wanglab/gogpt-training-data huggingface dataset:
Protein: Putative fatty acid elongase 2 (EC 2.3.1.199) (3-keto acyl-CoA synthase SPAC1639.01c) (Putative elongation of fatty acids protein 2) (Very-long-chain 3-oxoacyl-CoA synthase 2) (Q7LKX0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in the synthesis of very long chain fatty acids.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P25358}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable acyl-CoA desaturase
- Very-long-chain 3-oxoacyl-CoA reductase
- Putative enoyl reductase C646.07c
- Probable very-long-chain
- Putative fatty acid elongase 1
- Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Diacylglycerol O-acyltransferase 1
- Ankyrin repeat-containing protein C105.02c
Sequence:
MPDSPTLHHNHIIGLENGSLTSNNNHQGMASVSVGQFQYPIWSWLNSLADATFGKRPSSFEFIVNKTRFSSAPVVATIIISYYLLILVGGRIMRNRQPIRLQKIFQYYNLTFSIASAILALLIFEQVAPAIYKHGFFFSICNEKAWTQPLVFLYYCAYISKFLELTDTFFLVLRKKPLQFLHCYHHGATAVLVYTQIVGRTSISWLIIEINLLVHVTMYYYYYLVAKGIRVPWKKWVTRFQIVQFFADLGFIYFAVYTEVAYRLKFYKACMGHCSGHPLAAFCGLATISSYLVLFIVFYHNTYKKNAALKMKAKAAAATKGNSSESSKNADLKRLSKSNASIAEVKCNNIVTNLYPISSGLNNEK
Protein: Interactor of HORMAD1 protein 1 (Coiled-coil domain-containing protein 36) (Q6PDM4)
Organism: Mus musculus (Mouse)
Function: Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination. Probably acts by forming a complex with MEI4 and REC114, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis. Not required for HORMAD1 functions in pairing-independent synaptonemal complex formation, ATR recruitment to unsynapsed axes, meiotic silencing of unsynapsed chromatin (MSUC) or meiotic surveillance.
Subcellular location: Chromosome {ECO:0000269|PubMed:27723721}. Note=Specifically localizes to unsynapsed chromosomal regions during meiosis (PubMed:27723721). Appears on chromatin during preleptotene, when pre-meiotic replication occurs and axes have not yet developed (PubMed:27723721). Remains associated with unsynapsed axesn zygotene, when axes elongate and synapsis begins but disappears from synapsed axes (PubMed:27723721). Localization diverges in the two sexes beyond zygotene (PubMed:27723721). In spermatocytes, synapsis between the largely non-homologous X and Y chromosomes is mostly constrained to their short pseudoautosomal regions (PARs) (PubMed:27723721). At the zygotene-to-pachytene transition, high levels remain on unsynapsed sex chromosome axes but also on PARs (PubMed:27723721). However, by early pachytene disappears from both the synapsed and unsynapsed regions of sex chromosomes (PubMed:27723721). Reaccumulates on unsynapsed axes of sex chromosomes in mid-late pachytene and on desynapsing autosome axes in diplotene, but disappears from chromatin concomitant with axis disassembly after diplotene (PubMed:27723721). In oocytes, disappears from axes after all chromosomes synapsed and is undetectable on chromatin beyond zygotene (PubMed:27723721). Ovarian levels also dramatically decrease as oocytes progress to late prophase (PubMed:27723721). HORMAD1 is required for robust accumulation on chromatin and unsynapsed axes, suggesting that HORMAD1 recruits IHO1 to unsynapsed axes (PubMed:27723721). {ECO:0000269|PubMed:27723721}.
