wanglab/gogpt-training-data huggingface dataset:
Protein: Ras-responsive element-binding protein 1 (RREB-1) (Finger protein in nuclear bodies) (Raf-responsive zinc finger protein LZ321) (Zinc finger motif enhancer-binding protein 1) (Zep-1) (Q92766)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds specifically to the RAS-responsive elements (RRE) of gene promoters. Represses the angiotensinogen gene. Negatively regulates the transcriptional activity of AR. Potentiates the transcriptional activity of NEUROD1. Promotes brown adipocyte differentiation (By similarity). May be involved in Ras/Raf-mediated cell differentiation by enhancing calcitonin expression.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:15067362, ECO:0000269|PubMed:17550981, ECO:0000269|PubMed:9305772}.
Interaction partners:
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- C-terminal-binding protein 1
- Histone deacetylase 1
- REST corepressor 1
Sequence:
MTSSSPAGLEGSDLSSINTMMSAVMSVGKVTENGGSPQGIKSPSKPPGPNRIGRRNQETKEEKSSYNCPLCEKICTTQHQLTMHIRQHNTDTGGADHSCSICGKSLSSASSLDRHMLVHSGERPYKCTVCGQSFTTNGNMHRHMKIHEKDPNSATATAPPSPLKRRRLSSKRKLSHDAESEREDPAPAKKMVEDGQSGDLEKKADEVFHCPVCFKEFVCKYGLETHMETHSDNPLRCDICCVTFRTHRGLLRHNALVHKQLPRDAMGRPFIQNNPSIPAGFHDLGFTDFSCRKFPRISQAWCETNLRRCISEQHRFVCDTCDKAFPMLCSLALHKQTHVAADQGQEKPQATPLPGDALDQKGFLALLGLQHTKDVRPAPAEEPLPDDNQAIQLQTLKCQLPQDPGCTNLLSLSPFEAASLGGSLTVLPATKDSIKHLSLQPFQKGFIIQPDSSIVVKPISGESAIELADIQQILKMAASAPPQISLPPFSKAPAAPLQAIFKHMPPLKPKPLVTPRTVVATSTPPPLINAQQASPGCISPSLPPPPLKLLKGSVEAASNAHLLQSKSGTQPHAATRLSLQQPRAELPGQPEMKTQLEQDSIIEALLPLSMEAKIKQEITEGELKAFMTAPGGKKTPAMRKVLYPCRFCNQVFAFSGVLRAHVRSHLGISPYQCNICDYIAADKAALIRHLRTHSGERPYICKICHYPFTVKANCERHLRKKHLKATRKDIEKNIEYVSSSAAELVDAFCAPDTVCRLCGEDLKHYRALRIHMRTHCGRGLGGGHKGRKPFECKECSAAFAAKRNCIHHILKQHLHVPEQDIESYVLAADGLGPAEAPAAEASGRGEDSGCAALGDCKPLTAFLEPQNGFLHRGPTQPPPPHVSIKLEPASSFAVDFNEPLDFSQKGLALVQVKQENISFLSPSSLVPYDCSMEPIDLSIPKNFRKGDKDLATPSEAKKPEEEAGSSEQPSPCPAPGPSLPVTLGPSGILESPMAPAPAATPEPPAQPLQGPVQLAVPIYSSALVSSPPLVGSSALLSGTALLRPLRPKPPLLLPKPPVTEELPPLASIAQIISSVSSAPTLLKTKVADPGPASTGSNTTASDSLGGSVPKAATTATPAATTSPKESSEPPAPASSPEAASPTEQGPAGTSKKRGRKRGMRSRPRANSGGVDLDSSGEFASIEKMLATTDTNKFSPFLQTAEDNTQDEVAGAPADHHGPSDEEQGSPPEDKLLRAKRNSYTNCLQKITCPHCPRVFPWASSLQRHMLTHTDSQSDAETAAAAGEVLDLTSRDREQPSEGATELRQVAGDAPVEQATAETASPVHREEHGRGESHEPEEEHGTEESTGDADGAEEDASSNQSLDLDFATKLMDFKLAEGDGEAGAGGAASQEQKLACDTCGKSFKFLGTLSRHRKAHGRQEPKDEKGDGASTAEEGPQPAPEQEEKPPETPAEVVESAPGAGEAPAEKLAEETEGPSDGESAAEKRSSEKSDDDKKPKTDSPKSVASKADKRKKVCSVCNKRFWSLQDLTRHMRSHTGERPYKCQTCERTFTLKHSLVRHQRIHQKARHAKHHGKDSDKEERGEEDSENESTHSGNNAVSENEAELAPNASNHMAVTRSRKEGLASATKDCSHREEKVTAGWPSEPGQGDLNPESPAALGQDLLEPRSKRPAHPILATADGASQLVGME
