wanglab/gogpt-training-data huggingface dataset:
Protein: Reversion-inducing cysteine-rich protein with Kazal motifs (hRECK) (Suppressor of tumorigenicity 15 protein) (O95980)
Organism: Homo sapiens (Human)
Function: Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7. ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor: negatively regulates matrix metalloproteinase-9 (MMP9) by suppressing MMP9 secretion and by direct inhibition of its enzymatic activity. Also inhibits metalloproteinase activity of MMP2 and MMP14 (MT1-MMP).
Subcellular location: Cell membrane {ECO:0000269|PubMed:30026314, ECO:0000269|PubMed:9789069}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:9789069}.
Interaction partners:
- Matrix metalloproteinase-14
- Programmed cell death protein 4
- 72 kDa type IV collagenase
- SPARC
- Matrix metalloproteinase-9
- Metalloproteinase inhibitor 3
- Adhesion G protein-coupled receptor A2
Sequence:
MATVRASLRGALLLLLAVAGVAEVAGGLAPGSAGALCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLQRAPDYCPETMVEIWNCMNSSLPGVFKKSDGWVGLGCCELAIALECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREYCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQEFDRFCEYNPVEVSMLTCLADVREPCQLGCRNLTYCTNFNNRPTELFRSCNAQSDQGAMNDMKLWEKGSIKMPFINIPVLDIKKCQPEMWKAIACSLQIKPCHSKSRGSIICKSDCVEILKKCGDQNKFPEDHTAESICELLSPTDDLKNCIPLDTYLRPSTLGNIVEEVTHPCNPNPCPANELCEVNRKGCPSGDPCLPYFCVQGCKLGEASDFIVRQGTLIQVPSSAGEVGCYKICSCGQSGLLENCMEMHCIDLQKSCIVGGKRKSHGTSFSIDCNVCSCFAGNLVCSTRLCLSEHSSEDDRRTFTGLPCNCADQFVPVCGQNGRTYPSACIARCVGLQDHQFEFGSCMSKDPCNPNPCQKNQRCIPKPQVCLTTFDKFGCSQYECVPRQLACDQVQDPVCDTDHMEHNNLCTLYQRGKSLSYKGPCQPFCRATEPVCGHNGETYSSVCAAYSDRVAVDYYGDCQAVGVLSEHSSVAECASVKCPSLLAAGCKPIIPPGACCPLCAGMLRVLFDKEKLDTIAKVTNKKPITVLEILQKIRMHVSVPQCDVFGYFSIESEIVILIIPVDHYPKALQIEACNKEAEKIESLINSDSPTLASHVPLSALIISQVQVSSSVPSAGVRARPSCHSLLLPLSLGLALHLLWTYN
Protein: CREB-regulated transcription coactivator 3 (Transducer of regulated cAMP response element-binding protein 3) (TORC-3) (Transducer of CREB protein 3) (Q6UUV7)
Organism: Homo sapiens (Human)
Function: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR).
Subcellular location: Nucleus {ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:15589160, ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:30611118}. Cytoplasm {ECO:0000269|PubMed:15589160, ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:30611118}. Note=Appears to be mainly nuclear (PubMed:15454081). Translocates to the nucleus following adenylyl cyclase or MAP kinase activation (PubMed:30611118). {ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:30611118}.