Interaction partners:
- HORMA domain-containing protein 1
- Meiotic recombination protein REC114
- Ankyrin repeat domain-containing protein 31
- Type 2 DNA topoisomerase 6 subunit B-like
- Meiosis inhibitor protein 1
- Meiotic recombination protein SPO11
- CXXC-type zinc finger protein 1
- Histone-lysine N-methyltransferase PRDM9
Sequence:
MNFNVWNVKEMLSIPSGSGITKPSNWNNNQTDCSLSDSQFLFGSQFCPENSETLLPSLDAGACLRHPKQTQQNSVDSEPSIFIKYQAKPQLLGGDTKDESLFSLPLPVGKSKGLSKQFEEKKRRATDQSDSETLHSFVSHFPEVINKLQTSVEKTEENLSSRSQSILDSVETIAKTFQETARVQHDLMVESVRDKGSMEQAILEIQRTCAARQAEFMEMKSTLKNLEVLVVEQTKNLQQFCDNLSQLIVPGILEELKKFTSVPQVAGHLKDSTSQTSPSLTQSLHFTRQEKHPSEEPATWQAQEAPAGNPSTSSQRPGECGVWDEGAESGVFQKAALPTDGLHRGDGHVKNKTVPTYCKNWVMTTRSVSNHFSNLPSQRAGNGQGLMAQGASQRDVSKFEARVKNACPEYGPQSMCSFDSLEQSATEQKGRPCRKRRRGKKQQPQRSKRGGLLDRKQGQTSKAACAFIARHHCPQSPVCDPQGPLICWLTPRSSTKSTCHILGGTGETSQTARAAQGNLVQHSQRSSTDSSSQGDQQINWFSDLSLENLEPPQCKKGGTNLLCDPDFDSSDDNF
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (A0A0B4K7C5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- LD24679p
- Uncharacterized protein
- SUZ RNA-binding domain-containing
Sequence:
MSKSNLVISCLLLVAISNSLVRAQDLKVEVISTPEVCEQKSKNGDSLTMHYTGTLQADGKKFDSSFDRDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQGAGNVIPPKATLLFDVELINIGNAPPTTNVFKEIDDNADKQLSREEVIVYVSEYLKKQMTAVEGQDSEELKNMLAENDKLVEEIFQHEDKDKNGFISHDEFSGPKHDEL
Protein: Sexual differentiation process putative subtilase-type proteinase isp6 (EC 3.4.21.-) (P40903)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Subtilase-type proteinase psp3
- PDZ domain-containing protein C1685.05
- Serine/threonine-protein kinase atg1
- Sexual differentiation process putative amino-acid permease isp5
Sequence:
MRIPYSNLFSAAAGLALFASTACAAPVMPATDSDIAHAGIRPELDNAFYDSHGEAATPKHKPHAGPNAAPLLSASNADTTGLDSHYIIVLQPDLSEQEFQAHTNWVSEMHQMDIASQEDEYYDTSDSNYMFGLKHVYDFGEDSFKGYSGQFSSNIVEQIRLHPHVIAVERDQVVSIKKLETQSGAPWGLARISHKSVKYDDIGKYVYDSSAGDNITAYVVDTGVSIHHVEFEGRASWGATIPSGDVDEDNNGHGTHVAGTIASRAYGVAKKAEIVAVKVLRSSGSGTMADVIAGVEWTVRHHKSSGKKTSVGNMSLGGGNSFVLDMAVDSAVTNGVIYAVAAGNEYDDACYSSPAASKKAITVGASTINDQMAYFSNYGSCVDIFAPGLNILSTWIGSNTSTNTISGTSMATPHVAGLSAYYLGLHPAASASEVKDAIIKMGIHDVLLSIPVGSSTINLLAFNGAQE
Protein: Stardust, isoform I (EC 