Protein: Ras-related protein Rab-9A (EC 3.6.5.2) (Sid 99) (Q9R0M6)
Organism: Mus musculus (Mouse)
Function: Involved in the transport of proteins between the endosomes and the trans-Golgi network (By similarity). Involved in the recruitment of SGSM2 to melanosomes and is required for the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P51151}; Lipid-anchor {ECO:0000250|UniProtKB:P51151}; Cytoplasmic side {ECO:0000250|UniProtKB:P51151}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P51151}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P51151}. Late endosome {ECO:0000250|UniProtKB:P51151}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P51151}; Lipid-anchor {ECO:0000250|UniProtKB:P51151}; Cytoplasmic side {ECO:0000250|UniProtKB:P51151}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P51151}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51151}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Colocalizes with OSBPL1A at the late endosome. Recruited to phagosomes containing S.aureus or M.tuberculosis. Mainly localizes to late endosomes and partially localizes to Golgi. Colocalizes with NDE1 to membrane vesicles. {ECO:0000250|UniProtKB:P51151}.
Interaction partners:
- Small G protein signaling modulator 1
- GRIP and coiled-coil domain-containing protein 2
- Ras-related protein Rab-9B
- Pleckstrin homology domain-containing family M member 2
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- DENN domain-containing protein 2B
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- Rab GDP dissociation inhibitor beta
Sequence:
MAGKSSLFKIILLGDGGVGKSSLMNRYVTNKFDSQLFHTIGVEFLNKDLEVDGHFVTMQIWDTAGQERFRSLRTPFYRGSDCCLLTFSVDDSQSFQNLSNWKKEFIYYADVKEPESFPFVILGNKTDIKERQVSTEEAQAWCKDNGDYPYFETSAKDSTNVAAAFEEAVRRILATEDRSEHLIQTDTVNLHRKPKPNSSCC
Protein: Antimicrobial peptide 7 (XT-7) (P84381)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Has very strong antibacterial activity against many Gram-negative bacteria and the Gram-positive bacteria S.pneumoniae and Enterococcus sp. There is moderate antimicrobial activity against the Gram-negative bacterium P.aeruginosa and yeast C.albicans and weaker activity against the Streptococcal strains and E.coli. Has hemolytic activity against human red blood cells. Seems to disrupt the membranes by adopting an alpha-helical conformation.
Subcellular location: Secreted {ECO:0000269|PubMed:11738090}.
Interaction partners:
Sequence:
GLLGPLLKIAAKVGSNLL
Protein: Hexokinase-2 (EC 2.7.1.1) (Hexokinase type II) (Q8AYP7)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004450}.
