLSNPEGRMESEELVVQTEEDVPGAVPLESIQGGPFEEKIYIQWKPPNETNGVITLYEINYKAVGSLDPSADLSSQRGKVFKLRNETHHLFVGLYPGTTYSFTIKASTAKGFGPPVTTRIATKISAPSMPEYDTDTPLNETDTTITVMLKPAQSRGAPVSVYQLVVKEERLQKSRRAADIIECFSVPVSYRNASSLDSLHYFAAELKPANLPVTQPFTVGDNKTYNGYWNPPLSPLKSYSIYFQALSKANGETKINCVRLATKGASTQNSNTVEPEKQVDNTVKMAGVIAGLLMFIIILLGVMLTIKRRRNAYSYSYYLKLAKKQKETQSGAQREMGPVASADKPTTKLSASRNDEGFSSSSQDVNGFTDGSRGELSQPTLTIQTHPYRTCDPVEMSYPRDQFQPAIRVADLLQHITQMKRGQGYGFKEEYEALPEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACLCGNTAIPVCEFRSLYYNISRLDPQTNSSQIKDEFQTLNIVTPRVRPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQFCMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYLSSF
|
May be involved in both signal transduction and cellular adhesion in the CNS.
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.