wanglab/gogpt-training-data huggingface dataset:
Protein: Endoribonuclease YbeY (EC 3.1.-.-) (Q8CAV0)
Organism: Mus musculus (Mouse)
Function: Single strand-specific metallo-endoribonuclease involved in rRNA maturation.
Interaction partners:
- Superoxide dismutase, mitochondrial
- GTPase Era, mitochondrial
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein mL46
- Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 3
Sequence:
MSLVIKNLQRVVPIRRVPLRRKMDLVRSILGVKKFDLGIICVDNKTIQNINRIYRNKNVPTDVLSFSFHENLKAGEFPQPHSPDDYNLGDIFLGVEYILQHCRESEDYCDVLTVTATHGLCHLLGFTHSSKAEWQKMYNQEKLVLEELSRYTGARLQPLSRGLY
Protein: Odd-paired-like (ZIC family member 1 (Odd-paired homolog, Drosophila)) (Zinc finger protein ZIC 1) (O93311)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Forkhead box protein D3
- Muscle segment homeobox 1a.
- Paired box 3a
- Transcription factor SOX-10
- Homeobox protein GBX-2
- Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1
- V
- Paired box 7a
- Transcription factor AP-2-epsilon
- Transcription factor AP-2-alpha
Sequence:
MLLDAGPQYPTIGVTTFGSTRHHSTGEVTDREVALGINPFADGMGAFKINHSSHDLGSGQTAFSSQAPGYAAAALGHHHHPTHVSSYSTAAFNSTRDFLFRNRGFGDATSAQHSLFASAAGSFAGPHGHSDAAGHLLFPGLHEQAATHASSNVVNSQMRLGFSGDMYGRAEQYGHVASPRSEHYASTQLHGYGPMNMNMAAHHGAGAFFRYMRQPIKQELICKWIEPEQLTNPKKSCNKTFSTMHELVTHLTVEHVGGPEQSNHICFWEECGREGKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHESSSQGSQPSPAASSGYESSTPPTIVSPSTENQSSSSISPASSTVHHTSSHSTLSSNFNEWYV
Protein: HtrA serine peptidase 2 (B0BNB9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- E3 ubiquitin-protein ligase XIAP
- Serine/threonine-protein kinase PINK1, mitochondrial
- RING-type E3 ubiquitin transferase
- RING-type E3 ubiquitin transferase
- Cytochrome c, somatic
- Diablo IAP-binding mitochondrial protein
- Tumor necrosis factor receptor superfamily member 1A
- Baculoviral IAP repeat-containing protein 5
- TNF receptor-associated factor
- Endonuclease.
Sequence:
MAALKAGRGANWSLRAWRALGGIFWRKGPLLAPDLRALLTSGTPDPQARMTYGTPSLPARVPLGVLASRANLTSGTPDLWVRLTVGTPGSSDQEDCGSPGSRRREWLAVALGAGGAVLLLLWGWGRGPSTVLAAVPAPPPTSPRSQYNFIADVVEKTAPAVVYIEILDRHPFSGREVPISNGSGFIVASDGLIVTNAHVVADRRRVRVRLPSGDTYEAMVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVTAGISFAIPSDRLREFLHRGEKKNSWFGISGSQRRYIGVMMLTLTPSILAELQLREPSFPDVQHGVLIHKVILGSPAHRAGLRPADVILAIGEKMIQNAEDVYEAVRTQSQLAVRIRRGPETLTLYVTPEVTE
