wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic LigT (F4J1H2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein uL24c
- 2-succinylbenzoate--CoA ligase, chloroplastic/peroxisomal
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL46
- Endoribonuclease YBEY, chloroplastic
- Uncharacterized protein
- Chaperone DnaJ-domain superfamily protein
- Small ribosomal subunit protein uS17c
Sequence:
MFAYRTLFRIDRVFGFTSRCFQSKPESFSILSFRGSEKSAMDGYKKQKMVNLVWRPISTQTSSVIAEAGNEVQEVAQCSKSSDVSKEVIEGETASVVSAGKHSVSLEVGASLIKFIRGKEGTTQMKLEEEMGVKIILPSSRNKDHISIEGGSVDCVTKASKRIATIIDEVVRSPSLDYSHFVSLPLAIHPELVDKLVNFQNSILGIHSIASDKQDDQANRATTSVAVDLKANSETNQVNVGIKSIPIVSYPPKAKSKSSTLLDLGIEKSIFIKPSTFHLTVVMLKLWNKDRVNAACDVLKSIFPSVMDALDNKPVFIRLKGLDCMRGPLDKTRVLYAPVEEIGDEGRLLRACQVITDAFVKAGLVLEKDAKQSLKLHVTVMNARHRKRRKNNKKKMETFDAREIHKQFGNEDWGEYLIQEAHLSQRFVFDQNGYYRCCGSIPFPGEQRA
Protein: Zygote arrest protein 2.S (Zygote arrest protein 2) (Xzar2) (Zygote arrest protein 2A) (C0SPG1)
Organism: Xenopus laevis (African clawed frog)
Function: mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation. Probably promotes formation of some phase-separated membraneless compartment that stores maternal mRNAs in oocytes: acts by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (By similarity). Binds to the 3'-UTR of maternal mRNAs, inhibiting their translation.
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:C3VD30}.
Interaction partners:
- Protein furry homolog-like isoform X8
Sequence:
MAGFVYSPYNAYQGYGGNFGQNPHRPQAFPKNKQAAWKSNKSSEPPDYLDHFQRAQLKAILSQVNPNLTPRLRKVNTKEMGVQVNPRVDTGVQCSLGPRTLRRPPPPPSSPVKPTDCARFSRPVAVYSPVVDRRLFSLPQGGRLPKKSLPAPDSQSQPLKDRGPSPEEKEPETKEALEKSPVPGAEEPNEEEPNKPAFQFLEQKYGYFHCKDCKTRWESAYVWCISGSNKVYFKQLCRKCQKGFNPYRVEVIQCQVCAKTRCSCPQKKRHIDLKRPHRQELCGRCKNKKLSCDNTYSYKYIV
Protein: MAD2L1-binding protein (Caught by MAD2 protein) (p31(comet)) (Q15013)
Organism: Homo sapiens (Human)
Function: May function to silence the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 after it has become dissociated from the MAD2L1-CDC20 complex.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, spindle. Note=During early mitosis, unevenly distributed throughout the nucleoplasm. From metaphase to anaphase, concentrated on the spindle.
Interaction partners:
- Cell division cycle protein 20 homolog
- Pachytene checkpoint protein 2 homolog
- Mitotic spindle assembly checkpoint protein MAD2A
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Mitotic spindle assembly checkpoint protein MAD1
- Inositol polyphosphate 5-phosphatase K
Sequence:
MAAPEAEVLSSAAVPDLEWYEKSEETHASQIELLETSSTQEPLNASEAFCPRDCMVPVVFPGPVSQEGCCQFTCELLKHIMYQRQQLPLPYEQLKHFYRKPSPQAEEMLKKKPRATTEVSSRKCQQALAELESVLSHLEDFFARTLVPRVLILLGGNALSPKEFYELDLSLLAPYSVDQSLSTAACLRRLFRAIFMADAFSELQAPPLMGTVVMAQGHRNCGEDWFRPKLNYRVPSRGHKLTVTLSCGRPSIRTTAWEDYIWFQAPVTFKGFRE
Protein: Replication protein A 14 kDa subunit (RP-A p14) (Replication factor A protein 3) (RF-A protein 3) (P35244)
Organism: Homo sapiens (Human)
Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER), probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA. As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.
