wanglab/gogpt-training-data huggingface dataset:
Protein: Dystroglycan 1 (Dystroglycan) (Dystrophin-associated glycoprotein 1) (F1M8K0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004135}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}. Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
- Dystrophin
- Agrin
- Laminin subunit alpha-2
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Utrophin
- Sarcoglycan, delta
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Sarcoglycan, alpha
- Alpha-1-syntrophin
- Gamma-sarcoglycan
Sequence:
MSVDNWLLHPLWGQTFLLLLSVAVAQAHWPSEPSEAVRDWKNQLEASMHSVLSDFQEAVPTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLGANGSHVPQTASVFSIEVYPEDHSEPQSVRAASSDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELNNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIRGVETPAREGTMSAHLGYPVVGWHIANKKPTLPKRIRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIPPTRVSEAGTTVPGQIRPTLTIPGYVEPTAVVTPPTTTTKKPRVSTPKPATPSTDSSTTTTRRPTKKPRTPRPVPRVTTKAPITRLETASPPTRIRTTTSAVPRGGEANQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHKRPQGDKAPARFKAKLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIVGLSRRIADENGKPRPAFSNALEPDFKALSVAVAGSGSCRHLQFIPVAPPSPGTSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQDTVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP
Protein: Muscleblind-like protein 1 (Triplet-expansion RNA-binding protein) (Q9NR56)
Organism: Homo sapiens (Human)
Function: Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to expanded CUG repeat RNA, which folds into a hairpin structure containing GC base pairs and bulged, unpaired U residues.
Subcellular location: Nucleus {ECO:0000269|PubMed:10970838, ECO:0000269|PubMed:11590133, ECO:0000269|PubMed:11929853}. Cytoplasm {ECO:0000269|PubMed:18335541}. Cytoplasmic granule {ECO:0000269|PubMed:18335541}. Note=Localized with DDX1, TIAL1 and YBX1 in stress granules upon stress (PubMed:18335541). Localized in the cytoplasm of multinucleated myotubes (PubMed:18335541). Colocalizes with nuclear foci of retained expanded-repeat transcripts in myotubes from patients affected by myotonic dystrophy (PubMed:10970838, PubMed:11590133, PubMed:11929853).
Interaction partners:
- CUGBP Elav-like family member 1
- CCHC-type zinc finger nucleic acid binding protein
- Myotonin-protein kinase
- Heterogeneous nuclear ribonucleoprotein H
- Chloride channel protein 1
- KH domain-containing RNA-binding protein QKI
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoprotein L
- ATP-dependent RNA helicase A
- Heterogeneous nuclear ribonucleoprotein K
Sequence:
MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMTQSAVKSLKRPLEATFDLGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM
Protein: Gap junction beta-3 protein (Connexin-31) (Cx31) (P25305)
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 beta-2 protein
Sequence:
MDWKKLQDLLSGVNQYSTAFGRIWLSVVFVFRVLVYVVAAERVWGDEQKDFDCNTRQPGCTNVCYDNFFPISNIRLWALQLIFVTCPSMLVILHVAYREERERKHRQKHGEHCAKLYSHPGKKHGGLWWTYLFSLIFKLIIELVFLYVLHTLWHGFTMPRLVQCASVVPCPNTVDCYIARPTEKKVFTYFMVGASAVCIILTICEICYLIFHRIMRGLSKDKSTKSISSPKSSSRASTCRCHHKLLESGDLEAVPADDKLQASAPSLTPI
Protein: Large ribosomal subunit protein uL10x (60S acidic ribosomal protein P0-3) (P57691)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Interaction partners:
- Large ribosomal subunit protein uL24z
- Probable elongation factor 1-gamma 2
- Large ribosomal subunit protein eL8y
- Large ribosomal subunit protein uL3z
- Large ribosomal subunit protein P1w
- Large ribosomal subunit protein uL1y
- Large ribosomal subunit protein eL30x
- Large ribosomal subunit protein uL4z
- Large ribosomal subunit protein uL16x
- Large ribosomal subunit protein uL18y
Sequence:
MVKATKAEKKIAYDTKLCQLIDEYTQILVVAADNVGSTQLQNIRKGLRGDSVVLMGKNTMMKRSVRIHSENSGNTAILNLLPLLQGNVGLIFTKGDLKEVSEEVAKYKVGAPARVGLVAPIDVVVQPGNTGLDPSQTSFFQVLNIPTKINKGTVEIITPVELIKQGDKVGSSEAALLAKLGIRPFSYGLVVQSVYDNGSVFSPEVLDLTEDQLVEKFASGISMVTSLALAVSYPTLAAAPHMFINAYKNALAIAVATDYTFPQAEKVKEFLKDPSKFVVAAAAVSADAGGGSAQAGAAAKVEEKKEESDEEDYEGGFGLFDEE
Protein: Short-chain specific acyl-CoA dehydrogenase, mitochondrial (SCAD) (EC 1.3.8.1) (Butyryl-CoA dehydrogenase) (P16219)
Organism: Homo sapiens (Human)
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q3ZBF6}.