Protein: RE37904p (Q8MRB0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCSPAAATVAAAAGAAPIPAATAITTADPAATATATRVLQQQQLQQQVQVQHPQQLQLSQQQQQLQQELPLISDQYQTTSFQPHAVTLKDYDAQTLQQFGGQLDLCCASSFNQNHFYLSSPGFPRTVLNYLLPNQQRDCVFYIEKSSPNVCRLRIQFKFFDFGQNSGGSIGGSFGDGFGGGVSGGLGGGHSGGFGGQHNCNGDFLELDGQRYCGCRSGYVHKSHWDQGRKALRMRIGQSSSTTSNGFLLEIFQDQDSDGCRQDAGQGFGLGLQPQQPQRGLGLWPQGLQPQLGLQPQLGLQPQLGLPPQTAQMWPLQPGYPGYISGYPLPFSATPYRTARRISYARGIDAQQPSRVVETNSTRKEFYYFDGDEAFARSAVDDEDEDKAHLGVTTQPQSSSQSIVKPESPLVTKAFEQSSCSFDYMEVLKLSVDTLWLTKPLCFSPLRSWFPNIFG
Protein: RRM domain-containing protein (O45189)
Organism: Caenorhabditis elegans
Interaction partners:
- RNA-binding protein ASD-1
- Myoblast growth factor receptor egl-15
- RRM domain-containing protein
- Mec-8 protein
- RNA-binding protein sym-2
- RING-type domain-containing protein
- RRM domain-containing protein
- U1 small nuclear ribonucleoprotein C
Sequence:
MYGQVQDPLVHAAAAALAQSTNAEPVVGSRDTMFTKIFVGGLPYHTSDKTLHEYFEQFGDIEEAVVITDRNTQKSRGYGFVTMKDRASAERACKDPNPIIDGRKANVNLAYLGAKPRTNVQLAALAAGQVQLPLTTQLQALFQPRMGLPQMYYPTVTGLVNPLMAQQGAAAQQQLFDYNALAAVMNPQAAAAYGIQSQGKFAAAPTTIEQYAAYPAGYGLVPQSAYNIGNPQLQQLAAAQQQLEHQRV
Protein: Plexin B2 (Plexin-B2a precursor) (C5H5I1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MAWRALSAFSLLLCFGSSCCDDAQEQFSSPTIINNVVQDPQTGRIYLGAVNGIFQLNHNLQEEGRADTGPKKDNPQCTPPITAQCTDAKEMDNFNKLLLVNSANGTLIVCGSLFRGICSLVNLNSVNKPVYYSDTKGEKTYVASTEESVTVVGVISYFKDTTTNANLSVFLVGKGYGSSDSSKLISTRLLQEHGEMDVFENMVEASTVQTSAFVLRYHHDFRYTFKDNGYIYFLFSRSPGTSDSTKITFIARLCENDHHYYSYTELQLNCTVNTEQQGNTFNKVQAAYLAKPGKDLAQNIVPSNLNDKVLFGVFSADEADGRSALCMYPLSSINARFEEVIESCYTGEVLEDDKPKTVYSPYNSKNEAICKTKRDKNMVKAYICGAEFLPSPLASKPEYALAVKPIYTRNDMLTAVAVAVENEHTVAFLGTSGADVLKVHLDPNHTDFYNRIPGDRADGAVNKNLLFDSTLNHLYITTGKKISKVSVQACEQREDCHSCVSQRDPYCGWCVLEGRCTRKKDCRKGDGENAWLWSPKQTCVTIQSFEPPNISCKKTDSTQVVINIPSLPSISSPDRLECVFDGYRSQAKMEDTRVTCYLPSSDYIPPTPETQDFVAVPVKITVNDKIEVASSVFEFYNCAGVVKKSENTPCIACVTSKWGCQWNIQDHTCSDKDDSAHGSHIIGNMEANLCPQFEIPEPLRIPVGYKTPITFHGKNLDIYWGKTFQIGTELMKQVGEVTVEADGLKYRFEGYEFAYDKEPEVNVTFYIKDKDTDRKIDSTLRVVLYNCSVRREDCSLCKNAHKNDSCVWCDTTKSCIYRSLCDNELHQCPPPKITDIVPRYGPMNGRISVTIKGSNLGIKKEDIKKITVAKVPCIHQPERYSVSTSVVCEIGPFPSPPEDLPISPSKSGPVEVLVEGERTGTSEVEFTYRDPVPEAVFPVKGPAAGGTVITITGQDLDSASKDDITITVDKEPCEVLTFGHEITCRTGPYKGQKIPSDKLPVIVKYGKDTVKTVDAFEYSPDPKISEYFPQTSFVCGGRRILVIGSGFDQVQRATMRVLPSSDEFDVKASNVEFFQEVEKKNETTLEFLSPVVNKTYINLSLRTVIQLDNLVLNLTDFAYHPDPHFNKLKDKAITEGSIINVNGRGFAKAMTAKEAQAFVGDESCLVTILEDDKLFLVAPSSPPKSTSRRHRRDTSSDALELLIKFGNGEWNVGSVRFERKYEVPLYIIIPAVLIPMVLFIAVSIYCYRRKSQQAEREYEKIKNQLANLEESVRDRCTKEFTDLMIEMEDHTSDLSEARIPFLDYKNYTDRVFFLPSKDGANDVMITGKLDIPDNRRAIVDQALNQFSNLLNSKTFLINFIRTLEGRQEFNARNKVYFASLLTVALHGKLEYYTDIMRTLLLELMEEYVHSKNPKLMLRRSETVVERMLCNWMSICLYQFLKDSAGEPLYKLFKAIKHQVEKGPVDAKMKKAKYTLNDTGLLGDDVEYSILTLQVLVHGEGPDVTPVKVLNCDTISQVKEKIIEQVYRNLPYSQRPVVDSVALEWRPGSTGQILSDLDLTSQKEGRWKRINTLAHYNVRDGATLVLSRVLHTQQSFDQNMDNHEERNALLEDDKVFHLVRPADELEEVKSKRGSMKDKATTKAITEIYLTRLLSMKGTLQQFVDDFFRSVLCSGTVVPPAVKYFFDFLDEQAQKHDNVDDETIHIWKTNSLPLRFWVNILKNPHFIFDVHLTEVVDASLSVIAQTFMDACTKTEHKLTRESPSNKLLYAKEISTYKKMVDDYYKGIRQMVPVSDQDMNTHLAEISRSHTDKLNTQAALHQLYQYASKYYDGIISSLEEDPAAQSKQLTLRLQQIAAALENKVTDL