Subcellular location: Nucleus {ECO:0000269|PubMed:17596542, ECO:0000269|PubMed:9430682}.
Interaction partners:
- Replication protein A 70 kDa DNA-binding subunit
- Replication protein A 30 kDa subunit
- Replication protein A 32 kDa subunit
- DNA repair protein RAD52 homolog
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- Claspin
- DNA topoisomerase 3-alpha
- RecQ-mediated genome instability protein 1
- RecQ-like DNA helicase BLM
- CST complex subunit STN1
Sequence:
MVDMMDLPRSRINAGMLAQFIDKPVCFVGRLEKIHPTGKMFILSDGEGKNGTIELMEPLDEEISGIVEVVGRVTAKATILCTSYVQFKEDSHPFDLGLYNEAVKIIHDFPQFYPLGIVQHD
Protein: Protein tailless (Nuclear receptor subfamily 2 group E member 2) (P18102)
Organism: Drosophila melanogaster (Fruit fly)
Function: Orphan receptor that binds DNA as a monomer to hormone response elements (HRE) containing an extended core motif half-site sequence 5'-AAGTCA-3' in which the 5' flanking nucleotides participate in determining receptor specificity. This receptor binds to the consensus sequence [AG][AG]AAGTCAA. Plays a key role in the establishment of non-metameric domains at the anterior and posterior poles of the embryo. It may also play a role in the nervous system. The maternal terminal pathway activates the tll gene in the termini; TLL activity then represses segmentation and activates terminal-specific genes in these domains. Involved in the regulation of early eye development. In the embryonic visual system anlage drives cells to optic lobe as opposed to Bolwig's organ fate.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Huckebein
- Protein hunchback
- Fork head domain transcription factor slp1
- Homeotic protein bicoid
- Segmentation protein even-skipped
- Segmentation protein fushi tarazu
- Grunge, isoform J
- Protein fork head
Sequence:
MQSSEGSPDMMDQKYNSVRLSPAASSRILYHVPCKVCRDHSSGKHYGIYACDGCAGFFKRSIRRSRQYVCKSQKQGLCVVDKTHRNQCRACRLRKCFEVGMNKDAVQHERGPRNSTLRRHMAMYKDAMMGAGEMPQIPAEILMNTAALTGFPGVPMPMPGLPQRAGHHPAHMAAFQPPPSAAAVLDLSVPRVPHHPVHQGHHGFFSPTAAYMNALATRALPPTPPLMAAEHIKETAAEHLFKNVNWIKSVRAFTELPMPDQLLLLEESWKEFFILAMAQYLMPMNFAQLLFVYESENANREIMGMVTREVHAFQEVLNQLCHLNIDSTEYECLRAISLFRKSPPSASSTEDLANSSILTGSGSPNSSASAESRGLLESGKVAAMHNDARSALHNYIQRTHPSQPMRFQTLLGVVQLMHKVSSFTIEELFFRKTIGDITIVRLISDMYSQRKI
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 13 (ADAM-TS 13) (ADAM-TS13) (ADAMTS-13) (EC 3.4.24.87) (von Willebrand factor-cleaving protease) (vWF-CP) (vWF-cleaving protease) (Q76LX8)
Organism: Homo sapiens (Human)
Function: Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation.
Subcellular location: Secreted {ECO:0000269|PubMed:12791682}. Note=Secretion enhanced by O-fucosylation of TSP type-1 repeats.