Interaction partners:
Sequence:
MIASHLLAYFFTELNHDQAQKVDKYLYHMRLSEDTLQEVSERFRKEMEKGLGADTNPTASVKMLPSFVRSTPDGTEDGDFLALDLGGTNFRVLRVKVSDNGLQKVEMESQIYEIHEDLMRGSGMQLFDHIAECLGNFMEKLKIKDKKLPLGFTFSFPCHQTKLDESILVNWTKGFKCSSVEGKDVVSLLRRAIKKRGDFDIDIVAVVNDTVGTMMSCGYDDQNCEVGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGALNDIRTEFDHEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEGLLFQGKLSSDLRTTGHFETRFVSAIEKEKEGLQKAHEILTKLGLEPSHEDCLATHRICQIVSTRSANLCGATLAARLRRIKEYKGVDPLRSTVGVDGSVYKKYPHFARRLHKTVRKLLPDCEIRFVRSEDGSGKGAAMVTAVAYRLAAQHKARQKILEALKLSHEQLLEVKRRMRVEMEKGLGKETHAEATVKMLPTYVCSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGMRRGVEMHNKIYSIPLEVMQGTGEELFDHIVHCISDFLEYMGMKGVSLPLGFTFSFPCKQTNLDEGILLKWTKGFKATGCEGEDVVSLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPYCEVGLIVGTGSNACYMEEMRNVELVEGDEGRMCVNMEWGAFGDNGCLDDIQTEFDLAVDELSLNPGKQRFEKMISGMYLGEIVRNILMDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALLQVRSILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDFLKVTVGVDGTLYKLHPHFSAIMQDTVRQLSPCCEVTFLQSEDGSGKGAALITAVACRIREAGQ
Protein: Dof zinc finger protein DOF1.6 (AtDOF1.6) (Q9SX97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Uncharacterized protein At1g24000
Sequence:
MPSEPNQTRPTRVQPSTAAYPPPNLAEPLPCPRCNSTTTKFCYYNNYNLAQPRYYCKSCRRYWTQGGTLRDVPVGGGTRRSSSKRHRSFSTTATSSSSSSSVITTTTQEPATTEASQTKVTNLISGHGSFASLLGLGSGNGGLDYGFGYGYGLEEMSIGYLGDSSVGEIPVVDGCGGDTWQIGEIEGKSGGDSLIWPGLEISMQTNDVK
Protein: GH23250p (Raw) (Q9U3Z6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHKMVKLFLREVLNAWRAKARCNVVPDERTQELFHELSFHPSQKQISEMLQTAKKVARKGGSGQANGLTFGQFCVLAADLKRFRASTISNQPSYCDYQSLSAGLLLPELDDPASSSNQNLQSPAATNSSPAHSSKKPDNHGIELRSTKSFSSVDDTKKKKNATNEPVEVFLGGSCNPTTWRADVAIPALKELGISFYNPQVSDWTPDLIELEHRAKEKARVLFFVMDSETRASAGAIEAAHIAGQNCKQLVLVLHPYKPNQKILNEPISQQEYLDLNRNQLILKELVSRRGLPVLDNIPLGLQRTKDILGGIRDPPSKISSILDTVRGAFDRVNPLNDLLTVEQCKRALLFLGYAQSLVNLDNLNKIIINQRESLKLLQTHSPRAVADDADADGGNCSQPILPSQELIDFDLFCVISAYLSVLQQEIHESGCISPIKGTNVPPPQVYFTNAPDVDIYYSASKNISRTSSNASVPSNSSSGIGHDLERQSLFEQLSRSRDSGTSSPQPTGSSSLGKSPRPQILLNVESIETTEIITTKTIETKPNPVTASTVVHAEEEESDSNDSVLSSNSSIASAGDILCCGGGLDLRDVYLGGSCVLRTKWRQELAVPYLQSKGVSFHTPALHESIQQMILNQEQNQDQSQQPTVPPQEQQQQQRSFVRTRRKCRGNQLQLEEQEELTVAEESLSWSLPPVAVRQSLFNPSLLDSSRVLLFVITNETRSLAPMTLAAHCIGLMYNVVLAVQMLPEDCVLGDEKLTVAAIKDYNRGRSYLIDLAKRQGVPVFSDIRAALECTVAKVKAYNNRDRC