Protein: Ankyrin repeat and KH domain-containing 1 (Ankyrin repeat and KH domain-containing protein 1 isoform X1) (E9QEX9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MQDAVAGTAMLTDGFEDEIDSVTPRSPALGMGVGATPGAGLGGLGIGVGGKKVRLFGEAGGPTTDRLDFKLTAAAVLSSGPGSGSDEDEVSEVESFILDQEDLDNPVLKTASELLLSSAADGADLRTVDPETQARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAENTLNASQADNLVIFSRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDITPLMAAASGGYVDIVKLLLVHGADVNAQSSTGNTALTYACAGGFLDVVKVLLKEGANIEDHNENGHTPLMEAASAGHVEVARVLLEYGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTLACCGGFLEVADFLIKAGADIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQTGADLEHESEGGRTPLMKAARAGHLCTVQFLISKGANVNRATANNDHTVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVVSYLLDYPNNILSVPAPDLSQLTPPSHDTSQAPRVPFQALAMVVPPQEPDRVPSTIPTPPPVTSKGASKQRLSSLQSNSVASGGLDADLLPPFHPYQPLECIVEETEGKLNELGQRISAIEKAQLQSLELIQGEPLTKDKIEELKKSREEQVQKKKKILKELQKVERQLQLKTQQQFTKEYMETKGLKEELGQAAGVEMPGTPLPLQATQLGSDNECEGIHEKEDHRPTPTNEEDEDEEEDEDDIDCAKLPQVNTILQPPPPPPPQNQVLQSPPLQTSFVPIQPLTPQLSTDFSSAEYPGSSSPDLQRVLLGQPLTGLGPGLLAQASDGLMVATPAQTLTDTLDDIMAAVNSRVPVVNTTTSPSPQPSAQTPINTASPPSMLPLYPSVDIDAHTESNHDTALTLACAGGHEELVSVLIARGANIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTKDTPLSLACSGGRQEVVELLLLRGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQIETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSSRDTALTIAADKGHYKFCELLISRGAHIDVRNKKGNTPLWLAANGGHFDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVQYLVKEVNQFPSDIECMRYIATIADKELLKKCHQCMETIVKAKDQQAAEANKNASILLKELDLEKSREESKKQALAAKREKRKEKRKKKKEEQKRKLEEEEAKVKEVSFEMLDQKEDSAEEAEVPIEPPSATTTTTIGISATSATFTNSFGKKRANVATTPSTNRKNKKNKTKDTPSEPIILQDPQVALAQQKADKNKIHGEPRGGGATGGTSDSDNLDSTDCNSESSNGSKCQELTDLPSSSSSCSSAPTVFVGSNQPHFANEKRHGLSLPGSREEKVMVSISKPQIKSHEISDLTPSSLPTSFKTISLPVTSPNSKMNPLSPKRTQKREEGWKEVVRRSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIPRNHIRPPGANTKISSTYTTSTGATSTTAASSKGLPSVVPSANVSFQSTTNFTAQQASKLGKSMASGVRPPFVSLPPLAYAHPQLALLAAQTMNQIRHPRLPMAQFGGTFSPSPNTWGPFPVRPVSPGSANSSPKHSGNSAPRLVSTTPAHIDHPTAPVSSTSTPTASTSSPTSTAPANTPTPSSVRKQLFSSEPKSLAGIAVVTTSSNAPSAQIAPSPISCAPTTPTTPPPSSAATAATPQHPPKPEPASLSTPAKEKPVTEIAAPTAGAPSDGPSASAPLHFTSSPSGPSMLPPQPESRQTLPSHFPPSTESSSSSSSQPGSSHPVTRLPPPTSSNTITNTSSTLPHYGSPTAPGVSPRMQPPTPYYPMAPGALQEQQSVFVPPGATQETLKQQPPPQPTLAPAGMPPPSLPMSSTMGMINGSQMHLHSGKAQLPPNFGPAALFNHFSSIFDNNQVGNNQVWGACHLPARTPPEQPYSGTTNAYIGGMGQMESVMPPPDGSKAPGYRCSTQRMVSSPIGIHPMDGSMSSSTALTSFTTSISASPVFLPGPAPVGTPSFSRQHFSPHPWSASTSCESPVPSVSSGASSPLCTSTVTPALIQAKPSSSNQQDRKVPPPIGTERLARIRQTGSVNHTMLPTSYTPPVGQGGIWSFGVGSASETMSGWSQPLMGGGPVMHQQMQEPSAFSQHQAMERDDTGIVAPSNTFHQPLPTNFMDFPKGLPMSMYGGTMIPPHPQMAEGPGGPVYNGLHTSDPAWNPILKVVPNSAENADPQQVWPGTWAPHVGNVHLNHVN