Interaction partners:
- von Willebrand factor
- Coagulation factor VIII
- Platelet glycoprotein Ib alpha chain
- Complement factor H
- Complement factor H-related protein 1
- Complement factor H-related protein 3
- Haptoglobin
- Diacylglycerol kinase epsilon
- Complement C3
- Complement factor I
Sequence:
MHQRHPRARCPPLCVAGILACGFLLGCWGPSHFQQSCLQALEPQAVSSYLSPGAPLKGRPPSPGFQRQRQRQRRAAGGILHLELLVAVGPDVFQAHQEDTERYVLTNLNIGAELLRDPSLGAQFRVHLVKMVILTEPEGAPNITANLTSSLLSVCGWSQTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLITEDTGFDLGVTIAHEIGHSFGLEHDGAPGSGCGPSGHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVWDPPRPQPGSAGHPPDAQPGLYYSANEQCRVAFGPKAVACTFAREHLDMCQALSCHTDPLDQSSCSRLLVPLLDGTECGVEKWCSKGRCRSLVELTPIAAVHGRWSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACEKTQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLSLCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTCSPRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVRIGGRYVVAGKMSISPNTTYPSLLEDGRVEYRVALTEDRLPRLEEIRIWGPLQEDADIQVYRRYGEEYGNLTRPDITFTYFQPKPRQAWVWAAVRGPCSVSCGAGLRWVNYSCLDQARKELVETVQCQGSQQPPAWPEACVLEPCPPYWAVGDFGPCSASCGGGLRERPVRCVEAQGSLLKTLPPARCRAGAQQPAVALETCNPQPCPARWEVSEPSSCTSAGGAGLALENETCVPGADGLEAPVTEGPGSVDEKLPAPEPCVGMSCPPGWGHLDATSAGEKAPSPWGSIRTGAQAAHVWTPAAGSCSVSCGRGLMELRFLCMDSALRVPVQEELCGLASKPGSRREVCQAVPCPARWQYKLAACSVSCGRGVVRRILYCARAHGEDDGEEILLDTQCQGLPRPEPQEACSLEPCPPRWKVMSLGPCSASCGLGTARRSVACVQLDQGQDVEVDEAACAALVRPEASVPCLIADCTYRWHVGTWMECSVSCGDGIQRRRDTCLGPQAQAPVPADFCQHLPKPVTVRGCWAGPCVGQGTPSLVPHEEAAAPGRTTATPAGASLEWSQARGLLFSPAPQPRRLLPGPQENSVQSSACGRQHLEPTGTIDMRGPGQADCAVAIGRPLGEVVTLRVLESSLNCSAGDMLLLWGRLTWRKMCRKLLDMTFSSKTNTLVVRQRCGRPGGGVLLRYGSQLAPETFYRECDMQLFGPWGEIVSPSLSPATSNAGGCRLFINVAPHARIAIHALATNMGAGTEGANASYILIRDTHSLRTTAFHGQQVLYWESESSQAEMEFSEGFLKAQASLRGQYWTLQSWVPEMQDPQSWKGKEGT
Protein: Proteasome component ecm29 (Q9P7H8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Stabilizes the proteasome holoenzyme, probably by tethering the 20S proteolytic core particle and the 19S regulatory particle. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 26S proteasome regulatory subunit rpn11
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit rpn12
- Proteasomal ubiquitin receptor ADRM1 homolog rpn1301
- 26S proteasome regulatory subunit rpn10
- Proteasomal ubiquitin receptor ADRM1 homolog rpn1302
- Probable 26S proteasome subunit rpt4
- 26S proteasome regulatory subunit 8 homolog
- 26S proteasome regulatory subunit 4 homolog
- Probable 26S proteasome regulatory subunit rpn3
Sequence:
MAENELRLLNNAELKLALAESEDSFQSLVSVFLCPILLKLDSPHESVRNKTISIANHIMTRLNNNAQAILPLEALVSQYVEANQPLRKRFLLAFISIGEKRIPCSENLALLQICLNHVNEYPLVLLTLTIRLLRFSKPTSAITCSNDVILSLSSFYLIQKDQRIFSDLQFSQKTVDYRLSLLRWIHLSSWPSNWKWLAYFFASADSHSEVARLADEFTRDSGLPDLENLSHVNVLLDIALDKFRIEALHANFSVSISLRNKAIQHLLKSKIAANTDKAINCIEFILEAPPSMQPRLIQFTRWVVDKADPNFLKPKAAMILEKILSILSSNIIQSDLLRGFLYTTIGLLTKVDNHLITNSLLTNLLTSLQSELPDVRVSIDEALSIIIPYYSNFRFSNELLPVLEPFIFDSPESPAAYCALRFVLVAFPFDYLPARFICLKVQNPFVFHHSFIEEAKKGLNLSQWVQYNSVYSTNEAQEEDKVRAASYPSASEVISFILSDHDLKKFWESNAAEYCLAILEFIERCIYYSADRSLELYDNDKLSSIDALLIQDSKLREMVSEKCISLSNFNVFLEYVFYGTLLMHFEPTYALSRLVSFAPPEVTFSLPELDFLTSVFNFPLALRNTATRILGIILSTKDSTRISEVLSSCFTIISTSNNKNDNFFKAETALLIIGYTISYLAAQTNSAAVDSFILNSGSIKEFFSVLLEYLGSNVLHKKTTSLAIYKELFVYFTRDWITSYGVDFDEILNVLLRFLKEVEDTNVKVECLHVISRMSLSFSDDEMAEKILKAIYVTYHMDSPDILFASAEAMSILAGGHRNVFVKSTCPIFFQKQLDNYKADHYCFTLDFILTDCVNSPKPLLRRASSLWLFYIVRYCEPQTYTMTRLNDIYHSFLSFLVTQDDFVQDTASRGLKAMYDVLEGDERKSFTDNLISTIAADRVDEKTKAPLDADTALFTTNKGTVATYKDICSLASESGNPDLIYSFLSIAGNSSLWQARKGLASGISYLGIPEDQKRKTFSFDTSKSSSLLKKLYRFKHDPNPDVAKTMGEIWDTLVPSDLNLASHRKYLVEDCLEFMGSRSWRDRESSVNTLVSLLSNVPVTEYLNQLEDIWNMSFRTLDDIKESVREASFPLCKLLARSVIQSLEKTSHNTSPSGICKGKRIVSVALPFLLKHAYDQAKEVRSLTYSTITELVRTGNSTLTSFVPAIMQVMLEYLTEYESKAATFLDFHAKNYSIKQENIDNARTSAVQSSSMMDTLEKCIGLLDESSMQTLYPILNRMIAKPGGVPTKIGSAQVVMLLVIRRGPLVKQFASKLLQSLKSSCFDRNAAVSDAFASAIGYLLRVCPLEIASQTCQEIIDKFYDGNTNEQIISSKLTVYASRYAPDVFLNLGSLFFPFIFFGKHSSSISINGVLSKAWDELSSAGSSVNLYSEEIILLIQKNLIVTKWDVKRPAAAALLEFVNTSRLTYRQNDIYVLLNETMKDKSWPGKELLLEAYVKFLIKYPEFIKSQKMEEVHQVIVREFKRRNIVYKSHAMESVGELLSDENYRELDLYELSLNECGTFLQKEWFDKDDELNLEEKIALQRNSVYAMFNSSRPGNKNCNEMLLTYLSNALDENYLHWNVKLAILKNAPHLKKIMSNEEFLLYKDILYRCYEDNPSPKAKDYAEVIFGENYLSVLRN
Protein: Hyaluronan synthase 3 (EC 2.4.1.212) (Hyaluronate synthase 3) (Hyaluronic acid synthase 3) (HA synthase 3) (O00219)
Organism: Homo sapiens (Human)
Function: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of three isoenzymes responsible for cellular hyaluronan synthesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25795779, ECO:0000269|PubMed:26883802, ECO:0000269|PubMed:30394292}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:25795779}; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:O08650}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:26883802}. Note=Travels from endoplasmic reticulum (ER), Golgi to plasma membrane (PubMed:26883802). Actives only when present in plasma membrane (By similarity). O-GlcNAcylation controls its membrane localization (PubMed:26883802). A rapid recycling of HAS3 between plasma membrane and endosomes is controlled by the cytosolic levels of UDP-GlcUA and UDP-GlcNAc (PubMed:26883802). {ECO:0000250|UniProtKB:O08650, ECO:0000269|PubMed:26883802}.