Protein: ribonuclease Z (EC 3.1.26.11) (E7ES68)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XTMTVYQIPIHSEQRRGKHQPWQSPERPLSRLSPERSSDSESNENEPHLPHGVSQRRGVRDSSLVVAFICKLHLKRGNFLVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVECPDESFIQPICENATFQRYQQWMERFGPDTQHLVLNENCASVHNLRSHKIQTQLNLIHPDIFPLLTSFRCKKEGPTLSVPMVQGECLLKYQLRPRREWQRDAIITCNPEEFIVEALQLPNFQQSVQEYRRSAQDGPAPAEKRSQYPEIIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQVDRVLGTLAAVFVSHLHADHHTGLPSILLQRERALASLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSPAVERLISSLLRTCDLEEFQTCLVRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYAKVPLFSPNFSEKVGVAFDHMKVCFGDFPTMPKLIPPLKALFAGDIEEMEERREKRELRQVRAALLSRELAGGLEDGEPQQKRAHTEEPQAKKVRAQ
Protein: B9 domain containing 2 (M0QY88)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
Interaction partners:
Sequence:
MAEVHVIGQIIGASGFSESSLFCKWGIHTETGSRYVAQAGLELLRSNRPPTSASQSARIKNGRHGSSCQACGRAKRKWTPRR
Protein: Protein LMBR1L (Lipocalin-1-interacting membrane receptor) (LIMR) (Uteroglobin receptor) (Q9D1E5)
Organism: Mus musculus (Mouse)
Function: Plays an essential role in lymphocyte development by negatively regulating the canonical Wnt signaling pathway. In association with UBAC2 and E3 ubiquitin-protein ligase AMFR, promotes the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6. LMBR1L stabilizes the beta-catenin destruction complex that is required for regulating CTNNB1 levels. Acts as a LCN1 receptor and can mediate its endocytosis (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:31073040}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:31073040}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEAADYEVLSVREQLFHDRVRECIISILLFATLYILCHIFLTRFKKPAEFTTVDDEDATVNKIALELCTFTLAVALGAVLLLPFSIISNEVLLSLPRNYYIQWLNGSLIHGLWNLVFLFSNLSLVFLMPFAYFFTESEGFAGSRKGVLGRVYETVVMLILLTLLVLGMVWVASAIVDNDKASRESLYDFWEYYLPYLYSCISFLGVLLLLVCTPLGLARMFSVTGKLLVKPRLLEDLEEQLNCSAFEEAALTRRICNPTSCWLPLDMELLHRQVLALQAQRVLLEKRRKASAWQRNLGYPLAMLCLLVLTGLSVLIVAVHILELLIDEAAMPRGMQDAALGQASFSKLGSFGAIIQVVLIFYLMVSSVVGFYSSPLFGSLRPRWHDTSMTQIIGNCVCLLVLSSALPVFSRTLGLTRFDLLGDFGRFNWLGNFYIVFLYNAAFAGLTTLCLVKTFTAAVRAELIRAFGLDRLPLPVSGFPRASRKKQHQ
Protein: Polymeric immunoglobulin receptor (PIgR) (Poly-Ig receptor) [Cleaved into: Secretory component] (P15083)
Organism: Rattus norvegicus (Rat)
Function: Mediates selective transcytosis of polymeric IgA and IgM across mucosal epithelial cells. Binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment.
Subcellular location: [Polymeric immunoglobulin receptor]: Cell membrane {ECO:0000250|UniProtKB:P01833}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Secretory component]: Secreted {ECO:0000250|UniProtKB:P01833}.
Interaction partners:
- Joining chain of multimeric IgA and IgM
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Ig-like domain-containing protein.