Protein: ATP synthase subunit delta (ATP synthase F(1) sector subunit delta) (F-type ATPase subunit delta) (F-ATPase subunit delta) (P0ABA4)
Organism: Escherichia coli (strain K12)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:16079137}.
Interaction partners:
- ATP synthase subunit beta
- ATP synthase subunit a
- ATP synthase subunit c
- ATP synthase epsilon chain
- ATP synthase subunit alpha
- ATP synthase gamma chain
- ATP synthase subunit b
- Large ribosomal subunit protein uL4
- NADH-quinone oxidoreductase subunit C/D
- Small ribosomal subunit protein uS4
Sequence:
MSEFITVARPYAKAAFDFAVEHQSVERWQDMLAFAAEVTKNEQMAELLSGALAPETLAESFIAVCGEQLDENGQNLIRVMAENGRLNALPDVLEQFIHLRAVSEATAEVDVISAAALSEQQLAKISAAMEKRLSRKVKLNCKIDKSVMAGVIIRAGDMVIDGSVRGRLERLADVLQS
Protein: Nck-associated protein 1-like (Hematopoietic protein 1) (Membrane-associated protein HEM-1) (P55160)
Organism: Homo sapiens (Human)
Function: Essential hematopoietic-specific regulator of the actin cytoskeleton (Probable). Controls lymphocyte development, activation, proliferation and homeostasis, erythrocyte membrane stability, as well as phagocytosis and migration by neutrophils and macrophages. Component of the WAVE2 complex which signals downstream of RAC to stimulate F-actin polymerization. Required for stabilization and/or translation of the WAVE2 complex proteins in hematopoietic cells (By similarity). Within the WAVE2 complex, enables the cortical actin network to restrain excessive degranulation and granule release by T-cells. Required for efficient T-lymphocyte and neutrophil migration. Exhibits complex cycles of activation and inhibition to generate waves of propagating the assembly with actin. Also involved in mechanisms WAVE-independent to regulate myosin and actin polymerization during neutrophil chemotaxis. In T-cells, required for proper mechanistic target of rapamycin complex 2 (mTORC2)-dependent AKT phosphorylation, cell proliferation and cytokine secretion, including that of IL2 and TNF.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16417406}; Single-pass membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16417406}. Note=Localizes to the leading edge of polarized neutrophils. {ECO:0000269|PubMed:16417406, ECO:0000269|PubMed:17696648}.