2.7.4.8) (Q9W3H8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRILKQWNRRRSGSSIVVLDGDDLKPCLPDDYISGQHHLNHQQQLQLQQQLQQQHPLQQQHYRTHSGDIREIDQEMLTMLSVNQDNGPHREMAVDCPDTFIARNKTPPRYPPPRPPQKQHQATTAMAATQVAQQQTPSHKLQATLSSDPNGNSNSNNNSHIVGISSSSSSNNSSITDDFLCVVDGLYQGRKDTASPSSSAFDEVMSKHTLDSFGSIAYRHLHQQHQATSNGNSSSNTSNTNSNTNSNTNSNSNTNGNTSNNTAVSTKTATVTKTGVSSSNSNSNSLNSSNSSMHTSSSSSGHSSNIASATSSSSATSSSTVPDDLSLAPPGYEVSQQQQQQHLVATPVTMLLPPMAKHRELPVDVPDSFIEMVKTTPRYPPPAHLSSRGSLLSNGSASTAHTTLSSMGVAPSPVTATAAAAASASAACATTAVAAAAVSGVADGDARRVADELNGNAKPVPPPRDHLRVEKDGRLVNCSPAPQLPDRRAPGNASSGSSGATTHPLQHQQIAQIVEPTLEQLDSIKKYQEQLRRRREEEERIAQQNEFLRNSLRGSRKLKALQDTATPGKAVAQQQQQATLATQVVGVENEAYLPDEDQPQAEQIDGYGELIAALTRLQNQLSKSGLSTLAGRVSAAHSVLASASVAHVLAARTAVLQRRRSRVSGPLHHSSLGLQKDIVELLTQSNTAAAIELGNLLTSHEMEGLLLAHDRIANHTDGTPSPTPTPTPAIGAATGSTLSSPVAGPKRNLGMVVPPPVVPPPLAQRGAMPLPRGESPPPVPMPPLATMPMSMPVNLPMSACFGTLNDQNDNIRIIQIEKSTEPLGATVRNEGEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMQGTLTFLIVPAGSPPSVGVMGGTTGSQLAGLGGAHRDTAVLHVRAHFDYDPEDDLYIPCRELGISFQKGDVLHVISREDPNWWQAYREGEEDQTLAGLIPSQSFQHQRETMKLAIAEEAGLARSRGKDGSGSKGATLLCARKGRKKKKKASSEAGYPLYATTAPDETDPEEILTYEEVALYYPRATHKRPIVLIGPPNIGRHELRQRLMADSERFSAAVPHTSRARREGEVPGVDYHFITRQAFEADILARRFVEHGEYEKAYYGTSLEAIRTVVASGKICVLNLHPQSLKLLRASDLKPYVVLVAPPSLDKLRQKKLRNGEPFKEEELKDIIATARDMEARWGHLFDMIIINNDTERAYHQLLAEINSLEREPQWVPAQWVHNNRDES
Protein: U3 small nucleolar RNA-associated protein 16 (U3 snoRNA-associated protein 16) (O94259)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 6
- Uncharacterized WD repeat-containing protein C2E1P5.05
- Uncharacterized protein C18B11.06
- Uncharacterized protein C57A7.06
- rRNA biogenesis protein rrp5
- Pre-rRNA-processing protein esf2
- rRNA-processing protein utp23
- Uncharacterized protein C1565.05
- Ribosome production factor 2 homolog
- Brix domain-containing protein C4F8.04
Sequence:
MQSSRKIMILKRNIKGLKSSAIIATYLTLNKLFIDKFCKTQESTYPIHFVHCHFGGIKKFHSHCQLSSSYTNSGQKSFKSFNSLRFIVLKSKTCLLRYKLLIKTFCCITYSKIENLSNTRMARLTAPSKGPSFSNLNKPNDLLKAEIEDNEASHYSQNQSSDSDSDEAPEEVSLKSSSDEVKKRLQRLKGNELQLRKAEREKRRLQNERNRERNAQRVSASKLDLAILEAAEVEEINSTTEIEEKVDEASLDLYTPKGHKIVFPNNEIPKKRTRSFRKGDFKVSVLKETNDPLLAPNYEKKLSQRKRDWINRQSVPRASKRRRPLTY
Protein: NAD(P) dependent steroid dehydrogenase-like (C9JDR0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEPAVSEPMRDQVARTHLTEDTPKVNADIEKVNQNQAKRCTVIGGSGFLGQHMVEQLLARGYAVNVFDIQQGFDNPQVRFFLGDLCSRQDLYPALKGVNTVFHCASPPPSSNNKELFYRVNYIGTKNVIETCKEAGVQKLILTSSASVIFEGVDIKNGTEDLPYAMKPIDYYTETKILQERAVLGANDPEKNFLTTAIRPHGIFGPRDPQLVPILIEAARNGKMKFVIGNGKNLVDFTFVENVVHGHILAAEQL
Protein: Golgin 104 (LD45682p) (Q9VV40)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI01459p
- GH16843p
- FI23003p1
Sequence:
MESAQATPPAEMENPASVENGDSGRDSNHIEGKAIGDVDMKADSIEQQLEESDVKTESNGDQLTDQDEGKIEQDLKAAVLEQVPIEEEGLSLRFKDLQAQEKVKELQQTPSQPPQNDILSHVHCLAQLEEQRRNYEQQLEQLRTSNVQKDNMITLIQRENAILGKEKQACRKEMEMANKEKEATVIKFAMKEKLLIDAKKEKEAVEKQLAEAKKEVKNVSTRFLAVSEEKSRMTYIIDEKCNEVRKYQRECEKYKTEMGHLESKLKYHINKLNIETEAKAVVERKLEEEKNAPNKLEEKANEKLKMEFEANTILLKHEITSKTEALDKLTKEQQKLSAANKELQNQLQEITTEHNQLTEEYNRLRELHNSVEGSYSDELLNSAKLRGQLEELQLLRTQNTINEEKLMDQQKRVQKLEALVQDNETDLEQLKVKRQELLTINKEMSELIVQLQNDICLAKAKAQGLDAENKLLKQEKLTYDTKYNQLEQQLSLEASEKNEERLLLAKHLSEKTKMYELTKQKLEDVQGDFEATQHKHATVLKELHRELNKYKRGITEPKTPISYCSNCQQAINGYPTENPQQRSHSRSSSHGSMHSGSRRASESSESETVASSATTVQQPPPQQDLQAVPSKKVLVERILRLQQATARQTERIEFLENHTAALVAEVQKKSKVVQHYMLRDQTAGALTTSRSDQNKSELVKYGNGIMAAIYGGGSSKTGGENKAMSLELSLEINKKLQAVLEDTLLKNITLKENLDVLGLEVDNLTRKLRSLEGSCK
Protein: Interphotoreceptor matrix proteoglycan 1 (Interphotoreceptor matrix proteoglycan of 150 kDa) (IPM-150) (Sialoprotein associated with cones and rods) (Q17R60)
Organism: Homo sapiens (Human)
Function: Chondroitin sulfate-, heparin- and hyaluronan-binding protein (By similarity). May serve to form a basic macromolecular scaffold comprising the insoluble interphotoreceptor matrix.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:29777959}. Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix {ECO:0000269|PubMed:29777959, ECO:0000269|PubMed:9719680, ECO:0000269|PubMed:9813076}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q8R1W8}.
Interaction partners:
- Very long chain fatty acid elongase 4
- Peripherin-2
Sequence:
MYLETRRAIFVFWIFLQVQGTKDISINIYHSETKDIDNPPRNETTESTEKMYKMSTMRRIFDLAKHRTKRSAFFPTGVKVCPQESMKQILDSLQAYYRLRVCQEAVWEAYRIFLDRIPDTGEYQDWVSICQQETFCLFDIGKNFSNSQEHLDLLQQRIKQRSFPDRKDEISAEKTLGEPGETIVISTDVANVSLGPFPLTPDDTLLNEILDNTLNDTKMPTTERETEFAVLEEQRVELSVSLVNQKFKAELADSQSPYYQELAGKSQLQMQKIFKKLPGFKKIHVLGFRPKKEKDGSSSTEMQLTAIFKRHSAEAKSPASDLLSFDSNKIESEEVYHGTMEEDKQPEIYLTATDLKRLISKALEEEQSLDVGTIQFTDEIAGSLPAFGPDTQSELPTSFAVITEDATLSPELPPVEPQLETVDGAEHGLPDTSWSPPAMASTSLSEAPPFFMASSIFSLTDQGTTDTMATDQTMLVPGLTIPTSDYSAISQLALGISHPPASSDDSRSSAGGEDMVRHLDEMDLSDTPAPSEVPELSEYVSVPDHFLEDTTPVSALQYITTSSMTIAPKGRELVVFFSLRVANMAFSNDLFNKSSLEYRALEQQFTQLLVPYLRSNLTGFKQLEILNFRNGSVIVNSKMKFAKSVPYNLTKAVHGVLEDFRSAAAQQLHLEIDSYSLNIEPADQADPCKFLACGEFAQCVKNERTEEAECRCKPGYDSQGSLDGLEPGLCGPGTKECEVLQGKGAPCRLPDHSENQAYKTSVKKFQNQQNNKVISKRNSELLTVEYEEFNHQDWEGN
Protein: RNA guanylyltransferase (Q381X9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Transcription initiation protein, putative
- Nuclear cap-binding protein subunit 2
- Plastid-encoded RNA polymerase subunit alpha
- RNA polymerase-like protein
- DNA-direcetd RNA polymerase II, subunit 9, putative
- DNA-directed RNA polymerase subunit beta
- [RNA-polymerase]-subunit kinase
- Trans sialidase, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II, putative