Interaction partners:
- CREB-regulated transcription coactivator 2
- CREB-regulated transcription coactivator 1
- Cyclic AMP-responsive element-binding protein 1
- Serine/threonine-protein kinase SIK2
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
Sequence:
MAASPGSGSANPRKFSEKIALHTQRQAEETRAFEQLMTDLTLSRVQFQKLQQLRLTQYHGGSLPNVSQLRSSASEFQPSFHQADNVRGTRHHGLVERPSRNRFHPLHRRSGDKPGRQFDGSAFGANYSSQPLDESWPRQQPPWKDEKHPGFRLTSALNRTNSDSALHTSALSTKPQDPYGGGGQSAWPAPYMGFCDGENNGHGEVASFPGPLKEENLLNVPKPLPKQLWETKEIQSLSGRPRSCDVGGGNAFPHNGQNLGLSPFLGTLNTGGSLPDLTNLHYSTPLPASLDTTDHHFGSMSVGNSVNNIPAAMTHLGIRSSSGLQSSRSNPSIQATLNKTVLSSSLNNHPQTSVPNASALHPSLRLFSLSNPSLSTTNLSGPSRRRQPPVSPLTLSPGPEAHQGFSRQLSSTSPLAPYPTSQMVSSDRSQLSFLPTEAQAQVSPPPPYPAPQELTQPLLQQPRAPEAPAQQPQAASSLPQSDFQLLPAQGSSLTNFFPDVGFDQQSMRPGPAFPQQVPLVQQGSRELQDSFHLRPSPYSNCGSLPNTILPEDSSTSLFKDLNSALAGLPEVSLNVDTPFPLEEELQIEPLSLDGLNMLSDSSMGLLDPSVEETFRADRL
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1 (F8VZ70)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAARAGFQSVAPSGGAGASGGAGAAAALGPGGTPGPPVRMGPAPGQGLYRSPMPGAAYPRPGMLPGSRMTPQGPSMGPPGYGGNPSVRPGLAQSGMDQSRKRPAPQQIQQVQQQAVQNRNHNAKKKKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRLDIQEALKRPIKSALSKYDATKQKRKFSSFFKSLVIELDKDLYGPDNHLVEWHRTATTQETDGFQVKRPGDVNVRCTVLLMLDYQPPQFKLDPRLARLLGIHTQTRPVIIQAL
Protein: Protein S100-A16 (Aging-associated gene 13 protein) (Protein S100-F) (S100 calcium-binding protein A16) (Q96FQ6)
Organism: Homo sapiens (Human)
Function: Calcium-binding protein. Binds one calcium ion per monomer. Can promote differentiation of adipocytes (in vitro) (By similarity). Overexpression in preadipocytes increases their proliferation, enhances adipogenesis and reduces insulin-stimulated glucose uptake (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:17030513}. Cytoplasm {ECO:0000269|PubMed:17030513}. Note=Primarily nucleolar. A high intracellular calcium level induces nucleolar exit and nucleocytoplasmic transport, whereas a low intracellular calcium level leads to nuclear translocation and accumulation within specific region of nucleoli (PubMed:17030513).
Interaction partners:
- Protein S100-A14
- Protein S100-A3
- Protein S100-A5
- Protein S100-A11
- Protein S100-A6
- Protein S100-A10
Sequence:
MSDCYTELEKAVIVLVENFYKYVSKYSLVKNKISKSSFREMLQKELNHMLSDTGNRKAADKLIQNLDANHDGRISFDEYWTLIGGITGPIAKLIHEQEQQSSS
Protein: T-complex protein 1 subunit gamma (TCP-1-gamma) (CCT-gamma) (P39077)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
Subcellular location: Cytoplasm.
Interaction partners:
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit eta
- Phosducin-like protein 2
- Actin
- 10 kDa heat shock protein, mitochondrial
Sequence:
MQAPVVFMNASQERTTGRQAQISNITAAKAVADVIRTCLGPKAMLKMLLDPMGGLVLTNDGHAILREIDVAHPAAKSMLELSRTQDEEVGDGTTTVIILAGEILAQCAPYLIEKNIHPVIIIQALKKALTDALEVIKQVSKPVDVENDAAMKKLIQASIGTKYVIHWSEKMCELALDAVKTVRKDLGQTVEGEPNFEIDIKRYVRVEKIPGGDVLDSRVLKGVLLNKDVVHPKMSRHIENPRVVLLDCPLEYKKGESQTNIEIEKEEDWNRILQIEEEQVQLMCEQILAVRPTLVITEKGVSDLAQHYLLKGGCSVLRRVKKSDNNRIARVTGATIVNRVEDLKESDVGTNCGLFKVEMIGDEYFSFLDNCKEPKACTIMLRGGSKDILNEIDRNLQDAMAVARNVMLSPSLSPGGGATEMAVSVKLAEKAKQLEGIQQWPYQAVADAMECIPRTLIQNAGGDPIRLLSQLRAKHAQGNFTTGIDGDKGKIVDMVSYGIWEPEVIKQQSVKTAIESACLLLRVDDIVSGVRKQE
Protein: Pre-mRNA-splicing factor SPP381 (Suppressor of PRP38-1 mutation) (P38282)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the spliceosome and rRNA processing machinery. In association with the spliceosomal U4/U6.U5 tri-snRNP particle, required for splicing of pre-mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing helicase BRR2