Interaction partners:
- Protein BRICK1
- Actin-binding protein WASF2
- Abl interactor 1
- Abl interactor 2
- Cytoplasmic FMR1-interacting protein 1
- Cytoplasmic FMR1-interacting protein 2
- Actin-binding protein WASF1
- Actin-binding protein WASF3
- ABI gene family member 3
- Ras-related C3 botulinum toxin substrate 2
Sequence:
MSLTSAYQHKLAEKLTILNDRGQGVLIRMYNIKKTCSDPKSKPPFLLEKSMEPSLKYINKKFPNIDVRNSTQHLGPVHREKAEIIRFLTNYYQSFVDVMEFRDHVYELLNTIDACQCHFDINLNFDFTRSYLDLIVTYTSVILLLSRIEDRRILIGMYNCAHEMLHGHGDPSFARLGQMVLEYDHPLKKLTEEFGPHTKAVSGALLSLHFLFVRRNQGAEQWRSAQLLSLISNPPAMINPANSDTMACEYLSVEVMERWIIIGFLLCHGCLNSNSQCQKLWKLCLQGSLYITLIREDVLQVHKVTEDLFSSLKGYGKRVADIKESKEHVIANSGQFHCQRRQFLRMAVKELETVLADEPGLLGPKALFAFMALSFIRDEVTWLVRHTENVTKTKTPEDYADSSIAELLFLLEGIRSLVRRHIKVIQQYHLQYLARFDALVLSDIIQNLSVCPEEESIIMSSFVSILSSLNLKQVDNGEKFEFSGLRLDWFRLQAYTSVAKAPLHLHENPDLAKVMNLIVFHSRMLDSVEKLLVETSDLSTFCFHLRIFEKMFAMTLEESAMLRYAIAFPLICAHFVHCTHEMCPEEYPHLKNHGLHHCNSFLEELAKQTSNCVLEICAEQRNLSEQLLPKHCATTISKAKNKKTRKQRQTPRKGEPERDKPGAESHRKNRSIVTNMDKLHLNLTELALTMNHVYSFSVFEHTIFPSEYLSSHLEARLNRAIVWLAGYNATTQEIVRPSELLAGVKAYIGFIQSLAQFLGADASRVIRNALLQQTQPLDSCGEQTITTLYTNWYLESLLRQASSGTIILSPAMQAFVSLPREGEQNFSAEEFSDISEMRALAELLGPYGMKFLSENLMWHVTSQIVELKKLVVENMDILVQIRSNFSKPDLMASLLPQLTGAENVLKRMTIIGVILSFRAMAQEGLREVFSSHCPFLMGPIECLKEFVTPDTDIKVTLSIFELASAAGVGCDIDPALVAAIANLKADTSSPEEEYKVACLLLIFLAVSLPLLATDPSSFYSIEKDGYNNNIHCLTKAIIQVSAALFTLYNKNIETHLKEFLVVASVSLLQLGQETDKLKTRNRESISLLMRLVVEESSFLTLDMLESCFPYVLLRNAYREVSRAFHLN
Protein: Charged multivesicular body protein 2B (C9J0A7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACKVLAKQLVHLRKQKTRTFATMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD
Protein: Copper chaperone GriE (Grixazone biosynthesis protein E) (B1VTI4)
Organism: Streptomyces griseus subsp. griseus (strain JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235)
Function: Involved in the transfer of copper ion to the apo form O-aminophenol oxidase GriF in the grixazone biosynthetic pathway.