Interaction partners:
- Enoyl-CoA hydratase, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
- Trifunctional enzyme subunit alpha, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Peroxisomal bifunctional enzyme
- Ethylmalonyl-CoA decarboxylase
- 3-ketoacyl-CoA thiolase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Acyl-coenzyme A synthetase ACSM3, mitochondrial
Sequence:
MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
Protein: Coiled-coil domain-containing protein 102A (O01580)
Organism: Caenorhabditis elegans
Interaction partners:
- BPTI/Kunitz inhibitor domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Nematode cuticle collagen N-terminal domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
- Zwei Ig domain protein zig-7
- Dihydropyrimidinase 2
- Diacylglycerol kinase
- Sulfhydryl oxidase
Sequence:
MADSIASIGNRYIDNNDTDMHFLRTWAVRRCQHTDWDICERIRLGELKEARDRAAQMEKTMRWWSSCTADWRNRWSAVRDERNRAREEAETLRLNYDLLLEEKRFLAEQLYHVDSESDEPKLEISQKPEIDGTKRNAVVQTIHSISCDPPSILVKSYSAAQIEAVLREPSVDEPPVETTKSDINEELKAENEFLKDQANELNKCREKIETDGKTIQDLRLRIQSMERELMAAKNSKRASSS
Protein: Interleukin-1 receptor antagonist protein (IL-1RN) (IL-1ra) (IRAP) (IL1 inhibitor) (P25086)
Organism: Rattus norvegicus (Rat)
Function: Anti-inflammatory antagonist of interleukin-1 family of proinflammatory cytokines such as interleukin-1beta/IL1B and interleukin-1alpha/IL1A. Protects from immune dysregulation and uncontrolled systemic inflammation triggered by IL1 for a range of innate stimulatory agents such as pathogens.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P18510}.
Interaction partners:
- Interleukin-1 receptor type 1
- Interleukin-1 receptor type 2
- Interleukin-1 alpha
- Interleukin-10
- Interleukin-6
- C-C motif chemokine 2
- Tumor necrosis factor
- Interleukin-1 beta
- C-C motif chemokine 5
Sequence:
MEICRGPYSHLISLLLILLFRSESAGHPAGKRPCKMQAFRIWDTNQKTFYLRNNQLIAGYLQGPNTKLEEKIDMVPIDFRNVFLGIHGGKLCLSCVKSGDDTKLQLEEVNITDLNKNKEEDKRFTFIRSETGPTTSFESLACPGWFLCTTLEADHPVSLTNTPKEPCTVTKFYFQEDQ
Protein: UTP14A small subunit processome component (X6RJY0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MKGDFRKKKSEARTPLEQEIFNLLHKNKQPVTDPLLTPVEKASLRAMSLEEAKMRRAELQRARALQSYYEAKARREKKIKSKKYHKVVKKGKAKKALKEFEQLRKVNPAAALEELEKIEKARMMERMSLKHQNSGKWAKSKAIMAKYDLEARQAMQEQLSKNKELTQKLQVASESEEEEGGTEDVEELLVPDVVNEVQMNADGPNPWMLRSCTSDTKEAATQEDPEQLPELEAHGVSESEGEERPVAEEEILLREFEERRSLRKRSELSQDAEPAGSQETKDSGSQEVLSELRVLSQKLKENHQSRKQKASSEGTIPQVQ
Protein: GATOR1 complex protein NPRL3 (-14 gene protein) (Alpha-globin regulatory element-containing gene protein) (Nitrogen permease regulator 3-like protein) (Protein CGTHBA) (Q12980)
Organism: Homo sapiens (Human)
Function: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:28199306}. Note=Localization to lysosomes is mediated by the KICSTOR complex and is amino acid-independent. {ECO:0000269|PubMed:28199306}.