- Pre-mRNA-splicing factor 38
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- 23 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- U4/U6 small nuclear ribonucleoprotein PRP3
- Pre-mRNA-splicing factor 6
- Small nuclear ribonucleoprotein-associated protein B
- Pre-mRNA-splicing factor SNU114
- Pre-mRNA-processing factor 31
- U4/U6 small nuclear ribonucleoprotein PRP4
Sequence:
MSFRHFKRRLDTSSADESSSADEEHPDQNVSLTEKSASLSHSDLGGEILNGTGKNRTPNDGQESNESDGSPESDESPESEESSDNSDSSDSDDMRPLPRPLFMKKKANNLQKATKIDQPWNAQDDARVLQTKKENMIKNIDKANQVAKNYETMKLRLNTNYSTNEELIKQCLLLDDNDEVDSEKERQKWFERQNERKQKHRRIQLAKQRESEEYEAKRFEAMQKGKDGNTKYDVILDKEKEKLDHKKQRSAEKVEKSHNNNRYKITRTKNVEFGDLGKNSRDYEETEYSVI
Protein: Transcriptional activator Myb isoform 2 (V-myb avian myeloblastosis viral oncogene homolog) (F1QP25)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MARRHRHSVYSSDEDDDDVEIYDHDYDGPHAKTGKRHLGKTRWTREEDEKLKRLVEHHGSEDWKVIASFLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDQIIYQAHEKLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQHAAKVSPTPLNNSYSKPHLLNYNHTPSNTSMPASSMSNQYPYYTESSRVPFPLALQLNILNFPQHGTAAIQRHYSDEDPEKEKRVKEIEMLLMSTENELKGQQALPISMNGYGGWNRGSLADSSVGIVVSVPAPSLEQGCLPEESAHGNTNSPNNDSSSTLPEFIDAIDSFFNASVSPDSDSQNIPVTPSPVCSQKALQQDLALRPQKENELFRTPNLRRSIMECSPRTPTPFKSTLTMQDSKYGPLKRVHSPSLDSGVVGTIKQEPQECEISVGGVHLDQPPLKKIKQEVESVCLQWEGQDLHTQLFPSNGPAHDMPDLLTSSVLMLPNTEKTEDGHKAAQLPRRPIGSPLQQLNTWEQVLCGKTEEQTIPSEATHKYLSNYSSRALVI
Protein: Small-subunit processome Utp21 domain-containing protein (Q383N1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Sas10 C-terminal domain-containing protein
- Uncharacterized protein
- Periodic tryptophan protein 2, putative
- Nucleolar protein 56
- U3 small nucleolar RNA-associated protein 14
- U3 small nucleolar RNA-associated protein 15 C-terminal domain-containing protein
- U3 small nucleolar RNA-associated protein 13 C-terminal domain-containing protein
- Nucleolar RNA binding protein, putative
- U3 small nucleolar ribonucleoprotein protein MPP10, putative
- CCAAT-binding factor domain-containing protein
Sequence:
MESFSPFRVVGSVCGELPVSSTMLYGAPQLMVATGRTFQLFRGKELTMLRGGPHFEKRVRAVTQAGKYRFVAEGPRIHAFVHHKPLWNCMHNDVTQSRVDHILAVDDILFCVGNDKRVVVREIKSGNMLTEFLVDGSEETRAMITPAGYNNKLLLATAQGSLQLYNFKSGVCLWREKREPGAQITALAASNFKDIIAYGTSNGRVVVLNMATNEDIMSFDQEERGAVTALAFRTDKDVLVAGSSSGEVAMWDLENGCLDGLLTRGKQVKTETEVLESPHTNTVHSIVVLPTETATIVTAGADNALMQFRFDTVDGLGVLVRERRGHMGSCTEAKFYNSDLLLTAGTDRSLRVTHLFSDRASWELSQGQLGRRGREKQMGREAMKMPPAVAIASCTARNYQWASIVSIHESSSKMCGWRMDTRSLDCKLSGIKTSMHIARAVAMSDCGNFAVIGYSSGDVSVVSIQNKGVRQLLDSSLKPDDRAHCGSVECVEVACGNNIVVTAGLDSMIKLWSLFTCRLRTVVKTDCPLHKSCIHQPSSLFIAAQHFSIRVYHCNPDIGLTTQELRVPVRTFSGHTSPITALALAPDSYRYVVSASGDAALLVWDLASSACVGQYRLASPAISLAFHPDALFMVSTHAGERGAFLWSNNLRYGFVPEVITDPRARSVEELPQLHFPTAHGAAEDAEDDTVDNAVKCEKGLPGSGNEIKEEGESDGNDDGMLGDIAGAGGNAEQEVELFDAKKDTALMQIEREKVKWAELDEIISGGMRLAGVPRSMWFDLTLLEQIREKNQPLLPPKKRDVPFFLPTTQELRPTFLVAASNSKDKEALVSRVVNAPIAQLTPVQQMLVRNEHDAFLSYILSLGSPQAVDLEIKRAVDYVEGCSYTEKELERIKDCLHGLLSFVAEWLKRRENVDLVQGILAAVIHSHGPLITKCGAELINVLEELAELQNSIRYSVDHLIGYPSCLAGTFSGSHF
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (FK506-binding protein) (FKBP) (O42993)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Has an important role in sexual development and serves as the target for rapamycin action.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Calcineurin subunit B
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Serine/threonine-protein kinase tor1
- Peptidyl-prolyl cis-trans isomerase
- Serine/threonine-protein kinase tor2
- Peptidyl-prolyl cis-trans isomerase B
- Peptidyl-prolyl cis-trans isomerase cyp3
- 40 kDa peptidyl-prolyl cis-trans isomerase
- Peptidyl-prolyl cis-trans isomerase ppi1
- Calmodulin
Sequence:
MGVEKQVISSGNGQDFPKPGDRITMHYTGTLTNGKKFDSSVDRGSPFVCTIGVGQLIRGWDEGVPKMSLGEKAKLTITPDYGYGPRGFPGLIPPNSTLLFDVELLAINDKKA
Protein: Cytochrome b-c1 complex subunit 2, mitochondrial (Complex III subunit 2) (Core protein II) (Ubiquinol-cytochrome-c reductase complex core protein 2) (Q9DB77)
Organism: Mus musculus (Mouse)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (By similarity). The 2 core subunits UQCRC1/QCR1 and UQCRC2/QCR2 are homologous to the 2 mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-MPP respectively, and they seem to have preserved their MPP processing properties. May be involved in the in situ processing of UQCRFS1 into the mature Rieske protein and its mitochondrial targeting sequence (MTS)/subunit 9 when incorporated into complex III (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome b-c1 complex subunit 9
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit 10
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
Sequence:
MKLLSRAGSFSRFYSLKVAPKVKTSAAPGGVPLQPQDLEFTKLPNGLVIASLENYAPLSRIGLFVKAGSRYEDSNNLGTSHLLRLASSLTTKGASSFKITRGIEAVGGKLSVTATRENMAYTVEGIRSDIEILMEFLLNVTTAPEFRRWEVAALRSQLKIDKAVAFQNSQTRIIENLHDVAYKNALANPLYCPDYRMGKITSEELHYFVQNHFTSARMALVGLGVSHSVLKQVAEQFLNMRGGLGLAGAKAKYRGGEIREQNGDNLVHAAIVAESAAIGNAEANAFSVLQHLLGAGPHIKRGNNTTSLLSQSVAKGSHQPFDVSAFNASYSDSGLFGIYTISQAAAAGEVINAAYNQVKAVAQGNLSSADVQAAKNKLKAGYLMSVETSEGFLSEIGSQALAAGSYMPPSTVLQQIDSVADADVVKAAKKFVSGKKSMAASGNLGHTPFLDEL
Protein: Nuclear distribution protein nudE-like 1 (Protein Nudel) (Q78PB6)
Organism: Rattus norvegicus (Rat)
Function: Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts (By similarity). Plays a role, together with DISC1, in the regulation of neurite outgrowth.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Localizes to the mitotic spindle and to the microtubules of the manchette in elongated spermatids (By similarity). Localizes to the interphase centrosome. Localizes to the cell body of the motor neurons and colocalizes with assembled neurofilaments within axonal processes. Colocalizes with DISC1 in the perinuclear region, including the centrosome. {ECO:0000250}.
Interaction partners:
- Disrupted in schizophrenia 1 homolog
- Platelet-activating factor acetylhydrolase IB subunit alpha
- 14-3-3 protein epsilon
- Kinesin heavy chain isoform 5A
- Kinesin light chain 1
- Nuclear migration protein nudC
- Nuclear distribution protein nudE homolog 1
- Kinesin light chain 3
- Serine/threonine-protein kinase PLK1
- Ankyrin 2
Sequence:
MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYVPGSVNCGVMNSNGPECPRSGRATFFHKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV
Protein: Beta-hexosaminidase subunit beta (EC 3.2.1.52) (Beta-N-acetylhexosaminidase subunit beta) (Hexosaminidase subunit B) (N-acetyl-beta-glucosaminidase subunit beta) (Q6AXR4)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A (By similarity). During fertilization is responsible, at least in part, for the zona block to polyspermy. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and inactivates the sperm galactosyltransferase-binding site, accounting for the block in sperm binding to the zona pellucida (By similarity).
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P07686}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:P20060}.
Interaction partners:
- Beta-hexosaminidase subunit alpha
- GM2 ganglioside activator
Sequence:
MPGSPRRAPGLLLQALVAMVSLALVAPFGLQPALWPMPRSVQVFPRLLYISPENFQIDNSPNSTAGPSCSLLLEAFRRYYNYIFGFYKRHHGPAKFQDKPQLEKLLVFINLEPQCDAFPSMSSDESYSLLVQEPVALLKANEVWGALRGLETFSQLVYQDAYGTFTINESTIADSPRFPHRGILIDTSRHYLPVKTIFKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDIHMVLEYARLRGIRVIPEFDSPGHTQSWGKGQKNLLTPCFIQKIRTQKVGPVDPSLNTTYVFFDTFFKEISRVFPDQFIHLGGDEVEFECWASNPNIQNFMKKKGFGNNFRRLESFYIKKILDIITSLKKSSIVWQDVFDDQVELQPGTVVEVWKSENYLNELAQVTASGFPAILSAPWYLDLISYGQDWRNYYKAEPLNFEGSEKQKQLVIGGEACLWGEYVDATNLIPRLWPRASAVGERLWSPRIITNLENAYRRLAVHRCRMVSRGIAAQPLFTGYCNYENKMEK
Protein: RGS domain-containing protein (H2KYQ8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLSVTYPMIAKTNSQILTKFHHTETHQSTPNLHHHHHHHNISGPISRTLSYLRSKMDLALSTSSLYPSRDDVRQWEISFESLLNNKFGCALFRQFLKKEFSDENMDFWLECEEFKKMKDGKKSTTQKAIEIYSEFVAEHSPKEVNLDSDTRAATKAAVEAGCKPDTFALAQSRVEQLMSKDSYRRFLRDRLFLDLLESYEITDKEDKPSSSKDKN
Protein: WASP homolog-associated protein with actin, membranes and microtubules (WAS protein homology region 2 domain-containing protein 1) (WH2 domain-containing protein 1) (Q8TF30)
Organism: Homo sapiens (Human)
Function: Acts as a nucleation-promoting factor (NPF) that stimulates Arp2/3-mediated actin polymerization both at the Golgi apparatus and along tubular membranes. Its activity in membrane tubulation requires F-actin and interaction with microtubules. Proposed to use coordinated actin-nucleating and microtubule-binding activities of distinct WHAMM molecules to drive membrane tubule elongation; when MT-bound can recruit and remodel membrane vesicles but is prevented to activate the Arp2/3 complex. Involved as a regulator of Golgi positioning and morphology. Participates in vesicle transport between the reticulum endoplasmic and the Golgi complex. Required for RhoD-dependent actin reorganization such as in cell adhesion and cell migration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18614018}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:18614018}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18614018}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:18614018}. Note=Localized to a perinuclear compartment near the microtubule-organizing center (MTOC). Also detected on tubulo-vesicular structures in the cell periphery that frequently localized along microtubules. {ECO:0000269|PubMed:18614018}.
Interaction partners:
- Actin nucleation-promoting factor WAS
- Hematopoietic lineage cell-specific protein
- Actin-related protein 2
- Cell division control protein 42 homolog
- Actin, cytoplasmic 2
- Actin-related protein 3B
- Actin-related protein 3
- Actin, cytoplasmic 1
- Actin-related protein 3C
- Actin-binding protein WASF1
Sequence:
MEDEQPDSLEGWVPVREGLFAEPERHRLRFLVAWNGAEGKFAVTCHDRTAQQRRLREGARLGPEPEPKPEAAVSPSSWAGLLSAAGLRGAHRQLAALWPPLERCFPRLPPELDVGGGGAWGLGLGLWALLWPTRAGPGEAALQELCGQLERYLGAAADGCGGATVRDALFPAEGGAADCESPREFRERALRARWVEADARLRQVIQGHGKANTMVALMNVYQEEDEAYQELVTVATMFFQYLLQPFRAMREVATLCKLDILKSLDEDDLGPRRVVALEKEAEEWTRRAEEAVVSIQDITVNYFKETVKALAGMQKEMEQDAKRFGQAAWATAIPRLEKLQLMLARETLQLMRAKELCLNHKRAEIQGKMEDLPEQEKNTNVVDELEIQFYEIQLELYEVKFEILKNEEILLTTQLDSLKRLIKEKQDEVVYYDPCENPEELKVIDCVVGLQDDKNLEVKELRRQCQQLESKRGRICAKRASLRSRKDQCKENHRFRLQQAEESIRYSRQHHSIQMKRDKIKEEEQKKKEWINQERQKTLQRLRSFKDKRLAQSVRNTSGSEPVAPNLPSDLSQQMCLPASHAVSVIHPSSRKTRGVPLSEAGNVKSPKCQNCHGNIPVQVFVPVGDQTHSKSSEELSLPPPPPPPPPPPPPPPPPPPPLRALSSSSQAATHQNLGFRAPVKDDQPRPLVCESPAERPRDSLESFSCPGSMDEVLASLRHGRAPLRKVEVPAVRPPHASINEHILAAIRQGVKLKKVHPDLGPNPSSKPTSNRRTSDLERSIKAALQRIKRVSADSEEDSDEQDPGQWDG
Protein: Bowman-Birk type proteinase inhibitor 3 (LSI-3) (B3EWN7)
Organism: Lathyrus sativus (White vetchling)
Function: Inhibits trypsin (IC(50)=4.90 nM) and, to a lesser extent, alpha-chymotrypsin (IC(50)=1.87 uM).
Interaction partners:
Sequence:
GDDVKSACCDTCLCTKSNPPTCRCVDVGET
Protein: Putative GPI-anchored protein pfl2 (Pombe flocculin 2) (Q8TFG9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in agglutination during conjugation or other aspects of colony formation (By similarity). Induces flocculation when overexpressed.
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
- Putative cell-type specific agglutination protein pfl7
- Putative cell agglutination protein pfl8
- Putative cell agglutination protein pfl3
Sequence:
MKFFTASTLFLLAAQSLNSGVSASLSDPANTPTILADDIVHGYTPATYLSSVPTLLKRATTSYNYNTSSASSSSLTSSSAASSSLTSSSSLASSSTNSTTSASPTSSSLTSSSATSSSLASSSTTSSSLASSSITSSSLASSSITSSSLASSSTTSSSLASSSTNSTTSATPTSSATSSSLSSTAASNSATSSSLASSSLNSTTSATATSSSLSSTAASNSATSSSLASSSLNSTTSATATSSSISSTVSSSTPLTSSNSTTAATSASATSSSAQYNTSSLLPSSTPSSTPLSSANSTTATSASSTPLTSVNSTTTTSASSTPLSSVSSANSTTATSTSSTPLSSVNSTTATSASSTPLTSVNSTTATSASSTPLTSVNSTSATSASSTPLTSANSTTSTSVSSTAPSYNTSSVLPTSSVSSTPLSSANSTTATSASSTPLSSVNSTTATSASSTPLSSVNSTTATSASSTPLTSVNSTTATSASSTPLTSVNSTSATSASSTPLTSANSTTSTSVSSTAPSYNTSSVLPTSSVSSTPLSSANSTTATSASSTPLTSVNSTTATSASSTPFGNSTITSSASGSTGEFTNTNSGNGDVSGSVTTPTSTPLSNSTVAPTSTFTSSGFNTTSGLPTSSASTPLSNSTVAPTSTFTSSGFNTTSGLPTSSASTPSSNSSIVPTSTFTSSGFNTTSGLPTSSASTPLSNSTVAPTSTFTSSGFNTTSGLPTSSVSTPLSNSSAYPSSGSSTFSRLSSTLTSSIIPTETFGSTSGSATGTRPTGSSSQGSVVPTTSTGSSVTSTGTGTTTGVTEVTETSTFETTEIITSTIEPTTASGTGGGNPTAAPTNEPTVTTGTETTEGTATYTEPTTFTSTFSFTTTIIGGTTTIIPVNPGNPSSSVSAPPTTSFTPGPGGSGYPSYSNTTQGMNTTSIWNSSNSTIVSNVTATITGNVTITTGDLTTIDPTTFTSTYLSSGFQTVSNTTATSGSDDDVKTASTSSSTSYTSSSSSSSSTTSAASSKASVSMGLNGLMIAAVILLVA