Interaction partners:
- UDP-glucose 6-dehydrogenase
- CD44 antigen
Sequence:
MPVQLTTALRVVGTSLFALAVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQSLFAFLEHRRMRRAGQALKLPSPRRGSVALCIAAYQEDPDYLRKCLRSAQRISFPDLKVVMVVDGNRQEDAYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMDRVRDVVRASTFSCIMQKWGGKREVMYTAFKALGDSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIGLIPVSIWVAVLLGGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCGKKPEQYSLAFAEV
Protein: Protein PafC (Proteasome accessory factor C) (P9WIL9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the pafABC operon, but PafC does not seem to be involved in pupylation or substrate degradation. Appears to play at least a small role in resistance to reactive nitrogen intermediates (RNI) in vitro.
Interaction partners:
- Protein PafB
- Pup--protein ligase
- RNA polymerase-binding protein RbpA
- DNA-directed RNA polymerase subunit omega
- DNA-directed RNA polymerase subunit beta
- RNA polymerase sigma factor SigA
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta'
- Proteasome subunit alpha
- Sec-independent protein translocase protein TatA
Sequence:
MSALSTRLVRLLNMVPYFQANPRITRAEAAAELGVTAKQLEEDLNQLWMCGLPGYSPGDLIDFEFCGDTIEVTFSAGIDRPLKLTSPEATGLLVALRALADIPGVVDPQAARSAIAKIAAAAGAVAAVAEQAPTESPAAAAVRAAVRNSRALTIDYYAASHDTLTTRIVDPIRVLLIGGHSYLEAWSREAEGVRLFRFDRIVDAAELGEPAVPPESARQAPPDTSLFDGDLSLPSATLRVAPSASWMLEYYPIRELRQLPDGSCEVAMTYASEDWMTRLLLGFGSDVRVLAPESLAQRVRDAATAALDAYQAAAPP
Protein: SAM-dependent methyltransferase TRM5/TYW2-type domain-containing protein (Q38BT8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Multifunctional methyltransferase subunit TRM112
Sequence:
MGIVRVQRPLLWLLGAVFLLWVLRRQRRCSRFFASLKTSILKKLTCKRLGRKQPRVAVRKVDLFVEKVLAQGGLQDVDKIVGIFPRHFELVGHVVVVKLNRGIARDVFAPYARALAESFFPRVIDVVLLDTMGIVGELREPHLEVLWSSATSHFSVNDSLLKVTKERVRKASTFTSEDAELLGSCAEAVTFTTHVENGVRYSFDACKVMFCSGNVTERMHFASIIAKDEVVVDMFAGIGYFTLPLAINGGVKIVHALEKNKYSALYLAFNAVQNKVSDLIVIHCGDNRDVGSELCGRCDRVIMGYIPSCESFLPRAISFLRRSTRGEPMGVVHYHLLSEKDQVINTVTHHVRSTLDEATTSLMRIVNFRMVKSYAPKRFHFVVDMHFSSLQEPE
Protein: RNApolymerase 14 kDa subunit (A8MRK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase III subunit RPC6
- DNA binding / DNA-directed RNA polymerase
- DNA-directed RNA polymerase I subunit 2
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit 1
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase III subunit 2
- DNA-directed RNA polymerase family protein
Sequence:
MLVYIHVMLLEILIVFNECHIILSLRLMELICWCVDNDDYVNNQYCFQFCSPRVTVAAYTIPHPSLEQVNIRVQTTGDPAREVFKDACQELMQMNRHVRSVFDKAVAEYKDEQKRKEEAEEEELKRQRDLFGSMDIENN
Protein: Cytospin-B (Nuclear structure protein 5) (NSP5) (Sperm antigen HCMOGT-1) (Sperm antigen with calponin homology and coiled-coil domains 1) (Q5M775)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:15602574}.; SUBCELLULAR LOCATION: [Isoform 3]: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 5]: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- SH2 domain-containing protein 3C
- SH2 domain-containing protein 3A
- Histone deacetylase 2
- Serine protease 57
- Structural maintenance of chromosomes protein 1A
- Large ribosomal subunit protein mL62
Sequence:
MRSAAKPWNPAIRAGGHGPDRVRPLPAASSGMKSSKSSTSLAFESRLSRLKRASSEDTLNKPGSTAASGVVRLKKTATAGAISELTESRLRSGTGAFTTTKRTGIPAPREFSVTVSRERSVPRGPSNPRKSVSSPTSSNTPTPTKHLRTPSTKPKQENEGGEKAALESQVRELLAEAKAKDSEINRLRSELKKYKEKRTLNAEGTDALGPNVDGTSVSPGDTEPMIRALEEKNKNFQKELSDLEEENRVLKEKLIYLEHSPNSEGAASHTGDSSCPTSITQESSFGSPTGNQMSSDIDEYKKNIHGNALRTSGSSSSDVTKASLSPDASDFEHITAETPSRPLSSTSNPFKSSKCSTAGSSPNSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPPVDEEPESSEVDAAGRWPGVCVSRTSPTPPESATTVKSLIKSFDLGRPGGAGQNISVHKTPRSPLSGIPVRTAPAAAVSPMQRHSTYSSVRPASRGVTQRLDLPDLPLSDILKGRTETLKPDPHLRKSPSLESLSRPPSLGFGDTRLLSASTRAWKPQSKLSVERKDPLAALAREYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLELSEMLYTDRPDWQSVMQYVAQIYKYFET
Protein: Agamous-like MADS-box protein AGL63 (Protein GORDITA) (Q9SA07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in the regulation of fruit growth. Contributes to integument development. Controls organ size via cell expansion. Involved in the regulation of longitudinal growth of the fruit evenly throughout the radial axis. Functions redundantly with TT16/AGL32 to repress nucellus growth and promote its degeneration.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Agamous-like MADS-box protein AGL62
- Protein SENSITIVITY TO RED LIGHT REDUCED 1
- Protein PAF1 homolog
- Glycine-rich RNA-binding protein 8
- Protein SUPPRESSOR OF FRI 4
Sequence:
MRKGKRVIKKIEEKIKRQVTFAKRKKSLIKKAYELSVLCDVHLGLIIFSHSNRLYDFCSNSTSMENLIMRYQKEKEGQTTAEHSFHSDQCSDCVKTKESMMREIENLKLNLQLYDGHGLNLLTYDELLSFELHLESSLQHARARKSEFMHQQQQQQTDQKLKGKEKGQGSSWEQLMWQAERQMMTCQRQKDPAPANEGGVPFLRWGTTHRRSSPP
Protein: Inner kinetochore subunit CNN1 (CENP-T homolog) (Co-purified with NNF1 protein 1) (Constitutive centromere-associated network protein CNN1) (P43618)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly. CNN1 is important for the recruitment of the outer kinetochore Ndc80 complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:22561345, ECO:0000305|PubMed:22561346}. Note=Enriched at the kinetochore in anaphase. {ECO:0000269|PubMed:22561345}.
Interaction partners:
- Inner kinetochore subunit MCM22
- Inner kinetochore subunit WIP1
- Kinetochore protein SPC24
- Kinetochore protein SPC25
- Inner kinetochore subunit CTF3
- Inner kinetochore subunit MCM16
- Inner kinetochore subunit AME1
- Inner kinetochore subunit OKP1
- Inner kinetochore subunit NKP1
- Kinetochore-associated protein DSN1
Sequence:
MSTPRKAAGNNENTEVSEIRTPFRERALEEQRLKDEVLIRNTPGYRKLLSASTKSHDILNKDPNEVRSFLQDLSQVLARKSQGNDTTTNKTQARNLIDELAYEESQPEENELLRSRSEKLTDNNIGNETQPDYTSLSQTVFAKLQERDKGLKSRKIDPIIIQDVPTTGHEDELTVHSPDKANSISMEVLRTSPSIGMDQVDEPPVRDPVPISITQQEEPLSEDLPSDDKEETEEAENEDYSFENTSDENLDDIGNDPIRLNVPAVRRSSIKPLQIMDLKHLTRQFLNENRIILPKQTWSTIQEESLNIMDFLKQKIGTLQKQELVDSFIDMGIINNVDDMFELAHELLPLELQSRIESYLF
Protein: Ankyrin repeat domain-containing protein 27 (VPS9 domain-containing protein) (Q96NW4)
Organism: Homo sapiens (Human)
Function: May be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and regulate endosome dynamics. May regulate the participation of VAMP7 in membrane fusion events; in vitro inhibits VAMP7-mediated SNARE complex formation by trapping VAMP7 in a closed, fusogenically inactive conformation. Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with Rab32, Rab38 and VAMP7 (By similarity). Involved in the regulation of neurite growth; the function seems to require its GEF activity, probably towards Rab21, and VAMP7 but not Rab32/38 (By similarity). Proposed to be involved in Golgi sorting of VAMP7 and transport of VAMP7 vesicles to the cell surface; the function seems to implicate kinesin heavy chain isoform 5 proteins, GOLGA4, RAB21 and MACF1. Required for the colocalization of VAMP7 and Rab21, probably on TGN sites. Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with VPS29. Regulates the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (By similarity).
Subcellular location: Early endosome {ECO:0000269|PubMed:16525121, ECO:0000269|PubMed:24856514}. Late endosome {ECO:0000269|PubMed:23104059}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23104059}. Lysosome {ECO:0000269|PubMed:23104059}. Cell membrane {ECO:0000269|PubMed:23104059}. Melanosome {ECO:0000250|UniProtKB:Q3UMR0}. Note=Colocalizes with VAMP7 in transport vesicles in the shaft of hippocampal neurons (By similarity). {ECO:0000250|UniProtKB:Q3UMR0}.
Interaction partners:
- Ras-related protein Rab-32
- Vesicle-associated membrane protein 7
- Vacuolar protein sorting-associated protein 29
- Ras-related protein Rab-21
- Ras-related protein Rab-38
- Golgin subfamily A member 4
- Vacuolar protein sorting-associated protein 35
- Kinesin heavy chain isoform 5A
Sequence:
MALYDEDLLKNPFYLALQKCRPDLCSKVAQIHGIVLVPCKGSLSSSIQSTCQFESYILIPVEEHFQTLNGKDVFIQGNRIKLGAGFACLLSVPILFEETFYNEKEESFSILCIAHPLEKRESSEEPLAPSDPFSLKTIEDVREFLGRHSERFDRNIASFHRTFRECERKSLRHHIDSANALYTKCLQQLLRDSHLKMLAKQEAQMNLMKQAVEIYVHHEIYNLIFKYVGTMEASEDAAFNKITRSLQDLQQKDIGVKPEFSFNIPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSLAKDELGYCLTSFEAAIEYIRQGSLSAKPPESEGFGDRLFLKQRMSLLSQMTSSPTDCLFKHIASGNQKEVERLLSQEDHDKDTVQKMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYDVESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVMEAYHLSFERRQKSSEAPVQSPQRSVDSISQESSTSSFSSMSASSRQEETKKDYREVEKLLRAVADGDLEMVRYLLEWTEEDLEDAEDTVSAADPEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCAEQNSKIMELLQVVPSCVASLDDVAETDRKEYVTVKIRKKWNSKLYDLPDEPFTRQFYFVHSAGQFKGKTSREIMARDRSVPNLTEGSLHEPGRQSVTLRQNNLPAQSGSHAAEKGNSDWPERPGLTQTGPGHRRMLRRHTVEDAVVSQGPEAAGPLSTPQEVSASRS