wanglab/gogpt-training-data huggingface dataset:
Protein: Actin-like protein ARP9 (Chromatin structure-remodeling complex protein ARP9) (SWI/SNF complex component ARP9) (Q05123)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in transcriptional regulation. Heterodimer of ARP9 and ARP7 functions with HMG box proteins to facilitate proper chromatin architecture. Heterodimer formation is necessary for assembly into RSC complex. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.
Interaction partners:
- Chromatin structure-remodeling complex protein RSC6
- Chromatin structure-remodeling complex protein RSC8
- Chromatin structure-remodeling complex subunit RSC4
- SWI/SNF chromatin-remodeling complex subunit SNF5
- Chromatin structure-remodeling complex subunit RSC9
- SWI/SNF complex subunit SWI3
- Regulator of Ty1 transposition protein 102
- Chromatin structure-remodeling complex protein RSC58
- Nuclear protein STH1/NPS1
- Chromatin structure-remodeling complex subunit RSC2
Sequence:
MAPFRQDSILIIYPRSQTTLVQFGLNEETFTVPELEIPTQIYRTTRQDGSYTYHSTNKDNKAELIKPIQNGEIIDISAFTQFLRLIFVSILSDRANKNQDAFEAELSNIPLLLITHHSWSQSDLEIITQYVFESLEINNLIQLPASLAATYSMISLQNCCIIDVGTHHTDIIPIVDYAQLDHLVSSIPMGGQSINDSLKKLLPQWDDDQIESLKKSPIFEVLSDDAKKLSSFDFGNENEDEDEGTLNVAEIITSGRDTREVLEERERGQKVKNVKNSDLEFNTFWDEKGNEIKVGKQRFQGCNNLIKNISNRVGLTLDNIDDINKAKAVWENIIIVGGTTSISGFKEALLGQLLKDHLIIEPEEEKSKREEEAKSVLPAATKKKSKFMTNSTAFVPTIEYVQCPTVIKLAKYPDYFPEWKKSGYSEIIFLGAQIVSKQIFTHPKDTFYITREKYNMKGPAALWDVQF
Protein: Sentrin-specific protease 2 (EC 3.4.22.-) (Axam2) (SMT3-specific isopeptidase 2) (Smt3ip2) (Sentrin/SUMO-specific protease SENP2) (Q9HC62)
Organism: Homo sapiens (Human)
Function: Protease that catalyzes two essential functions in the SUMO pathway. The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway (By similarity). Deconjugates SUMO2 from MTA1. Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB. Acts as a regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1 during the late phase of viral infection (By similarity).
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12192048}. Nucleus membrane {ECO:0000269|PubMed:12192048}; Peripheral membrane protein {ECO:0000269|PubMed:12192048}; Nucleoplasmic side {ECO:0000269|PubMed:12192048}. Cytoplasm {ECO:0000269|PubMed:16738331}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000269|PubMed:16738331}.
Interaction partners:
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 2
- Ran GTPase-activating protein 1
- Nuclear pore complex protein Nup153
- Segment polarity protein dishevelled homolog DVL-3
- Segment polarity protein dishevelled homolog DVL-1
- Segment polarity protein dishevelled homolog DVL-2
- Lamin-B1
- Lamin-B2
- Nuclear pore complex protein Nup133
Sequence:
MYRWLVRILGTIFRFCDRSVPPARALLKRRRSDSTLFSTVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTKPMVTSACNGTRNVAPSGEVFSNSSSCELTGSGSWNNMLKLGNKSPNGISDYPKIRVTVTRDQPRRVLPSFGFTLNSEGCNRRPGGRRHSKGNPESSLMWKPQEQAVTEMISEESGKGLRRPHCTVEEGVQKEEREKYRKLLERLKESGHGNSVCPVTSNYHSSQRSQMDTLKTKGWGEEQNHGVKTTQFVPKQYRLVETRGPLCSLRSEKRCSKGKITDTETMVGIRFENESRRGYQLEPDLSEEVSARLRLGSGSNGLLRRKVSIIETKEKNCSGKERDRRTDDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRGDIQTLKNYHWLNDEVINFYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKVHWSLVVIDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNSDLNLLEWTHHSMKPHEIPQQLNGSDCGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL
Protein: complement subcomponent C1r (EC 3.4.21.41) (F1NAB7)
Organism: Gallus gallus (Chicken)
Interaction partners:
- Uncharacterized protein
- Calponin-homology
- Mannose-binding protein
- Uncharacterized protein.
- Complement C1q C chain
- Fibrinogen C-terminal domain-containing protein.
- Complement C1q B chain
- Complement C1q A chain.
- Uncharacterized protein.
Sequence:
MEMHTPFLLWATLFTGVISSGPVPRKLFGEIRSPNYPKPYPNNNISSWDIIVPKGYVVKLTFRYFDLEPSETCFYDYVKIRADKKSLGRYCGQLGSTTGNHPGRKEFVSKGNRMHLSFHSDFSNEDNGVVVPYRGFLAYYKAVDLDECDPDNAAEDDEGLRCQHICHNYVGGYFCSCRPGYQLQSDYRSCKVECSSELFTEASGYLSSPEYPHPYPEDLQCNYSIRLEKGLSVILKFLEPFEIDDHQQVHCPYDQLQIQARGREIGEFCGKKSPGSIETKSNEVDILFFTDESGYSRGWKIHYTSERIRCPQPVPRDQFTIIRDLQPVYRYQDYFIVSCQTGYNLVEGNRTLLSFTAVCQADGTWHQPMPRCEIVNCGSPAKLTNGIFSYVNKPANNTYQSVITYQCNEPYYHIVTRGGGDRYTCSSEGTWVDRDGQKRIPACLPVCGKPDNPVIGVQRIVGGKKAREGNFPWQALTEIHGRGGGALLSDRWILTAAHTIFPKGSARNNVSLDELAKDASIFLGHSDVEQIIRMGNHPVHRIFIHPDYNPNDEHNYNGDIALLELKYPVTLGPTVLPICLPDTSNTTFYMDGYMGYVSGFGVEKNFLSNNLKYVQLPAVSREKCQSWLDSKKRENPMVFSENMFCAGFLREKRDTCQGDSGSAFTVLDLESGRWVATGIVSWGIGCAQGYGFYTKILGYLDWIKGIIKEDTL
Protein: Fructose-bisphosphate aldolase (FBP aldolase) (FBPA) (EC 4.1.2.13) (37 kDa major allergen) (Fructose-1,6-bisphosphate aldolase) (IgE-binding allergen) (Q9URB4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1548078}.
Interaction partners:
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Enolase 1
- Pyruvate decarboxylase
- Phosphoglycerate mutase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glucose-6-phosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Transketolase
- Pyruvate kinase
Sequence:
MAPPAVLSKSGVIYGKDVKDLFDYAQEKGFAIPAINVTSSSTVVAALEAARDNKAPIILQTSQGGAAYFAGKGVDNKDQAASIAGSIAAAHYIRAIAPTYGIPVVLHTDHCAKKLLPWFDGMLKADEEFFAKTGTPLFSSHMLDLSEETDDENIATCAKYFERMAKMGQWLEMEIGITGGEEDGVNNEHVEKDALYTSPETVFAVYESLHKISPNFSIAAAFGNVHGVYKPGNVQLRPEILGDHQVYAKKQIGTDAKHPLYLVFHGGSGSTQEEFNTAIKNGVVKVNLDTDCQYAYLTGIRDYVTNKIEYLKAPVGNPEGADKPNKKYFDPRVWVREGEKTMSKRIAEALDIFHTKGQL
Protein: BAG-associated GRAM protein 1 (Q8W4D4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in proteolytic processing of BAG6.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Aspartyl protease APCB1
- Two pore calcium channel protein 1
- C3HC4-type RING finger protein
- C3HC4-type RING finger protein
- ACT domain-containing protein ACR1
- BAG family molecular chaperone regulator 7
Sequence:
MVQSAVEVLLPSAWEIEVAVVASVFLIASYWLFAYRGGGDDDVVGVGFDRSRLMQNLDSGDAFDKDKIGHLRGDTQTNAAYIVKVELLAAKNLIGANLNGTSDPYAIVNCGSEKRFSSMVPGSRNPMWGEEFNFPTDELPAKINVTIHDWDIIWKSTVLGSVTINVEREGQTGPVWHSLDSPSGQVCLNINAIKLPVNAPRAVTGYAGAGRRRVTLDQQGPTIVHQKPGPLQTIFDLLPDEVVEHSYSCALERSFLYHGRMYVSAWHICFHSNVFSKQMKVVVPLGDIDEIRRSQHALINPAITIILRMGAGGHGVPPLGTPDGRVRYKFASFWNRNHTLKALQRAVNNYHAMLEVEKKERAQSALRAHSSSVKGGGKVQVKAPEDTAAVPVKFQAFIKEEVLVNIYNDVFASTPEQVLNVLLADDSTYTNEYRSARKDKNLNIEPWHTAEEYDGQVREIKFRSICNSPMCPPDTAVTEWQHVVLSPDKKVLVFETVQQPHDVPFGSYFEVHCRWRLEAKDETSSVIDIRVGVHFKKWCLMQSKIKAGAIDEYKKEVEVMLEVALSYLKSHSSSSSHGDIDKSALSSPTPENIS
Protein: RGG repeats nuclear RNA binding protein C (Q9LVT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds RNA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9SQ56}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O23523}.
Interaction partners:
- Large ribosomal subunit protein eL20x
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL20w
- Large ribosomal subunit protein eL20z
- Large ribosomal subunit protein uL4z
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL18z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein RACK1z
- Small ribosomal subunit protein eS1z
Sequence:
MASLNPFDLLGDDAEDPSQLAVALSQKVEKAAAAVQPPKAAKFPTKPAPPSQAVRESRNAPQGGRGGTGGRGGFSRGRGNGGYNRDNRNNDAPGNENGFSGGYRRPSEDADGASRGGSVGGYRVGGGREGPRRGGVANGESGDVERPPRNYDRHSRTGHGTGMKRNGGGRGNWGTTEDDIPPTSEEPTTEVEKSPVAEKQGGEDETPEAKKELTAEEKAQKEAEEAEAREMTLEEYEKILEEKKKALQATKVEERKVDTKVFESMQQLSNKKNTDEEIFIKLGSDKEKRKDATEKAKKSLSINEFLKPADGKRYNGRGGGSRGRGGRGGRGEGGNQRYAKEAAAPAIGDTAQFPSLG
Protein: Cyclin-dependent kinase 4 homolog (CDK4/6) (EC 2.7.11.22) (Cell division protein kinase 4) (Q9XTR1)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase which, in association with cyclin D-like protein cyd-1, is required for the progression through the G1 phase of the cell cycle during postembryonic development by phosphorylating and inhibiting lin-35 and fzr-1. In complex with cyd-1, involved in sex determination during gonadogenesis by regulating the asymmetric division of the somatic gonadal precursor cell (SGP).
Interaction partners:
- G1/S-specific cyclin-D
- G2/mitotic-specific cyclin-A1
- Retinoblastoma-like protein homolog lin-35
- G1/S-specific cyclin-E
- Cyclin-like domain-containing protein
- G2/mitotic-specific cyclin-B
- Cyclin N-terminal domain-containing protein
- Cell division control protein
- Fizzy-related protein homolog
- Cyclin-dependent kinase inhibitor 1
Sequence:
MTIRHILAIRKKSLELPSDLKTFLRVLANCQHLKKNKKCRRTIFSVDFQNNQRQKPSNFHFWTVIKKFSKKILKSFIIKFGNNGTIAVVFSIFPTGATPSLTFLFQALGKGAYGNVYRVRSLHDGKDYALKQIMISSKNEGIPQSVLREITVMKHLARKAHPNIISLKSVFHQLDPVRAILKINMIMERCDWDLHTFLRNIPRGVPEQQAKHVTAQIVRALDFLHTHSIIHRDLKPQNILLNRDQTVKLADFGLSKEYSNTTAFTTLVVTLWYRSPEVLLQSYYNSTVDMWALGCIVSEIYCRQPLFVGQNEAEQLTDIFKKMGTPVGKDWPSESVIARDSFPQYRPTNLKDLSPQMSKQAIEFVQQCLRYDHSKRLSARGALSHPFLKPAVATKSRVLKQINFNK
Protein: Thioredoxin 1 (Trx-1) (P0AA25)
Organism: Escherichia coli (strain K12)
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Interaction partners:
- Thioredoxin reductase
- Transcription termination factor Rho
- Phosphoadenosine 5'-phosphosulfate reductase
- Maltose/maltodextrin-binding periplasmic protein
- Glutaredoxin 3
- Glutathione reductase
- Thiol:disulfide interchange protein DsbD
- Thiol:disulfide interchange protein DsbC
- Thiol:disulfide interchange protein DsbA
- Alkyl hydroperoxide reductase C
Sequence:
MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA
Protein: Retinoic acid-induced protein 3 (G-protein coupled receptor family C group 5 member A) (Phorbol ester induced gene 1) (PEIG-1) (Retinoic acid-induced gene 1 protein) (RAIG-1) (Q8NFJ5)
Organism: Homo sapiens (Human)
Function: Orphan receptor. Could be involved in modulating differentiation and maintaining homeostasis of epithelial cells. This retinoic acid-inducible GPCR provide evidence for a possible interaction between retinoid and G-protein signaling pathways. Functions as a negative modulator of EGFR signaling (By similarity). May act as a lung tumor suppressor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9857033}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9857033}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in perinuclear vesicles, probably Golgi-associated vesicles. {ECO:0000269|PubMed:18000218}.
Interaction partners:
- Metabotropic glutamate receptor 2
Sequence:
MATTVPDGCRNGLKSKYYRLCDKAEAWGIVLETVATAGVVTSVAFMLTLPILVCKVQDSNRRKMLPTQFLFLLGVLGIFGLTFAFIIGLDGSTGPTRFFLFGILFSICFSCLLAHAVSLTKLVRGRKPLSLLVILGLAVGFSLVQDVIAIEYIVLTMNRTNVNVFSELSAPRRNEDFVLLLTYVLFLMALTFLMSSFTFCGSFTGWKRHGAHIYLTMLLSIAIWVAWITLLMLPDFDRRWDDTILSSALAANGWVFLLAYVSPEFWLLTKQRNPMDYPVEDAFCKPQLVKKSYGVENRAYSQEEITQGFEETGDTLYAPYSTHFQLQNQPPQKEFSIPRAHAWPSPYKDYEVKKEGS
Protein: Erythrocyte membrane protein band 4.1 like 2 (E9PII3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTEVGSVSEVKKDSSQLGTDATKEKPKEVAENQQNQSSDPEEEKGSQPPPAAESQSSLRRQKREKETSESRGISRFIPPWLKKQKSYTLVVAKDGGDKKEPTQAVVEEQVLDKEEPLPEEQRQAKGDAEEMAQKKQEIKVEVKEEKPSVSKEEKPSVSKVEMQPTELVSKEREEKVKETQEDKLEGGAAKRETKEVQTNELKAEKASQKVTKKTKTVQCKVTLLDGTEYSCDLEKHAKGQVLFDKVCEHLNLLEKDYFGLLFQESPEQKNWLDPAKEIKRQLRNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQDIASGRLPCSFVTHALLGSYTLQAELGDYDPEEHGSIDLSEFQFAPTQTKELEEKVAELHKTHRGLSPAQADSQFLENAKRLSMYGVDLHHAKDSEGVDIKLGVCANGLLIYKDRLRINRFAWPKILKISYKRSNFYIKVRPAELEQFESTIGFKLPNHRAAKRLWKVCVEHHTFYRLVSPEQPPKAKFLTLGSKFRYSGRTQAQTRQASTLIDRPAPHFERTSSKRVSRSLDGAPIGVMDQSLMKDFPGAAGEISAYGPGLVSIAVVQDGDGRREVRSPTKAPHLQLIEGKIDGGAGGDSGTLLTAQTITSESVSTTTTTHITKTVKGGISETRIEKRIVITGDGDIDHDQALAQAIREAREQHPDMSVTRVVVHKETELAEEGED
Protein: DASH complex subunit dad1 (Outer kinetochore protein dad1) (P87297)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. Mediates interaction between the DASH and sim4 complexes leading to loading of DASH onto the kinetochore.
Subcellular location: Nucleus {ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:16079915}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16079914}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:16079915}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20624975}. Note=Associates with the mitotic spindle and the kinetochore (PubMed:16079914). Unlike the other DASH complex members, dad1 remains associated with the kinetochore throughout the cell cycle (PubMed:16079914, PubMed:16079915). In the cytoskeleton, localizes to cortical microtubules (Probable). {ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:16079915, ECO:0000305|PubMed:20624975}.
Interaction partners:
- DASH complex subunit dam1
- DASH complex subunit ask1
- DASH complex subunit dad4
- DASH complex subunit dad2
- DASH complex subunit spc19
- DASH complex subunit dad3
- DASH complex subunit spc34
- DASH complex subunit duo1
- Kinetochore protein nsk1
- Kinetochore protein ndc80
Sequence:
MSSENMDITENIQNEQNKDFDDIDFERRRRLLTLQISKSMNEVVNLMSALNKNLESINGVGKEFENVASLWKEFQNSVLQKKDREMLDAP
Protein: Protein BREAST CANCER SUSCEPTIBILITY 1 homolog (AtBRCA1) (Q8RXD4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in DNA repair and in cell-cycle control. Required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:16957774}.
Interaction partners:
- Nibrin homolog
- Serine/threonine-protein kinase ATM
- Protein BREAST CANCER SUSCEPTIBILITY 2 homolog B
- DNA repair protein RAD50
- Serine/threonine-protein kinase ATR
- DNA repair protein RAD51 homolog 1
- Protein BREAST CANCER SUSCEPTIBILITY 2 homolog A
- BRCA1-associated RING domain protein 1
- Double-strand break repair protein MRE11
- RING-type E3 ubiquitin transferase BRCA1
Sequence:
MADTSHLERMGRELKCPICLSLYNSAVSLSCNHVFCNACIVKSMKMDATCPVCKIPYHRREIRGAPHMDSLVSIYKNMEDASGIKLFVSQNNPSPSDKEKQVRDASVEKASDKNRQGSRKGRASKRNEYGKTKEIDVDAPGPIVMKPSSQTKKRVQLLQNLSAESLTKPTESVETAEKPKDYTENTVIRLDEHPSLNKEGNLSPFFWLRDEDDGENSSQRTESDQLLGTTPVNVPSFSDLMDSDHESPSKEDEQQKPNPGDMFDSEMFEWTQRPCSPEILPSPVKAKVLGRDEIDLTQKKLPKVKVASSKCKNRKAGSARNTVARRSIGVSQEDNMESSAAATISEQQDSRGTSGTIIRNDVNTDENVKAKRATRSKAQSTRVQSDLNVSNEADGKQGTKRKRSSIKSSPAHPIAGPNELSLGTEIVGKGDQDQAHGPSDTHPEKRSPTEKPSLKKRGRKSNASSSLKDLSGKTQKKTSEKKLKLDSHMISSKATQPHGNGILTAGLNQGGDKQDSRNNRKSTVGKDDHTMQVIEKCSTINKSSSGGSAHLRRCNGSLTKKFTCAFCQCSEDTEASGEMTHYYRGEPVSADFNGGSKVIHVHKNCAEWAPNVYFNDLTIVNLDVELTRSRRISCSCCGLKGAALGCYNKSCKNSFHVTCAKLIPECRWDNVKFVMLCPLDASIKLPCEEANSKDRKCKRTPKEPLHSQPKQVSGKANIRELHIKQFHGFSKKLVLSCSGLTVEEKTVIAEFAELSGVTISKNWDSTVTHVIASINENGACKRTLKFMMAILEGKWILTIDWIKACMKNTKYVSEEPYEITMDVHGIREGPYLGRQRALKKKPKLFTGLKFYIMGDFELAYKGYLQDLIVAAGGTILRRRPVSSDDNEASTIVVFSVEPSKKKTLTQRRSDAEALAKSARARAASSSWVLDSIAGCQILVLI
Protein: Leukocyte surface antigen CD53 (Cell surface glycoprotein CD53) (CD antigen CD53) (Q61451)
Organism: Mus musculus (Mouse)
Function: Required for efficient formation of myofibers in regenerating muscle at the level of cell fusion. May be involved in growth regulation in hematopoietic cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22847234, ECO:0000269|PubMed:31748347, ECO:0000269|PubMed:36542833}. Cell junction {ECO:0000269|PubMed:22847234}. Membrane {ECO:0000269|PubMed:22847234}; Multi-pass membrane protein {ECO:0000269|PubMed:22847234}. Note=Concentrates in localized microdomains along the plasma membrane at the contact sites between cells of fused myotubes. {ECO:0000269|PubMed:22847234}.
Interaction partners:
- Lysosomal-associated transmembrane protein 5
- CD48 antigen
- Receptor-type tyrosine-protein phosphatase C
- CD82 antigen
- Integrin beta-2
- TYRO protein tyrosine kinase-binding protein
- CAMPATH-1 antigen
- Cathepsin S
- Leukocyte antigen CD37
Sequence:
MGMSSLKLLKYVLFIFNLLFWVCGCCILGFGIYFLVQNTYGVLFRNLPFLTLGNILVIVGSIIMVVAFLGCMGSIKENKCLLMSFFVLLLIILLAEVTIAILLFVYEQKLNTLVAEGLNDSIQHYHSDNSTMKAWDFIQTQLQCCGVNGSSDWTSGPPSSCPSGADVQGCYNKAKSWFHSNFLYIGIITICVCVIQVLGMSFALTLNCQIDKTSQALGL
Protein: Probable methyltransferase At1g29790 (EC 2.1.1.-) (Q8RWB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAGFTMSLNLLLLVAMVATNILSLYHLSSTTNFFQSTVKSSQSSVPTVPDHLLRQLHTIRAAINHLTTHQPDKSTSTSTSRAAVSSSSSSTAPKELLIYSKLSPIASACHNYPDLLHEYMNYTPFSLCPSDTDLVEKLILRGCHPLPRRRCFSRTPRNPSDSKPESNVLWSYYSCKSFDCLITKFSDLGFDLSLEKSKSQFSAYKSELDLPISQLLQIAKSANSVLRLGIDVGGGTGSFAAAMKARNVTVLTTTMNFNAPYSEAVAMRGLVPLHVPLQQRLPVFDGVVDLVRCGRAVNRWIPVTVMEFFFFDLDRILRGGGYLWLDRFFSKKVDLENVYAPMIGKLGYKKVKWAVANKADSKHGEVFLTALLQKPVAR
Protein: Thioredoxin-like fold domain-containing protein (Q583K4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDLDRDSEASSVDELTKRFVTLLSKEDFETHVVGEPEALCALVVTTFLCPHSAKLLPLVKERFVLRDRHQTRRVRYFNVALVPEERTNIQQLIEKDPVYIATKRPPSKVQKQELHRQAYEMLVELLLFLEVRSTPCMLFFVQGKIVKDSDDLNAPRLIAEGSSTAKWEAVLQNAVIRRNTIMKEYDEAKRMEKRRLERERRREARRRAREEEAEENEEEEEDY
Protein: Gap junction alpha-5 protein (Connexin-40) (Cx40) (P28234)
Organism: Rattus norvegicus (Rat)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
Interaction partners:
- Gap junction alpha-1 protein
- Gap junction alpha-4 protein
- Gap junction gamma-1 protein
- Gap junction beta-2 protein
- Gap junction alpha-8 protein
- Gap junction beta-1 protein
- Gap junction protein
- Gap junction alpha-3 protein
- NF-kappa-B inhibitor alpha
- Sodium channel protein type 5 subunit alpha
Sequence:
MGDWSFLGEFLEEVHKHSTVIGKVWLTVLFIFRMLVLGTAAESSWGDEQADFRCDTIQPGCQNVCYDQAFPISHIRYWVLQIIFVSTPSLVYMGHAMHTVRMQEKQKLREAEKAKEAGGTGTYEYLAEKAELSCWKEVNGKIVLQGTLLNTYVCTILIRTAMEVAFMVGQYLLYGIFLDTLHVCRRSPCPHPVNCYVSRPTEKNVFIVFMMAVAGLSLFLSLAELYHLGWKKIRQRLAKSRQGDKHQLLGPSTSLVQGLTPPPDFNQCLKNSPDEKFFSDFSNNMGSRKNPDPLATEEVPNQEQIPEEGFIHTQYGQKPEQPSGASAGHRFPQGYHSDKRRLSKASSKARSDDLSV
Protein: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial (Complex I-KFYI) (CI-KFYI) (NADH-ubiquinone oxidoreductase KFYI subunit) (Q9CQY9)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 subunit C2
- NADH dehydrogenase 1 alpha subcomplex subunit 3
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase flavoprotein 3, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH dehydrogenase 1 alpha subcomplex subunit 12
Sequence:
MAPSVVLRSFSRLLAPARLPSCSSTRSKFYVREPVNAKPNWLAVGLSVGASVFMWIYLIQTHNEDVLEYKRRNGLE
Protein: Pancreatic alpha-amylase (PA) (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) (P00689)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Glycogen phosphorylase, liver form
- Glycogen phosphorylase, brain form
- Glycogen phosphorylase, muscle form
- 1,4-alpha-glucan branching enzyme
- Glycogen debranching enzyme
- Lysosomal alpha-glucosidase
- Glucosidase, alpha; neutral C
- Alpha-amylase.
- Pancreatic triacylglycerol lipase
- Insulin-2
Sequence:
MKFVLLLSLIGFCWAQYDPHTADGRTAIVHLFEWRWADIAKECERYLAPKGFGGVQVSPPNENIIINNPSRPWWERYQPISYKICSRSGNENEFKDMVTRCNNVGVRIYVDAVINHMCGSGNSAGTHSTCGSYFNPNNREFSAVPYSAWYFNDNKCNGEINNYNDANQVRNCRLSGLLDLALDKDYVRTKVADYMNNLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAIKGSEYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFVPTDRALVFVDNHDNQRGHGAGGASILTFWDARMYKMAVGFMLAHPYGFTRVMSSYRRTRNFQNGKDVNDWIGPPNNNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVAFRNVVNGQPFANWWDNGSNQVAFSRGNRGFIVFNNDDWALSSTLQTGLPAGTYCDVISGDKVNGNCTGLKVNVGSDGKAHFSISNSAEDPFIAIHADSKL
Protein: Uncharacterized protein YMR160W (Q03823)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MDVVQQKQDKQLQHQTQEQQQIREDQQEVPPQRPRQQNRWKPWWNSTADDEPNTGRIAEYPNGQGRSSPTTDFQDSVNSNNDNKGIWSKIASFATSRYRSAPIVVDDNTRYSQLNTEQINFLENEAKDIISKKSKSWCWYEAIPHISNSSNIIDSIDTPGIISVSGTGSAKCPLPLNKYPGEGGNPGYNVFINDSLILPSDNPLNFLHVQPLRTKVLNTIKNYYNFPNEQHLYLRQKKTALLKDKRIIIISVVGDLPEKYEQRSLESQRSAYYLSRKLSQNLAQEQPQRVLTLSFQCPLHNQDLIPTYKECVELLNHWAHLFKEVDSIFFVGVYHSVPLTLLLAKYIVQNNEVLEFDENTTVSVLSFQSCLQGYRFWDHSTDFTSNSYNNLGSNSSTNENDSNDHDSNNDFTTKSQQIKEKQLFQGIDKKQQDTLSKIKNYRRIDSSESKLVQDALDWLLFNWDTFRLTFFGKLYDNFMTISEKLAIDYNHPKILRNLWCNGKYMGIDLKNANNLNLDTDDEATSNINDVHVRTPNFESRLKIPTNRLFEITLWDILMITENLGYKQFIPIINLLSPFFISRSFNDYTLPPNIRKQYQNSNKIWLQEMDSKWKMNGHQLNYDQREGESLGSSSESLLPENISTVKDFLQFVQYQNEKSSDFVRIYSDIYDDDKVYKCFLYNTIFTKNPLSRKHLRLNIDLDTPTSILNTVNQYDLVWKIHDSFSKLIQLKNLPQREIPHALRLSISLNCFLDSTTSTSGPVFQRDTVEALRRLTEIWRTYQDWSPPTRGLKHLRDILSVLAMYDNPKNLINDVRRT