- Ras-related protein Rab-3B
- Interleukin-2
- CD79a molecule
- B-cell antigen receptor complex-associated protein beta chain
- Lck interacting transmembrane adaptor 1
- Tyrosine-protein kinase SYK
- IgG receptor FcRn large subunit p51
Sequence:
MRLSLFALLVTVFSGVSTQSPIFGPQDVSSIEGNSVSITCYYPDTSVNRHTRKYWCRQGANGYCATLISSNGYLSKEYSGRASLINFPENSTFVINIAHLTQEDTGSYKCGLGTTNRGLFFDVSLEVSQVPEFPNDTHVYTKDIGRTVTIECRFKEGNAHSKKSLCKKRGEACEVVIDSTEYVDPSYKDRAILFMKGTSRDIFYVNISHLIPSDAGLYVCQAGEGPSADKNNADLQVLEPEPELLYKDLRSSVTFECDLGREVANDAKYLCRKNKETCDVIINTLGKRDPAFEGRILLTPRDDNGRFSVLITGLRKEDAGHYQCGAHSSGLPQEGWPVQAWQLFVNEESTIPNSRSVVKGVTGGSVAIVCPYNPKESSSLKYWCHWEADENGRCPVLVGTQALVQEGYEGRLALFDQPGSGAYTVILNQLTTQDSGFYWCLTDGDSRWRTTIELQVAEATKKPDLEVTPQNATAVIGETFTISCHYPCKFYSQEKYWCKWSNDGCHILPSHDEGARQSSVSCDQSSQIVSMTLNPVKKEDEGWYWCGVKEGQVYGETTAIYVAVEERTRGSPHINPTDANARAKDAPEEEAMESSVREDENKANLDPRLFADEREIQNAGDQAQENRASGNAGSAGGQSGSSKVLFSTLVPLGLVLAVGAVAVWVARVRHRKNVDRMSISSYRTDISMGDFRNSRDLGGNDNMGATPDTQETVLEGKDEIETTTECTTEPEESKKAKRSSKEEADMAYSAFLFQSSTIAAQVHDGPQEA
Protein: Uncharacterized protein (Q54WE3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MKLLLSLLCLVYFLVASVSSQNNTINFTPFFDAQCQKEGGGIGFGYDPSNCYNFHPGQCPHPNFIPLISPDDLNNICLKVKDVSSTEWTLEFRSNGDCEQGDLIAEETFTSDCAYSSFFGAYYSVSKYNVNELPSQTMLFYIYNKQGFEVCTLMDTLNFNFLFNNTVLTGQANGKTFQEKYFCNGAAYTTVCQGDHYCKTNELVGCDDLDFQASCTD
Protein: Dihydrolipoyl dehydrogenase 2, chloroplastic (ptLPD2) (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase 2) (Protein LIPOAMIDE DEHYDROGENASE 2) (Pyruvate dehydrogenase complex E3 subunit 2) (E3-2) (PDC-E3 2) (F4JLP5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lipoamide dehydrogenase is a component of the plastidial pyruvate dehydrogenase complex (PDC).
Subcellular location: Plastid, chloroplast stroma {ECO:0000250}.
Interaction partners:
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 5 of pyruvate dehydrogenase complex, chloroplastic
- Dihydrolipoyllysine-residue acetyltransferase component 4 of pyruvate dehydrogenase complex, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial
Sequence:
MQSVLSLSFSQASLPLANRTLCSSNAAPSTPRNLRFCGLRREAFCFSPSKQLTSCRFHIQSRRIEVSAAASSSAGNGAPSKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMKAFGLQVSAAGYDRQGVADHASNLATKIRNNLTNSMKALGVDILTGFGAVLGPQKVKYGDNIITGKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPDWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINTRKIDYHTGVFASKITPAKDGKPVLIELIDAKTKEPKDTLEVDAALIATGRAPFTNGLGLENINVTTQRGFIPVDERMRVIDGNGKLVPHLYCIGDANGKLMLAHAASAQGISVVEQVTGRDHVLNHLSIPAACFTHPEISMVGLTEPQAREKAEKEGFKVSIAKTSFKANTKALAENEGEGLAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVVDELFKAAKVDSPASVTAQSVKVTV
Protein: Proline/serine-rich coiled-coil protein 1 (Q9D0P7)
Organism: Mus musculus (Mouse)
Function: Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate, and for normal rate of chromosomal segregation during anaphase. Plays a role in the regulation of mitotic spindle dynamics. Increases the rate of turnover of microtubules on metaphase spindles, and contributes to the generation of normal tension across sister kinetochores. Recruits KIF2A and ANKRD53 to the mitotic spindle and spindle poles. May participate in p53/TP53-regulated growth suppression (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12427559}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12427559}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Detected at the mitotic spindle and spindle poles. Diffusely distributed throughout the cell during interphase (By similarity). {ECO:0000250}.