Sequence:
MSATDVASELRSGAPEYVPTFLRCKQSENVTAFESPVVFLMFGCRGAGKSTQSTLLSKTYNLLYLSSGDIYKSGKQPFVELRKILNEHFGDGKERVYNGVVLDRFIANSEFEAFYVQTALRSVGLPVPFVFMLAIDQGLAAKRAEERGDNKGGNQRWRAVEQKAQAITANTVYAPIQCLKTIRVESDMTIDDVFNEIKTTIANQLPPDLFNLQLPREARREVEGTVLVEDYELYMELANDVHTVVGNLRGRRDSAPLSNVGAHLDKEYFSFANKRLRSQLTTMHVTLKADGLRFLVMKHKTRGYIGFPSAFTHCYELNDLFEGVEMAPKPYTELKKWMNDKSCELPADFLLDTEVVVHEKKPTLYIIDFIYFWGLDGRRMQFEQRLKVLREYFGDMKPQGQVIAMKDYVPINKIRTLVEEMKRRTELPVDGLIFQHNGSYRFGSDKFLIKWKPVHLCTVDFRLANGRVENGVWTFDLFVTDDFIEENGFREVAYPGATALIPASVVEENGLQNGMIIEMALSEKESVKKTSPNAPSEKTRWTFRNARNDKPSPNKYSIVTRICELMHVDLDELVSLCEKVPFYRNV
Protein: Green fluorescent protein (P42212)
Organism: Aequorea victoria (Water jellyfish) (Mesonema victoria)
Function: Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
Interaction partners:
Sequence:
MSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFSYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITHGMDELYK
Protein: Polyadenylate-binding protein-interacting protein 2 (PABP-interacting protein 2) (PAIP-2) (Poly(A)-binding protein-interacting protein 2) (Q9D6V8)
Organism: Mus musculus (Mouse)
Function: Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Polyadenylate-binding protein-interacting protein 1
- Polyadenylate-binding protein 1
- Eukaryotic translation initiation factor 3 subunit J-A
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C
Sequence:
MKDPSRSSTSPSIINDDVIINGHSHEEDNPFAEYMWMENEEEFNRQIEEELWEEEFIERCFQEMLEEEEEHEWFIPARDLPQTMDQIQDQFNDLVISDGSSLEDLVVKSNLNPNAKEFVPGVKY
Protein: Collagen alpha-1(XVI) chain (Q07092)
Organism: Homo sapiens (Human)
Function: Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:9022684}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-3
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Matrix metalloproteinase-9
- Collagen alpha-2
Sequence:
MWVSWAPGLWLLGLWATFGHGANTGAQCPPSQQEGLKLEHSSSLPANVTGFNLIHRLSLMKTSAIKKIRNPKGPLILRLGAAPVTQPTRRVFPRGLPEEFALVLTLLLKKHTHQKTWYLFQVTDANGYPQISLEVNSQERSLELRAQGQDGDFVSCIFPVPQLFDLRWHKLMLSVAGRVASVHVDCSSASSQPLGPRRPMRPVGHVFLGLDAEQGKPVSFDLQQVHIYCDPELVLEEGCCEILPAGCPPETSKARRDTQSNELIEINPQSEGKVYTRCFCLEEPQNSEVDAQLTGRISQKAERGAKVHQETAADECPPCVHGARDSNVTLAPSGPKGGKGERGLPGPPGSKGEKGARGNDCVRISPDAPLQCAEGPKGEKGESGALGPSGLPGSTGEKGQKGEKGDGGIKGVPGKPGRDGRPGEICVIGPKGQKGDPGFVGPEGLAGEPGPPGLPGPPGIGLPGTPGDPGGPPGPKGDKGSSGIPGKEGPGGKPGKPGVKGEKGDPCEVCPTLPEGFQNFVGLPGKPGPKGEPGDPVPARGDPGIQGIKGEKGEPCLSCSSVVGAQHLVSSTGASGDVGSPGFGLPGLPGRAGVPGLKGEKGNFGEAGPAGSPGPPGPVGPAGIKGAKGEPCEPCPALSNLQDGDVRVVALPGPSGEKGEPGPPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGTTGRPGLSGEPGVQGPAGPKGEKGDGCTACPSLQGTVTDMAGRPGQPGPKGEQGPEGVGRPGKPGQPGLPGVQGPPGLKGVQGEPGPPGRGVQGPQGEPGAPGLPGIQGLPGPRGPPGPTGEKGAQGSPGVKGATGPVGPPGASVSGPPGRDGQQGQTGLRGTPGEKGPRGEKGEPGECSCPSQGDLIFSGMPGAPGLWMGSSWQPGPQGPPGIPGPPGPPGVPGLQGVPGNNGLPGQPGLTAELGSLPIEQHLLKSICGDCVQGQRAHPGYLVEKGEKGDQGIPGVPGLDNCAQCFLSLERPRAEEARGDNSEGDPGCVGSPGLPGPPGLPGQRGEEGPPGMRGSPGPPGPIGPPGFPGAVGSPGLPGLQGERGLTGLTGDKGEPGPPGQPGYPGATGPPGLPGIKGERGYTGSAGEKGEPGPPGSEGLPGPPGPAGPRGERGPQGNSGEKGDQGFQGQPGFPGPPGPPGFPGKVGSPGPPGPQAEKGSEGIRGPSGLPGSPGPPGPPGIQGPAGLDGLDGKDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSTGRPGAEGEPGAMGPQGRPGPPGHVGPPGPPGQPGPAGISAVGLKGDRGATGERGLAGLPGQPGPPGHPGPPGEPGTDGAAGKEGPPGKQGFYGPPGPKGDPGAAGQKGQAGEKGRAGMPGGPGKSGSMGPVGPPGPAGERGHPGAPGPSGSPGLPGVPGSMGDMVNYDEIKRFIRQEIIKMFDERMAYYTSRMQFPMEMAAAPGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGVRGLPGTKGEKGDIGIGIAGENGLPGPPGPQGPPGYGKMGATGPMGQQGIPGIPGPPGPMGQPGKAGHCNPSDCFGAMPMEQQYPPMKTMKGPFG
Protein: Uncharacterized protein (G8B5M3)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
Sequence:
MQYSKVAILSAVAGSAVASYNSTVTDIATTVVTITSCEENKCTEVPVTTGLTTVTEVDTIYTTYCPLPSTEAPESSAPETKAPETSAPASKAPESSAAESKSTVAAESSEAPSVSSFEAGAGKLQVGAALVGAAALLL
Protein: Putative histone deacetylase complex subunit cti6 (Q1MTR4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Could be a component of the RPD3C(L) histone deacetylase complex (HDAC).
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Transcriptional regulatory protein rxt2
- Transcriptional regulatory protein rxt3
- Transcriptional regulatory protein sds3
- Chromatin modification-related protein png2
- Histone deacetylase clr6
- Chromatin modification-related protein eaf3
- Paired amphipathic helix protein pst3
- Transcriptional regulatory protein dep1
- Histone deacetylase phd1
- Set3 complex subunit hif2
Sequence:
MPSNSTPANEEKEEESEKIQKSPVDTPHTPNGSVSDNEENETSSTGEVTRCVCGIVESDDEASDGGLYIQCDQCSVWQHGNCVGFADESEVPEVYYCEICHPEFHKVYQRGRGAKQSKYLGNGKPIEASQTEESSSTPPSPATKKSSKQRLTMNSRDAALDYEEYLAIAKEKSLIPRRSRGRTSSKSLSPPAPQDESQGTEINLKQKIEEENDEILEDSKESKDENEENKETSTTNVAETDAPEEETVDTVEEIADEEKHSVKEESGEASPQSSQQSTITSISTTTRSTRKAKREAAAEDKADLPAAVAPKPSKTRKVGGRRGKSSSNDNHRIPQLHPDGTFVETITKPKGLHSRITMTEMRRRVASMLEYIGHIQVEMAAQSAGNQSSTKSSKEGPEEEKETLRMVDNLTRDLLHWEQRFSRT
Protein: Axin interactor, dorsalization-associated protein (Axin interaction partner and dorsalization antagonist) (Q8C4Q6)
Organism: Mus musculus (Mouse)
Function: Acts as a ventralizing factor during embryogenesis (By similarity). Inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling.