Interaction partners:
Sequence:
MPMNRREMVMATTGAALAAAAAVPLLSGGEGEGAAEAAAAPAKATGRGREHTERYLGRSIRVAAPADGGGVFIDGRPLHIMKFADDAYLSSMCHYEMAPTPLHAARRAVEELRGAALQPSTHGTHVTHL
Protein: Nuclear distribution protein nudE homolog 1 (NudE) (Q9NXR1)
Organism: Homo sapiens (Human)
Function: Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post-mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Cleavage furrow. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:34793709}. Note=Localizes to the interphase and S phase centrosome. During mitosis, partially associated with the mitotic spindle. Concentrates at the plus ends of microtubules coincident with kinetochores in metaphase and anaphase in a CENPF-dependent manner. Also localizes to the cleavage furrow during cytokinesis. manner. Also localizes to the cleavage furrow during cytokinesis. Colocalizes with RAB9A to membrane vesicles (PubMed:34793709). {ECO:0000269|PubMed:34793709}.
Interaction partners:
- Disrupted in schizophrenia 1 protein
- Platelet-activating factor acetylhydrolase IB subunit beta
- Centriole and centriolar satellite protein OFD1
- Nuclear distribution protein nudE-like 1
- Dynein light chain 1, cytoplasmic
- Nuclear migration protein nudC
- Trafficking kinesin-binding protein 1
- Ras-related protein Rab-9A
- Cyclin-dependent kinase 1
- 14-3-3 protein epsilon
Sequence:
MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISALNIVGDLLRKVGALESKLASCRNLVYDQSPNRTGGPASGRSSKNRDGGERRPSSTSVPLGDKGLDTSCRWLSKSTTRSSSSC
Protein: Probable pyruvate dehydrogenase protein X component, mitochondrial (Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex) (O94709)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000305}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- [Pyruvate dehydrogenase
- Putative glycine cleavage system H protein, mitochondrial
- Glutathione reductase
- Putative lipoate-protein ligase A
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MLKHYIHQCVKASSCKHSLSVKQRYFHCSALNGVASMFRMPALSPTMEEGNITKWHFKEGDSFKSGDILLEVETDKATMDVEVQDNGILAKVLIEKGSNIPVGKNIAIVADAEDNLKDLELPKDEASSEEQSFSSSKEEVKPIVQDRETKSNVEHKSTSQANDAVNKSFLPSVSYLIHQYKIENPWSIPATGPHGRLLKGDVLAHVGKIDKGVPSSLQKFVRNLEVLDFSGVEPKKPSYTEDSVPVRKSTMIETLKTVPMKDEYITFERSISLEKLKSLLAKRKEKDAFGIDEVVSAMIGDALSISELSKVEPNSIESAYDLLLGAPIVKLKSSVSNFQPKLFPKNNNTKDLHKYIRDSMIGLPSNLSDYVKLNFSSVTKSSSNNVEFLDDVYDMLLGSNSDSIDSRINRHEEPSTTEDLTLTLSIKDNISKSRAIKFVDCLKSNFENPEFVLSRW
Protein: Transcription factor ILR3 (Basic helix-loop-helix protein 105) (AtbHLH105) (bHLH 105) (Protein IAA-LEUCINE RESISTANT 3) (Transcription factor EN 133) (bHLH transcription factor bHLH105) (Q9FH37)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Plays a role in resistance to amide-linked indole-3-acetic acid (IAA) conjugates such as IAA-Leu and IAA-Phe. May regulate gene expression in response to metal homeostasis changes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:25452667}.