Interaction partners:
- Cadherin EGF LAG seven-pass G-type receptor 2
- Myosin-binding protein H-like
- Sortilin
Sequence:
MEDLKEDIKFIVDETLDFGGLSPSDSHEEEDITVLVSPEKPLRRGLAHRSNPNEVAPALQGVRFSLGPLSPEKLEEILDEANRLAAQLEECALKDRERAGTGPGRPSPRGKPSPRRETFVLKDSPVRDLLPTVSSWSTPPPSSLAGLRSSDKKGSARAVRVASGKKPSSIKKESPTCNLFPASKSPGRSPLAQPILPPRRKTGFGARTTASPPIPVRPVPQSSASNSQCSSRLQGAAVKSSSRLPVPSAIPKPATRVPLIGRSLPPGKGALAPDSLSTQKGHPSAIGHRASVSQKTNLPTTSAARGRTTSAARGRAQPLRKAAVPGPTR
Protein: Kexin (A0A1D8PEG3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Pheromone-processing carboxypeptidase KEX1
- Ste13p
- RING-type domain-containing protein
- Ubiquitin-protein ligase
- RING-type domain-containing protein
- Secreted aspartic protease 9
Sequence:
MLPIKLLIFILGYLLSPTLQQYQQIPPRDYENKNYFLVELNTTNSQKPLIDFISHYRGHYNFEHQLSSLDNHYVFSIDKSHPHNSFLGNHNSNEYNLMKRQLGHEQDYDELISYVESIHLLPMKKLSKRIPVPIEMEDVVFENRDDTGSDNHEATDEAHQKLIEIAKKLDIHDPEFTTQWHLINLKYPGHDVNVTGLWLEDILGQGIVTALVDDGVDAESDDIKQNFNSEGSWDFNNKGKSPLPRLFDDYHGTRCAGEIAAVKNDVCGIGVAWKSQVSGIRILSGPITSSDEAEAMVYGLDTNDIYSCSWGPTDNGKVLSEPDVIVKKAMIKGIQEGRDKKGAIYVFASGNGGRFGDSCNFDGYTNSIYSITVGAIDYKGLHPQYSEACSAVMVVTYSSGSGEHIHTTDIKKKCSATHGGTSAAAPLASGIYSLILSANPNLTWRDVQYISVLSATPINEEDGNYQTTALNRKYSHKYGYGKTDAYKMVHFAKTWVNVKPQAWYYSDVIQVNQTITTTPEQKAPSKRDSPQKIIHSSVNVSEKDLKIMNVERVEHITVKVNIDSTYRGRVGMRIISPTGVISDLATFRVNDASTRGFQNWTFMSVAHWGETGIGEWKVEVFVDDSKGDQVEINFKDWQFRIFGESIDGDKAEVYDITKDYAAIRRELLEKEKQNSKSTTTTSSTTTATTTSGGEGDQKTTTSAENKESTTKVDNSASITTSQTASLTSSNEQHQPTESNSDSDSDTDDENKQEGEEDNDNDNGNKKANSDNTGFYLMSIAVVGFIAVLLVMKFHKTPGSGRRRRRRDGYEFDIIPGEDYSDSDDDEDDSDTRRADEDSFDLGHRNDQRVVSASQQQRQYDRQQDEARDRLFDDFNAESLPDYENDMFKIGDEEEEEEEGQQSAKAPSNSEGNSGTSTKKYKDNEADEDHKDVVGTQ
Protein: Granzyme M (EC 3.4.21.-) (Met-ase) (Natural killer cell granular protease) (RNK-Met-1) (Q03238)
Organism: Rattus norvegicus (Rat)
Function: Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha-tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells (By similarity).