Interaction partners:
Sequence:
MSEVTRSLLQRWGASLRRGADFDSWGQLVEAIDEYQILARHLQKEAQAQHNNSEFTEEQKKTIGKIATCLELRSAALQSTQSQEEFKLEDLKKLEPILKNILTYNKEFPFDVQPIPLRRILAPGEEENLEFEEDEEGGAGAGPPDSFSARVPGTLLPRLPSEPGMTLLTIRIEKIGLKDAGQCIDPYITVSVKDLNGIDLTPVQDTPVASRKEDTYVHFNVDIELQKHVERLTKGAAIFFEFKHYKPKKRFTSTKCFAFMEMDEIKPGPIVIELYKKPTDFKRKKLQLLTKKPLYLHLHQSLHKE
Protein: NTF2-related export protein (p15) (Q9V3H8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Stimulator of protein export for NES-containing proteins (By similarity). Plays a role in the nuclear export of mRNA. Also plays a role in the nuclear export of U1 snRNA, tRNA, and mRNA (By similarity). In ovaries, plays a role in transposable element silencing regulation. Forms a complex with nxf2, Panx and piwi which acts as effector of cotranscriptional transposon silencing. In ovarian follicle cells, enables the nuclear export of flamenco (flam) transcripts and subsequent piRNA biogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:31384064}. Nucleus envelope {ECO:0000269|PubMed:31384064}. Note=Associates with the nuclear pore complex. {ECO:0000269|PubMed:31384064}.
Interaction partners:
- Nuclear RNA export factor 2
- Nuclear RNA export factor 1
- LD14924p
- Nuclear export factor 4
- Protein panoramix
- NTF2-related export protein
- THO complex subunit 5
- E3 SUMO-protein ligase RanBP2
- Protein Rae1
- ATP-dependent RNA helicase WM6
Sequence:
MDSDLKAKVESCARTADTFTRLYYASVDNRRQQIGRLYLDNATLSWNGNGAIGRQMIESYFQELPSSNHQLNTLDAQPIVDQAVSNQLAYLIMASGSVKFADQQLRKFQQTFIVTAENDKWKVVSDCYRMQEV
Protein: Carboxypeptidase (EC 3.4.16.-) (O76725)
Organism: Caenorhabditis elegans
Interaction partners:
- Serine protease K12H4.7
- Putative serine protease F56F10.1
- EGF-like domain-containing protein
- Putative phospholipase B-like 2
Sequence:
MILLLFITLFALGSTAPADQQITSLPNLTEPLRSKHYAGYLSISDVKQLFYWYVESEESPETAPVVLWLNGGPGCASMEGLFIEMGPFRVRNYGEEVNRNPWTWNRIANIIYLDAPAGVGFSYYNTTKKVFTDDEVAQDNFNALKMWFARFPERKTNDFYIAGESYGGTYVPMLSARITKANVDFPQFKGMLVGNGCVDDQINFNTNIMYQYYHAVVDETQMQNVTQQCCNGTMDCDYYTISQGNDTCGDLVNQLSYSIYYTGYDPYFLYFACYLNPNLPYPPHEEIRKLQKNVLRNNLYKKIIGESPVLKNKYFYPPSNDIQGQPDCASHDDHFPYLNSPEVKKALRIPDYVPKYEMCNMEIAENYQSQYPTMKKFFDTVIDAKKHVAMFNGDADTLCNYVENSQFIYKTLKKTVKTAMMPWNDPVQLPMAVGQVTEYDGITLISIKGGGHFPAATEQKPKETFQMFQNYVKHQNYSTPVAFDKTFNLTSTIIAVGSKLFLSFCISIILFL
Protein: Protein phosphatase PP2A regulatory subunit A (PR65) (P31383)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subsets of substrates.