Interaction partners:
- GATOR1 complex protein DEPDC5
- GATOR2 complex protein MIOS
- GATOR1 complex protein NPRL2
- Ras-related GTP-binding protein C
- GATOR2 complex protein WDR24
- KICSTOR complex protein kaptin
- Ras-related GTP-binding protein A
- GATOR2 complex protein WDR59
- KICSTOR complex protein SZT2
- Nucleoporin SEH1
Sequence:
MRDNTSPISVILVSSGSRGNKLLFRYPFQRSQEHPASQTSKPRSRYAASNTGDHADEQDGDSRFSDVILATILATKSEMCGQKFELKIDNVRFVGHPTLLQHALGQISKTDPSPKREAPTMILFNVVFALRANADPSVINCLHNLSRRIATVLQHEERRCQYLTREAKLILALQDEVSAMADGNEGPQSPFHHILPKCKLARDLKEAYDSLCTSGVVRLHINSWLEVSFCLPHKIHYAASSLIPPEAIERSLKAIRPYHALLLLSDEKSLLGELPIDCSPALVRVIKTTSAVKNLQQLAQDADLALLQVFQLAAHLVYWGKAIIIYPLCENNVYMLSPNASVCLYSPLAEQFSHQFPSHDLPSVLAKFSLPVSLSEFRNPLAPAVQETQLIQMVVWMLQRRLLIQLHTYVCLMASPSEEEPRPREDDVPFTARVGGRSLSTPNALSFGSPTSSDDMTLTSPSMDNSSAELLPSGDSPLNQRMTENLLASLSEHERAAILSVPAAQNPEDLRMFARLLHYFRGRHHLEEIMYNENTRRSQLLMLFDKFRSVLVVTTHEDPVIAVFQALLP
Protein: Microtubule-associated protein (Q382Y3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDRRLIEMQAVITRREAEFRKQNMDLMTELMGDMRSQDNLFDKNMKDLQFRLKGLEKQKADIIKAEDEVKDKLSKLSAARTKLAEQMAEMKEKMDGIRRQRPSGSLTARGKKPSKEPSVDM
Protein: Limpet, isoform A (Limpet, isoform E) (Limpet, isoform I) (RE22626p) (RE65447p) (Q9VVB8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTDVDVLSSRMKSRLHLQTKTIGAERIKKAKDNNEDIAVLSMFLPNASAVEENRNFYCQLGDYCRLGDPRASKAGTKKMEYKTRQWHENCFCCCVCKTAIGTKSFIPREQEIYCAGCYEEKFATRCIKCNKVITSGGVTYKNEPWHRECFTCTHCNITLAGQRFTSRDEKPYCAECFGELFAKRCTACVKPITGIGGTRFISFEDRHWHHDCFVCASCKASLVGRGFITDGPDILCPDCAKQKLM
Protein: Spliceosome-associated protein CWC27 homolog (Antigen NY-CO-10) (Probable inactive peptidyl-prolyl cis-trans isomerase CWC27 homolog) (PPIase CWC27) (Serologically defined colon cancer antigen 10) (Q6UX04)
Organism: Homo sapiens (Human)
Function: As part of the spliceosome, plays a role in pre-mRNA splicing. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity.