Subcellular location: Secreted. Cytoplasmic granule. Note=Granules of large granular lymphocytes.
Interaction partners:
Sequence:
LLLLLALKTLWAVGNRFEAQIIGGREAVPHSRPYMVSLQNTKSHMCGGVLVHQKWVLTAAHCLSEPLQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHPGYNLKYENDLALLKLDGRVKPSKNVKPLALPRKPRDKPAEGSRCSTAGWGITHQRGQLAKSLQELDLRLLDTRMCNNSRFWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVCGKGKVDGILSFSSKNCTDIFKPTVATAVAPYSSWIRKVIGRWSPQPLT
Protein: Asator, isoform J (EC 2.7.11.1) (L0MN72)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHLQEYLRNDENASAPDDGNQSCQPSSKQDQYLSPNRNCQKNLLRLYPPPPSKPPPLVGAILQTRLLHQISPSAIADADADLNAVGELLYPNVLQRSATLPAKHNRLGVRSRVTFKVPSSNLPAQDSYSHQPRNQVAVAAKDGILVDVKAKESVKMTSEDLLQPGHVVKERWKVVRKIGGGGFGEIYEGQDLITREQVALKVESARQPKQVLKMEVAVLKKLQGKEHVCRFIGCGRNDRFNYVVMQLQGKNLAELRRAQPRGAFSLSTTLRLGLQILKAIESIHSVGFLHRDIKPSNFSVGRLPYNCRRVYMLDFGLARQYTTGTGEVRCPRAAAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVNGQLPWRKIKDKEQVGLTKEKYDHRILLKHLPSDLKQFLEHIQSLTYGDRPDYAMLIGLFERCMKRRGVKESDPYDWEKVDSTAIGNISATGNPSIPIKSDYMHGNITQMTVAASNASGTEYIRKRAEIETAHITATDPLNIKEKVDKNCNATSLAQPAKGSGEPMVQHGNAANNQNITSKGLQQQSTLTNSQVAIANIQSAPSMIEREDVQYTKLEEGAPTKFITMKPNGECDNVDIAAKCIFEQKHVEANDDIVGRASLSGVEQHYKSQIKKHNSPEIANKQIQRTGTVTNDKTSEVNRSTEEQKSTFGRLRVLTAPPMSVHDLPSGGGHSHQVSDLSGKQDPYAATSNAAPIGINSSSTKFGSQHGQIFGLAAMPPINRRSATSTNLRPSSSASQRINSGSTIGGAVGNGSNTARSSVAGDHSVTQFALIDDENVSALQQVTKGGALTLASQWKSQFDDSEDTTDNEWNREHQLQPNLEQLIKLDISLPLNEAKPFPQHGVAGTGKLINPPGEAKGRPKRYTLNITGIENYEALRISIPNCWSEPAMGNVLRKGLEPPAVQQAAFDDTVYRMDIARNVCVRETYSEITHLARPSTSSVLRNRLPSPFKKDSALQLNSTNDSLDKSRHRNSLPNVSVNDIFDDLQMKLNLDLGSAIQENNCCISGRLEIRVIPKDTSHPDDSVYYDAMGAVKNTPTANEGHDHSDQAVNNCDEMEATSAVIAFPNKSISKIMSPPGRDATEERTGASLCSLYSAGVNKLKLNGNTAPRTQFKKGSTDGFGENESEFDFPLLNPSKIPVRQSKCASWAGADFISASKPLESAEVPQEIPYHPQSDTTYSVIDSIPVRKTTYSIALECPPNISDLTPGLSYFYCNIVVPLRLFSILLTES
Protein: T-cell leukemia, homeobox 1 (Transcription factor) (Q9QX99)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MEHLGPHHLHPGHAEPISFGIDQILNSPDQGGCMGPASRLQDGDYGLGCLVGGAYTYGGGGSAAGAGAGGTGAYGAGGPGGPGGPAGGGGGACSMGPLPGSYNVNMALAGGPGPGGGGGGGGAGGAGALSAAGVIRVPAHRPLAGAVAHPQPLATGLPTVPSVPAVPGVNNLTGLTFPWMESNRRYTKDRFTGHPYQNRTPPKKKKPRTSFTRLQICELEKRFHRQKYLASAERAALAKALKMTDAQVKTWFQNRRTKWRRQTAEEREAERQQANRILLQLQQEAFQKSLAQPLPADPLCVHNSSLFALQNLQPWSDDSTKITSVTSVASACE