Interaction partners:
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
- Serine/threonine-protein phosphatase 2A activator 2
- Serine/threonine-protein phosphatase PP1-1
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Antagonist of mitotic exit network protein 1
- Protein phosphatase methylesterase 1
- Factor arrest protein 11
Sequence:
MSGARSTTAGAVPSAATTSTTSTTSNSKDSDSNESLYPLALLMDELKHDDIANRVEAMKKLDTIALALGPERTRNELIPFLTEVAQDDEDEVFAVLAEQLGKFVPYIGGPQYATILLPVLEILASAEETLVREKAVDSLNNVAQELSQEQLFSDFVPLIEHLATADWFSSKVSACGLFKSVIVRIKDDSLRKNILALYLQLAQDDTPMVKRAVGKNLPILIDLLTQNLGLSTDEDWDYISNIFQKIINDNQDSVKFLAVDCLISILKFFNAKGDESHTQDLLNSAVKLIGDEAWRVRYMAADRFSDLASQFSSNQAYIDELVQPFLNLCEDNEGDVREAVAKQVSGFAKFLNDPSIILNKILPAVQNLSMDESETVRSALASKITNIVLLLNKDQVINNFLPILLNMLRDEFPDVRLNIIASLKVVNDVIGIELLSDSLLPAITELAKDVNWRVRMAIIEYIPILAEQLGMQFFDQQLSDLCLSWLWDTVYSIREAAVNNLKRLTEIFGSDWCRDEIISRLLKFDLQLLENFVSRFTILSALTTLVPVVSLDVVTEQLLPFISHLADDGVPNIRFNVAKSYAVIVKVLIKDEAKYDALIKNTILPSLQTLCQDEDVDVKYFAKKSLAECQELLKN
Protein: ATP synthase mitochondrial F1 complex assembly factor 2 (ATP12 homolog) (Q8N5M1)
Organism: Homo sapiens (Human)
Function: May play a role in the assembly of the F1 component of the mitochondrial ATP synthase (ATPase).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11410595}; Peripheral membrane protein {ECO:0000305|PubMed:11410595}.
Interaction partners:
- ATP synthase mitochondrial F1 complex assembly factor 1
- ATP synthase F
- ATP synthase F
- Transmembrane protein 70
- ATP synthase F
- ATP synthase F
- ATP synthase F
- Protein FMC1 homolog
Sequence:
MWRSCLRLRDGGRRLLNRPAGGPSASMSPGPTIPSPARAYAPPTERKRFYQNVSITQGEGGFEINLDHRKLKTPQAKLFTVPSEALAIAVATEWDSQQDTIKYYTMHLTTLCNTSLDNPTQRNKDQLIRAAVKFLDTDTICYRVEEPETLVELQRNEWDPIIEWAEKRYGVEISSSTSIMGPSIPAKTREVLVSHLASYNTWALQGIEFVAAQLKSMVLTLGLIDLRLTVEQAVLLSRLEEEYQIQKWGNIEWAHDYELQELRARTAAGTLFIHLCSESTTVKHKLLKE
Protein: Adenosylhomocysteinase-like 1 (dAhcyL1) (Inactive S-adenosyl-L-homocysteine hydrolase) (S-adenosylhomocysteine hydrolase-like protein 1) (Q9VZX9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Might play a role in the regulation of methionine metabolism possibly by binding and inactivating Ahcy.
Interaction partners:
- Cystathionine beta-synthase
- Adenosylhomocysteinase-like 2
- Adenosylhomocysteinase
- Betaine-homocysteine S-methyltransferase
- FI01821p
- FI04487p
- cystathionine gamma-lyase
- S-adenosylmethionine synthase
- L-serine deaminase
- Methanethiol oxidase
Sequence:
MNNLADTVVVDPGFGGGDKQQQAGPAPQDASVVVPPPATKQSSALKKTSRYRSRSLSASSTDSFSSASYTGSSEDGDDVPPREKVQKNSKGSSDFCVRNIGAQHAFGRREIEIAEQEMPGIIALKKRAAEDKPLKDAKIVGCTHINAQTAVLIETLVELGASVRWAACNIYSTQNEVAAALAESGIPIFAWRGETEEDFWWCIDRCVNAENWQPNMILDDGGDATHLMLKKYPTMFKLVKGIVEESVTGVHRLYQLSKAGKLTVPAMNVNDSVTKTKFDNLYSCKESILDSLKRSTDVMFGGKQVVVCGYGDVGKGCAQALKGQGCIVYITEIDPICALQASMDGFRVVKLNEVIRNVDIVVTATGNKNVVVREHMDKMKSGCIVCNMGHSNTEIDVNGLRTPDLTWEKVRSQVDHIIWPEGKYIILLAEGRLVNLSCSSIPSFAVSITSATQALALIELFNAPPGRYKSDVYLLPKKMDEYVASLHLPTFDAHLTELSDEQAKYMGLNKAGPFKPNYYRY