Subcellular location: Nucleus {ECO:0000305|PubMed:29360106}.
Interaction partners:
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- E3 ubiquitin-protein ligase RNF113A
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16
- Smad nuclear-interacting protein 1
- BUD13 homolog
- Cell division cycle 5-like protein
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing-splicing factor 8
- RNA-binding motif protein, X-linked 2
Sequence:
MSNIYIQEPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVLFNPFDDIIPREIKRLKKEKPEEEVKKLKPKGTKNFSLLSFGEEAEEEEEEVNRVSQSMKGKSKSSHDLLKDDPHLSSVPVVESEKGDAPDLVDDGEDESAEHDEYIDGDEKNLMRERIAKKLKKDTSANVKSAGEGEVEKKSVSRSEELRKEARQLKRELLAAKQKKVENAAKQAEKRSEEEEAPPDGAVAEYRREKQKYEALRKQQSKKGTSREDQTLALLNQFKSKLTQAIAETPENDIPETEVEDDEGWMSHVLQFEDKSRKVKDASMQDSDTFEIYDPRNPVNKRRREESKKLMREKKERR
Protein: Cysteine desulfurase (CyD) (EC 2.8.1.7) (Q8KUU5)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Cargo protein of a type 2A encapsulin nanocompartment probably involved in sulfur metabolism. Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules.
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:33821786}.
Interaction partners:
Sequence:
MTNTVPSVPAVPNLPTQSDPFFNERSLEQLTQTVLQDLQQAGVSEAESAPTPLSVPTPALPTTSALAVPQSPTAIANVPAPPSSIDERSLAQLAQAVLQDPQLASAIASIFPSVTLPTSASVPRSVPVPPSFLPSLVPTAPPIHDEVGVIPHHQLPVPSQPTPAGLQQTASSKSGSGFYFIDEQVETAIAALHSNLTVFPQLTTSSIPTLTGAHSAGAVGFDIHQVRRDFPILQERVNGRPLVWFDNAATTQKPQVVIDRLSHYYQHENSNIHRAAHELAARSTDAYEAAREQVRHFLNAASTEEVVFVRGTTEAINLVAKSWGSQNLKEGDEIVITWLEHHANIVPWQQLSAETGARLRVVPVDDYGQVRLDEYQKLLSDRTKIVSFTQVSNALGTITPAKEIIELAHRYGAKVLLDGAQSVSHLAVDVQALDCDWFVFSGHKVFGPTGIGVLYGKQELLDATLPWQSGGNMIADVTFEKTVYQPAPARFEAGTGNIADAVGLGAALEYVQKIGLEAIAAYEHELLVHGTALLSQIPGLRLIGTAPHKAAVLSFVLEGFSPEAIGQALNREGIAVRAGHHCAQPILRRFGLETTVRPSLAFYNTFEELETLAAAIRRIQTGSLAL
Protein: APC membrane recruitment protein 3 (Amer3) (Protein FAM123C) (Q8N944)
Organism: Homo sapiens (Human)
Function: Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates to the cell membrane following binding to PtdIns(4,5)P2. {ECO:0000250}.