Protein: Probable DNA-binding protein creA (Carbon catabolite repressor A) (A2QCJ9)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Transcription regulator component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Represses the transcription of the alcR, alcA and aldA genes by binding to a GC-rich region in their promoter. Also plays a role in response to carbon starvation and the control of extracellular proteases activity (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MPPPASSVDFSNLLNPQNNSTDSTPSTPVDSSKTPSTPSSTQSNSNMASSVSLLPPLMKGARPATEEVRQDLPRPYKCPLCDRAFHRLEHQTRHIRTHTGEKPHACQFPGCTKRFSRSDELTRHSRIHNNPNSRRSNKAQHLAAAAAAAAGQDNAMANTASAMMPPPSKPMTRSAPVSQVGSPDISPPHSFSNYASHMRSNLGPYARKGERASSGMDINLLATAASQVERDEHFSFHAGPRNHHLFSSRHHGSGRLPSLSAYAITHNMSRSHSHEDDDGYSHRVKRSRPNSPNSTAPSSPTFSHDSLSPTPDHTPLATPAHSPRLRPLGSSDLHLPSIRHLSLHHTPALAPMEPQPEGPNYYSPSQGHHGPSISDIMSKPDGTQRKLPVPQVPKVAVQDMLNPGSGFSSVTSSTANSVAGGDLAERF
Protein: Heat shock cognate 90 kDa protein (P54651)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Protein SGT1 homolog
- CS domain-containing protein
- Heat shock 70 kDa protein, mitochondrial
- Heat shock factor-type DNA-binding domain-containing protein
- peptidylprolyl isomerase
- Luminal-binding protein 1
- Activator of 90 kDa heat shock protein ATPase homolog
- Heat shock cognate 70 kDa protein 1
- RapGAP/RanGAP domain-containing protein
- protein-serine/threonine phosphatase
Sequence:
MAESQVERFTFQAEINQLMSLIINTFYSNKEVFLRELISNASDALDKIRYQSLTDASVLESKTELEIKIIPDKTAKTLTLIDSGIGMTKTDMVKNLGTIARSGTKNFMEQLQSGAADISMIGQFGVGFYSAYLVADTVIVHSKNNDDEQYVWESSAGGEFTIALDHTEPLGRGTKIVLHMKEDQLDYLDETKIKNLVKKHSEFIQYPISLLTIKEKEVDEETTAKEGEEESTDAKIEEIEEEKEKKKVKVQEKEWDVLNKTKPLWTRNPSDVTKEEYNSFYKSISNDWEEPLAVKHFSVEGQLEFKAILFVPKKAPFDLFESKKKANNIKLYVKRVFIMDNCADIIPEYLNFVRGIVDSEDLPLNISRETLQQNKILTVIRKNLVKKCIELFNEIAENSEDYKKFYEAFSKNLKLGVHEDSQNREKFADLLRYQTSKSGDELVTLKEYVGRMKEGQNEIYYITGESKKAVENSPFIEGLKKKNLEVIYMCDPIDEYAVQQLKEYDGKKLVSITKEGLKLDETEDEKKKAEQDKAANEELLKQVKDVLGDKVEKVVLSTRLANSPCVLVTSEYGWSANMERIMKAQALRDSSMSSYMSSKKTLELNPDHPIVRDLAKKAAEKSKTFKDFVYLLYETALLTSGFSLDEPSSFASRIHRMIKLGLSIQDDSSATTEESTNTTTSDDIPPLEENDEPSEMEKVD