Interaction partners:
- Transcription factor bHLH101
- Transcription factor bHLH100
- Transcription factor ORG2
- Transcription factor ORG3
- Ferric reduction oxidase 2
- Fe
- Probable nicotianamine synthase 4
- Ferric reduction oxidase 3, mitochondrial
- Transcription factor FER-LIKE IRON DEFICIENCY-INDUCED TRANSCRIPTION FACTOR
- Protein ZINC INDUCED FACILITATOR 1
Sequence:
MVSPENANWICDLIDADYGSFTIQGPGFSWPVQQPIGVSSNSSAGVDGSAGNSEASKEPGSKKRGRCESSSATSSKACREKQRRDRLNDKFMELGAILEPGNPPKTDKAAILVDAVRMVTQLRGEAQKLKDSNSSLQDKIKELKTEKNELRDEKQRLKTEKEKLEQQLKAMNAPQPSFFPAPPMMPTAFASAQGQAPGNKMVPIISYPGVAMWQFMPPASVDTSQDHVLRPPVA
Protein: Zgc:110761 (Q5BJ14)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPEPTEAEVKPEEEAPGDDVEPTELTGLFVEKPESVVAIAGKDVTFVVKVDSTNLTRKPTMKWLKGKWMDLGSKAGKHIQLKETYDRNTKIYTYEMKLVKVVPGDAGGYRCEVSAKDKCDSCTFEVTVEAAEQEQQADILSAFKRADAGEDEGDLDFSALLKAAKKKKKPEPELEVDVWELLKSAHPSEYEKIAFKYGITDLRGMLKRLKKMKVVEPKFSEAFLRRLESAYSVNKGKKIVMSVEVADPNAEVKWLRNGQEIKPSAKYIMEADGNIRTLTINKCSLADDAAYECVAGTDKCFTEVFVKEPPITITKLLDDYHVVVGERVEFEIEVSEEGAHVIWLFEDQQLSREDKDSKYRFKKDGKRHCLIIQEATLEDNGMFYVYTNGGQSKGELIVEEKELEVLQSIADLTVKSAEQAMFKCEVSDEKVTGKWFKDGVEVLPSDRIKISHIGRIHRLTIDDVKPGDAGDYTFVPDGYALSISPKLNFLEIKIDYVPRQDPPKIHLDVSGNMVSQNTIIVVAGNKLRLDVEITGEPAPTVCWMRDDKPVTDSEGRVRVENKKDLSCFIIEGAEREDEGNYTITVTNPAGEDKANLFIKIVDVPDPPENVKCTGVGEDTANIVWDPPKFDGGAPLKGYLMERKKKGSSRWTKLNFDVYASTTYEAKRMIEGILYEMRVFAVNGIGISAPSLNSKPFMPIAPTSEPTKLTVDDVTDTTCSLKWLAPEKIGAGGLDGYIIEFCKEGESEWHPANTDLVERQSFVVRNLPTGEKMNFRVVAVNIAGRSPPALLGQPVTVREIMEHPKIRLPRDLRTKYIRRVGEKINLVIPFQGKPRPIATWLKDGQPVDEKKVGVRNSNVDSILFIRAAERDHSGKYTLILKIENMEDSATIEIRIVDKPGPPIGVHVTDVWGFNAALEWKPPKDDGNCEITGYTIQKAEKKTKEWFTVYEHNRRTNCTVSDLIIGNEYMFRVYSENLCGLSEDPCMSKNNAIISKSGLDYKPPPYKEKDMNCAPKFTAPLVDRAVTIGYSTAISCAVRAFPKPKIIWMKNKMIIGDDPKFLMQNNQGVLTLNIRKPSTFDSGKYSCRAVNELGEDEVECKLEIKAIPTEKKD
Protein: Miro domain-containing protein (Q389V9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGAADSPDLLRVLVVGHTGVGKTLFLQRLHRSTVERREGPLRARGHTVGFNVEVISTHRENKFGSSTHVSDNERHIAFVEVGGNRNFGRSGHFPLSLMTFHGVIFVYDHHNIESATDLMYWYEYLKGYGAVGSGGTARVMLVETTHIPLTDDPSSAARVLPDELLGSYLQESIKKAPTFREKMCHTVRSLFRRCASVSRLSVTDFQPQYLRFLPRVAVFLHQLMSIVENLLLFIMAVTLFGPGQKSVSFCPPSVSAALRTIEDDASGTRTLKQCPLYDQGLFEATALEEVLSFLGSLRSA
Protein: Glypican-1 (Q6QA54)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}. Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