Interaction partners:
Sequence:
MELKRGKTFIKSSLQVSHEKPPDPAAVAAAREGTGPWSVLPGGQQRPHSEKGPQASPSAQEYDRCPNKGAQLDPKGGPAALCGATFKPVRKCKTHDSMSGAGRATAATGQLVGSASFPGSPGSRRMIDYRHFVPQMPFVPAVAKSIPRKRISLKRPKKCFRNLFHIRRNKTEDLASLAAEGKSLPSPGDPSDPGGRRSKAFLPPGEGPGLDGLCQDLLDSELLADASFGLCRALCEDVASLQSFDSLTGCGEVFADESSVPSLELNEGPESPTQAAQGLESKVPRGPLQGSVEQLASPAQNEASDFTRFWDSVNRSVRQQQRALLGPWLSGPQGTDRDQSRLDTAGLAELPLCPCRDPRSGSKASSIDTGTPKSEQPESVSTSDEGYYDSFSPGLEEDKKEAESPGTPAATFPRDSYSGDALYELFHDPSEGPLGPSPDDDLCVSESLSGPALGTPLSICSFRVGAEENLAPAPGPDLLSQGFLQSSWKGKECLLKLCDTELAITMGIVSWLRRGPTPRAPPTPGQPAAPPGSQGAPRAPTEKLGGREGLASDAGGATVCSAPSRQELWAHPGTTGLLAGESKALGGATQGTGTLSRDASREEETRGHSEGLFSSMESAATSTTDTSGKNKAPVPSTWPCSQKEPGPPGVLGCFRGPWRPGHGGDTLDAEPMLAGCVARVAALKISSNEQPPAAWPPRQDMGSGLFGQRWARGPDMLEQKQSSSSPSMTTIHGLPYSASTQDQRCRDRVQDLSWLRVEPTGLGVQAWASVEDQPLQLSTEAVEQVAHGSQLDSEPRSAPAARWSSQGHHPESLGLTLNSQQEGGVSASAPECRCSLLAREGLLCGQPEVGASGPAMAEPHL
Protein: Trafficking protein, kinesin binding 2 (Q6P9N8)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Mitochondrial Rho GTPase 2
- Mitochondrial Rho GTPase 1
- Kinesin heavy chain isoform 5A
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid receptor subunit delta
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit alpha-5
- Gamma-aminobutyric acid receptor subunit alpha-3
- Gamma-aminobutyric acid receptor subunit beta-3
Sequence:
MSQSQNAIFKSRTGEANLMSSNHRDSESITDVCSNEDLPEVELVNLLEEQLPQYKLRVDSLFLYENQDWAQSSHQQQDAPETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNEALEEQLGQAFDQVNQLQHELSKKDELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMLHEKLRELEEENMALRSKACHIKTETFTYEEKEQQLVNDCVKELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRSKSGPSAHLCFSQSYGVFTGESLAAEIEGTMRKKLSLDEESVSKQKAQQKRVFDTVKVANDTRGRSVTFPVLLPIPGSNRSSVIMTAKPFESGVQPAEDKTLLSPGGSTEVPGNSQPTNPPGSPEDSDLATALHRLSLRRQNYLSEKQFFAEEWERKIQILAEQEEEVSSCDAPTENLASVCTDQSETTDLGSASCLRGFMPEKLQIVKPLEGSQTLHHWQQLAQPNLGTILDPRPGVITKGFTQVPKDVVYHISDLEEDEEEGITFQVQQPLQLEQKPALPTPVTGIFLPPMTSAGGPGTVATSNPGKCLSFTNSTFTFTTCRILHPSDITQVTPSSGFPSLACGSSASSSSNTAVNSPAASYRLSIGESITNRRDSTITFSSTRSLAKLLQERGISAKVYHSPASENPLLQPCPKALATPSTPPNSPAQSPCSSPLPFEPRVHVSENFLASRPAETFLQEMYGLRPSRAPPDVGQLKMNLVDRLKRLGIARVVKTPDPQENGKSREAEMGLQKPDPAVYLNSGGSLLCGLRRNQSLPVMMGSFGAPVCTTSPKMGILKED
Protein: Lectin CaBo (Lectin Cbo) (P58906)
Organism: Canavalia bonariensis
Function: D-mannose-specific lectin.
Interaction partners:
Sequence:
MAISKKSSLYLPIFTFITMLLMVVNKVSSSTADANALHFTFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGNSVGRALFYAPVHIWESSAVVASFDATFKFLIKSPDSEPADGITFFIANIDSSIPSGSGGRLLGLFPDANIIKNSTTIDFNAAYNADTIVAVELDTYPNTDIGDPNYPHIGIDIKSIRSKKTTRWNIQNGKVGTAHINYNSVGKRLSAIVSYPNSDSATVSYDVDLDNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKSN
Protein: Cell adhesion molecule 2 (Immunoglobulin superfamily member 4D) (IgSF4D) (Nectin-like protein 3) (NECL-3) (Synaptic cell adhesion molecule 2) (SynCAM 2) (Q8BLQ9)
Organism: Mus musculus (Mouse)
Function: Adhesion molecule that engages in homo- and heterophilic interactions with the other nectin-like family members, leading to cell aggregation. Important for synapse organization, providing regulated trans-synaptic adhesion. Preferentially binds to oligodendrocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein. Synapse {ECO:0000250}. Cell projection, axon {ECO:0000250}. Note=Found in the axoplasm of myelinated axons. {ECO:0000250}.