MRFFPWGFWLLCVASAPARGDSGSKARSCAEVRQLYGAKGFSLNGVPQAEISGEHLRICPQGYTCCTSEMEENFANKSRSEFEAMMKEAGRSVQTILTAQYRSFDNYFQDLLNKSEKALYDTFPSLYGELYTQNTKVFKDLYSELRRYYRGSNINLEEALNEFWTRLLERLFKLMNAQYHITDEYLDCMVKHAEQHKPFGEVPRDLKVKATRAFIVARSYAQGFLVGSDVVKKVSQVSLSHECTRAVMKLMYCPHCRGMASVKPCSNYCLNVVKGCLANQADLNTEWKYLMDALVAVADRIDGPSNVDTVIGTIHMRISEAISNLQENKDSITAKVFQGCGNPKISTKGSSSEDKKRRGKVTLEAKSSAVALEMLVLDAKGNLTALKSYWVTLPGVLCSKKVMASAAADDKCWNGMTKGSYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLGNANMGNDVDFQDASDDMSGSGSGDSCPDDVCGKRLSKSPSTRQPETHAIPKQSGHGVIGASSRSLPSAFLLFLLGASIAVQHLWR
Protein: STAG1 cohesin complex component (F8WCB3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MITSELPVLQDSTNETTAHSDAGSELEETEVKGKRKRGRPGRPPSTNKKPRKSPGEKSRIEAGIRGAGRGRANGHPQQNGEGEPVTLFEVVKLGKSAMQSLHVVCIHLVGRGERKRSSVYFLEAFGPSIYIPLMGTYHILSPWWMTGLNHINKTGTSHFWI
Protein: Protein unc-13 homolog D (Munc13-4) (B2RUP2)
Organism: Mus musculus (Mouse)
Function: Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis (By similarity). Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Late endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Lysosome {ECO:0000269|PubMed:18354201}. Note=Colocalizes with cytotoxic granules at the plasma membrane. Localizes to endosomal exocytic vesicles. {ECO:0000250}.
Interaction partners:
- Ras-related protein Rab-27A
- Syntaxin-11
- Syntaxin-binding protein 2
- Syntaxin-19
- Ras-related protein Rab-27B
- Lysosomal-trafficking regulator
- Perforin-1
Sequence:
MATHLSHPQRRPLLRQAIKIRRRRVRDLQDPPPQATQEVQVQSHHFSPEERDLLYEEALYTVLHRLGQPEPNHVKEASELLSYLQEAFQVQPEEHQQMLRRVRELEKPVFCLKATVKQAKGILGKDVSGFSDPYCLLGIEQKVGVAEGSPVSRRRQKAVVKHTIPEEETHRTQVKSQTLNPVWDETFILEFEDIANASFHLDMWDLDTVESVRQKLGELTDLHGLRRIFKEARKDKGQDDFLGNVVLRLQDLRCREDQWFPLEPCTETYPDRGQCHLQFQFIHKRRATAASRSQPSYTVHFHLLQQLVSHEVTQHQAGSTSWDASLSPQAVTILFLHATQKDLSDFHQSMAQWLAYSRLYQSLEFPSSCLLHPITSIEYQWIQGRLKAEQREELATSFTSLLAYGLSLIRKFRSVFPLSVSDSPSRLQSLLRVLVQMCKMKAFGELCPDSAPLSQLVSEALRMGTVEWFHLMQQHHQPMVQGILEAGKALLNLVQDVMGDLYQCRRTWNKIFHNVLKIDLFSMAFLELQWLVAKRVQDHTVAAGNLVSPDIGESLFQLYVSLKELCQLGPVPSDSREVLALDGFHRWFQPAIPSWLQKTYSVALERVQRAVQMDTLVPLGELTKHSTSAVDLSTCFAQISHTARQLDWPDPEEAFMITVKFVEDTCRLALVYCSLIKARARELSAVQKDQSQAADMLCVVVNNMEQLRLIIDKLPTQLAWEALEQRVGAVLEEGQLQNTLHAQLQGALAGLGHEIRTGVRTLAEQLEVGIATHIQKLIGVKESVLPEDAILPLMKFLEVKLCYMNTNLVQENFSSLLTLLWTHTLTVLVEVASSQRSSSLASGRLKVALQNLEVCFHAEGCGLPPEALHTDTFQALQNDLELQAASSRELIQKYFCSRIQQQAETTSERLGAVTVKVSYRASEQRLRVELLSASSLLPLDSNGSSDPFVQLTLEPRHEFPEVAPRETQKHKKELHPLFDETFEFLVPAEPCQKAWACLLLTVLDHDRLGADDLEGEAFLPLCRVPGLTDCAEPGEAPQMRLPLTYPAPNGDPILRLLESRKGDREAQAFVKLRRQRAKQASQHAP