Interaction partners:
Sequence:
MIWKRSAVLRFYSVCGLLLQGSQGQFPLTQNVTVVEGGTAILTCRVDQNDNTSLQWSNPAQQTLYFDDKKALRDNRIELVRASWHELSISVSDVSLSDEGQYTCSLFTMPVKTSKAYLTVLGVPEKPQISGFSSPVMEGDLMQLTCKTSGSKPAADIRWFKNDKEIKDVKYLKEEDANRKTFTVSSTLDFRVDRSDDGVAVICRVDHESLNATPQVAMQVLEIHYTPSVKIIPSTPFPQEGQALTLTCESKGKPLPEPVLWTKDGAELPDPDRMVVSGRELNILFLNKTDNGTYRCEATNTIGQSSAEYVLIVHDVPNTLLPTTIIPSLTTAPVTTSVTITTSPSTSASSSSRRDPNSLAGQNGPDHALIGGIVAVVVFVTLCSIFLLGRYLARHKGTYLTNEAKGAEDAPDADTAIINAEGSQVNAEEKKEYFI
Protein: Protein disulfide-isomerase 2-3 (AtPDIL2-3) (EC 5.3.4.1) (Protein disulfide-isomerase 5-2) (AtPDIL5-2) (Protein disulfide-isomerase 9) (PDI9) (O48773)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000305}.
Interaction partners:
- Endoplasmic reticulum oxidoreductin-1
- Endoplasmic reticulum oxidoreductin-2
- Calreticulin-2
- Heat shock 70 kDa protein BIP1
- Protein YIP
- Calreticulin-1
- Transcription factor MEE8
- Prostaglandin E synthase 2
- MD-2-related lipid-recognition protein 3
- Thioredoxin-like 3-1, chloroplastic
Sequence:
MYKSPLTLLTLLTICFGFFDLSSALYGSSSPVVQLTASNFKSKVLNSNGVVLVEFFAPWCGHCKALTPTWEKVANILKGVATVAAIDADAHQSAAQDYGIKGFPTIKVFVPGKAPIDYQGARDAKSIANFAYKQIKGLLSDRLEGKSKPTGGGSKEKKSEPSASVELNASNFDDLVIESNELWIVEFFAPWCGHCKKLAPEWKRAAKNLQGKVKLGHVNCDVEQSIMSRFKVQGFPTILVFGPDKSSPYPYEGARSASAIESFASELVESSAGPVEVTELTGPDVMEKKCGSAAICFISFLPDILDSKAEGRNKYLEMLLSVAEKFKKQPYSFMWVAAVTQMDLEKRVNVGGYGYPAMVAMNVKKGVYAPLKSAFELQHLLEFVKDAGTGGKGNVPMNGTPEIVKTKEWDGKDGELIEEDEFSLDELMGGDDAVGSKDEL
Protein: 26S proteasome regulatory non-ATPase subunit (Q580S3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proteasome regulatory ATPase subunit 5
- Proteasome subunit beta
- Proteasome regulatory ATPase subunit 6
- Ubiquitin carboxyl-terminal hydrolase
- Proteasome regulatory non-ATPase subunit 8
- Proteasome subunit beta
- Proteasome subunit alpha type
- 26S proteasome regulatory subunit 4 homolog
- Proteasome regulatory non-ATP-ase subunit 5
- Proteasome subunit beta
Sequence:
MSDNRKAVDVTVLSEDPKKKENEKKAREAESLKMSEEDERIKGQVELLVTRVGDSNTELAAVAVDQLIDLLRTHTSGSVASVPKPLKYVRSMYGQLERVQKETTNPKLAVRLHDVLSFVAMTIEFPDGQRPALEHKLLGTQDDLAHWGHEYLRFLAGCISTEWKERVSKGESVVHLDGFIQQIVSYMVKHQDEPTAVDLLMEVENIKAIIPFIDGHNHRRIASYLAAASKYLTRPMDTEALRVVYDIYVKMESYTEALFVALQLGDRAAVENLFKMCEKSSVSLQMALSCARYRFFLPNDNEEQGILSSANGNMKLSELYRHVATELDAMTPLTPEDIFKTGLDGKQSSSASDSSFKLACSFASGLVNCGYGKDMYLTGEEATWPSEQTDNRLFATTSMLGLIHLWDHADGLLEIEKYLHSDTVNIRAGACLATGISLCGVSHPYDPALGLLNDFVCAPHKEVRIGAILGLGYAYAGSMREEIRELLVPILIDGEQTMEVQCLTALALSMVFVGSTDEGMVETITHILLEMPEKDLKESATCYIILALGCLFLGRQEAADTLLDTLQTSSPIIRRYAEIVVRSCAYAATGNVVVIQNFFHAIAENDEPEDTEVPAAEGDGNGQQQKKNRQQQSTENAAHLNYKAAAVLGIALVALGEDIGTEMAKRSIIHTLLVDTVSKGEANISGRHAIPLAYALLSASNPGMQVVETLNRLSHDSDMLTAINAIVAMGVVAAGSNNARVVSKLRNLALYYQKDRFASYLFSVRLAQGFTMMGRGHLTLSPLLNDRSLVSPTALMGLLVFLHSALNFEEIILGKYSYMVSSIAPSINPRMVLAVDDQMEVVKDGVQVRVGLPVDTVAVAGKPKSITGFQTQTTPTLISVTDKVEVASQKYRPVASVVEGTFVVEEKPNME
Protein: Trimethyllysine dioxygenase, mitochondrial (EC 1.14.11.8) (Epsilon-trimethyllysine 2-oxoglutarate dioxygenase) (Epsilon-trimethyllysine hydroxylase) (TML hydroxylase) (TML-alpha-ketoglutarate dioxygenase) (TML dioxygenase) (TMLD) (Q9NVH6)
Organism: Homo sapiens (Human)
Function: Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:15754339}.
Interaction partners:
- T-cell receptor-associated transmembrane adapter 1
- E3 ubiquitin-protein ligase TRIM36
- Tripartite motif-containing protein 5
- E3 ubiquitin-protein ligase TRIM45
- E3 ubiquitin-protein ligase TRIM31
- E3 ubiquitin-protein ligase TRIM17
Sequence:
MWYHRLSHLHSRLQDLLKGGVIYPALPQPNFKSLLPLAVHWHHTASKSLTCAWQQHEDHFELKYANTVMRFDYVWLRDHCRSASCYNSKTHQRSLDTASVDLCIKPKTIRLDETTLFFTWPDGHVTKYDLNWLVKNSYEGQKQKVIQPRILWNAEIYQQAQVPSVDCQSFLETNEGLKKFLQNFLLYGIAFVENVPPTQEHTEKLAERISLIRETIYGRMWYFTSDFSRGDTAYTKLALDRHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAEQVLQKAPEEFELLSKVPLKHEYIEDVGECHNHMIGIGPVLNIYPWNKELYLIRYNNYDRAVINTVPYDVVHRWYTAHRTLTIELRRPENEFWVKLKPGRVLFIDNWRVLHGRECFTGYRQLCGCYLTRDDVLNTARLLGLQA
Protein: Histone H3.1/H3.2 (P09988)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H4
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Histone H2B-alpha
- Chromatin-associated protein swi6
- Chromo domain-containing protein 1
- Histone chaperone cia1
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- FACT complex subunit spt16
- Histone acetyltransferase gcn5
Sequence:
MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS