wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c oxidase assembly factor 3 homolog, mitochondrial (Coiled-coil domain-containing protein 56) (Mitochondrial translation regulation assembly intermediate of cytochrome c oxidase protein of 12 kDa) (Q9Y2R0)
Organism: Homo sapiens (Human)
Function: Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for efficient translation of MT-CO1 and mitochondrial respiratory chain complex IV assembly.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:23260140}; Single-pass membrane protein {ECO:0000269|PubMed:23260140}.
Interaction partners:
- Cytochrome c oxidase assembly protein COX14
- Surfeit locus protein 1
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 1
- Heme A synthase COX15
- COX assembly mitochondrial protein homolog
- Cytochrome c oxidase assembly factor 1 homolog
- Cytochrome c oxidase assembly protein COX16 homolog, mitochondrial
- Cytochrome c oxidase assembly factor 6 homolog
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
Sequence:
MASSGAGDPLDSKRGEAPFAQRIDPTREKLTPEQLHSMRQAELAQWQKVLPRRRTRNIVTGLGIGALVLAIYGYTFYSISQERFLDELEDEAKAARARALARASGS
Protein: Solute carrier organic anion transporter family member 2B1 (Organic anion transporter moatp1) (Organic anion transporting polypeptide 2B1) (OATP2B1) (Solute carrier family 21 member 9) (Q9JHI3)
Organism: Rattus norvegicus (Rat)
Function: Mediates the Na(+)-independent transport of organic anions such as taurocholate, the prostaglandins D2 (PGD2), E1 (PGE1) and E2 (PGE2), leukotriene C4, thromboxane B2 and L-thyroxine. Also plays a role in the reuptake of neuropeptides such as substance P/TAC1 and vasoactive intestinal peptide/VIP released from retinal neurons. May act as a heme transporter that promotes cellular iron availability. Also transports heme by-product coproporphyrin III (CPIII), and may be involved in their hepatic disposition (By similarity). May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (By similarity). Shows a pH-sensitive substrate specificity which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment. The exact transport mechanism has not been yet deciphered but most likely involves an anion exchange, coupling the cellular uptake of organic substrate with the efflux of an anionic compound. Hydrogencarbonate/HCO3(-) acts as a probable counteranion that exchanges for organic anions. Cytoplasmic glutamate may also act as counteranion in the placenta (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O94956}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:O94956}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:O94956}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Solute carrier family 22 member 7
- Organic anion transporter 3
- Hepatic sodium/bile acid cotransporter
- Solute carrier family 22 member 1
- ATP-binding cassette sub-family C member 2
- Bile salt export pump
- ATP-binding cassette sub-family C member 3
- Solute carrier family 15 member 1
Sequence:
MPDRSTKATMGAEDIHERKVSMEPRDSHQDAQPRGMFQNIKFFVLCHSILQLAQLMISGYLKSSISTVEKRFGLSSQTSGLLAAFNEVGNISLILFVSYFGSRVHRPRMIGCGAILVAVAGLLMALPHFISEPYRYDHSSPDRSQDFEASLCLPTTMAPASALSNDSCSSRTETKHLTMVGIMFTAQTLLGIGGVPIQPFGISYIDDFAHHSNSPLYLGILFAITMMGPGLAYGLGSLMLRLYVDIDRMPEGGINLTTKDPRWVGAWWLGFLISAGLVVLAASPYFFFPREMPKEKYELHFRQKVLAGGASIGSKGEELSSQHEPLKKQAGLPQIAPDLTVVQFIKVFPRVLLRTLRHPIFLLVVLSQVCTSSMVAGTATFLPKFLERQFSITASFANLLLGCLTIPLAIVGIVVGGVLVKRLHLSPMQCSALCLLGSLLCLLLSLPLFFIGCSTHHIAGITQDLGAQPGPSLFPGCSEPCSCQSDDFNPVCDTSAYVEYTTPCHAGCTGRVVQEALDKSQVFYTNCSCVAGNGTISAGSCESACSRLVLPFILLISLGAAVASITHTPSFMLILRGVKKEDKTLAVGMQFMLLRVLAWMPSPVIHGSAIDTTCVHWALTCGRRAVCRYYDHDLLRNRFIGLQFFFKSGSLVCFALVLAILRQQSREASTKATVKSSDLQEL
Protein: Potassium channel tetramerization domain containing 10 (F5H268)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLKNIELFDKLSLRFNGRVLFIKDVIGDEICCWSFYGQGRKIAEVCCTSIVYATEKKQTKVEFPEARIYEETLNILLYEAQDGRGPDNALLEATGGAAGRSHHLDEDEERERIERVRRIHI
Protein: Ribonuclease H2 subunit B (Ribonuclease HI subunit B) (A0A2R8YEH2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKGNPEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKKNSKMTAAQKALAKVDKSGMKNGVSLLLPRLEYNGVISAHHNLRLQGSSDSPASASRVAEITGLPTGHFVMAAQRQKRGK
Protein: Synaptotagmin-5 (Synaptotagmin V) (SytV) (O00445)
Organism: Homo sapiens (Human)
Function: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Recycling endosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=In mast cells, localizes to the endocytic recycling compartment. {ECO:0000250}.
Interaction partners:
- Synaptosomal-associated protein 25
- Vesicle-associated membrane protein 2
- Syntaxin-1A
Sequence:
MFPEPPTPGPPSPDTPPDSSRISHGPVPPWALATIVLVSGLLIFSCCFCLYRKSCRRRTGKKSQAQAQVHLQEVKGLGQSYIDKVQPEVEELEPAPSGPGQQVADKHELGRLQYSLDYDFQSGQLLVGILQAMGLAALDLGGSSDPYVRVYLLPDKRRRYETKVHRQTLNPHFGETFAFKVPYVELGGRVLVMAVYDFDRFSRNDAIGEVRVPMSSVDLGRPVQAWRELQAAPREEQEKLGDICFSLRYVPTAGKLTVIVLEAKNLKKMDVGGLSDPYVKVHLLQGGKKVRKKKTTIKKNTLNPYYNEAFSFEVPCDQVQKVQVELTVLDYDKLGKNEAIGRVAVGAAAGGAGLRHWADMLANPRRPIAQWHSLRPPDRVRLLPAP
Protein: Mitochondrial import receptor subunit TOM34 (Translocase of outer membrane 34 kDa subunit) (Q9CYG7)
Organism: Mus musculus (Mouse)
Function: Plays a role in the import of cytosolically synthesized preproteins into mitochondria. Binds the mature portion of precursor proteins. Interacts with cellular components, and possesses weak ATPase activity. May be a chaperone-like protein that helps to keep newly synthesized precursors in an unfolded import compatible state (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
Sequence:
MAPKVSDSVEQLRAAGNQNFRNGQYGEASALYERALRLLQARGSADPEEESVLYSNRAACYLKDGNCTDCIKDCTSALALVPFSIKPLLRRASAYEALEKYALAYVDYKTVLQIDNSVASALEGINRITRALMDSLGPEWRLKLPPIPVVPVSAQKRWNSLPSDNHKETAKTKSKEATATKSRVPSAGDVERAKALKEEGNDLVKKGNHKKAIEKYSESLLCSSLESATYSNRALCHLVLKQYKEAVKDCTEALKLDGKNVKAFYRRAQAYKALKDYKSSLSDISSLLQIEPRNGPAQKLRQEVNQNMN
Protein: Neuraminidase (EC 3.2.1.18) (C3W5S3)
Organism: Influenza A virus (strain swl A/California/04/2009 H1N1)
Subcellular location: Host membrane {ECO:0000256|ARBA:ARBA00004597}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004597}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000256|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000256|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane. {ECO:0000256|HAMAP-Rule:MF_04071}.
Interaction partners:
Sequence:
MNPNQKIITIGSVCMTIGMANLILQIGNIISIWISHSIQLGNQNQIETCNQSVITYENNTWVNQTYVNISNTNFAAGQSVVSVKLAGNSSLCPVSGWAIYSKDNSVRIGSKGDVFVIREPFISCSPLECRTFFLTQGALLNDKHSNGTIKDRSPYRTLMSCPIGEVPSPYNSRFESVAWSASACHDGINWLTIGISGPDNGAVAVLKYNGIITDTIKSWRNNILRTQESECACVNGSCFTVMTDGPSNGQASYKIFRIEKGKIVKSVEMNAPNYHYEECSCYPDSSEITCVCRDNWHGSNRPWVSFNQNLEYQIGYICSGIFGDNPRPNDKTGSCGPVSSNGANGVKGFSFKYGNGVWIGRTKSISSRNGFEMIWDPNGWTGTDNNFSIKQDIVGINEWSGYSGSFVQHPELTGLDCIRPCFWVELIRGRPKENTIWTSGSSISFCGVNSDTVGWSWPDGAELPFTIDK
Protein: Calcium-binding protein E (Calcium-binding protein 5) (Q869S9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Calcium-binding protein H
- Calcium-binding protein I
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco11
Sequence:
MSKVEAQIEKIFTSFDKDGDGNLSWDEVFSRMSSNSNIKDPLAATKSMFDHYNRDADTENLSIQEIREVLMSKKIKQDLIRTEKALRSKVKDFRKKYDTDNDGVVTFDEMYQLYLKDPDFDEEDDELSAEEREKAKCRRAKSSCRYFFSAVDKDKNDKLSYLEIHEYLKKHPEFDLGPSQ
Protein: dTDP-4-dehydrorhamnose reductase (EC 1.1.1.133) (dTDP-4-keto-L-rhamnose reductase) (dTDP-6-deoxy-L-lyxo-4-hexulose reductase) (dTDP-6-deoxy-L-mannose dehydrogenase) (dTDP-L-rhamnose synthase) (A0QTF8)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage. Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose (By similarity).
Interaction partners:
- dTDP-4-dehydrorhamnose 3,5-epimerase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- dTDP-glucose 4,6-dehydratase
- Glucose-1-phosphate thymidylyltransferase
- Glucose-1-phosphate thymidylyltransferase
- dTDP-RhA:a-D-GlcNAc-diphosphoryl polyprenol, a-3-L-rhamnosyl transferase
- Transcriptional regulator, LytR family protein
- NAD dependent epimerase/dehydratase family protein
- NAD-dependent epimerase/dehydratase
- Glycosyl transferase, group 2 family protein, putative
Sequence:
MDLINGMGTSPGYWRTPREPGNDHRRARLDVMAQRIVITGAGGMVGRVLADQAAAKGHTVLALTSSQCDITDEDAVRRFVANGDVVINCAAYTQVDKAEDEPERAHAVNAVGPGNLAKACAAVDAGLIHISTDYVFGAVDRDTPYEVDDETGPVNIYGRTKLAGEQAVLAAKPDAYVVRTAWVYRGGDGSDFVATMRRLAAGDGAIDVVADQVGSPTYTGDLVGALLQIVDGGVEPGILHAANAGVASRFDQARATFEAVGADPERVRPCGSDRHPRPAPRPSYTVLSSQRSAQAGLTPLRDWREALQDAVAAVVGATTDGPLPSTP
Protein: Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial (EC 1.2.4.1) (PDHE1-A type II) (P35487)
Organism: Mus musculus (Mouse)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- L-lactate dehydrogenase C chain
- [Pyruvate dehydrogenase
- Pyruvate carboxylase, mitochondrial
- L-lactate dehydrogenase A chain
- Pyruvate kinase PKM
Sequence:
MRKMLTAVLSHVFSGMVQKPALRGLLSSLKFSNDATCDIKKCDLYRLEEGPPTSTVLTRAEALKYYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSILAELTGRKGGCAKGKGGSMHMYGKNFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSALWKLPCVFICENNLYGMGTSNERSAASTDYHKKGFIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHGHSMSDPGISYRSREEVHNVRSKSDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFATTDPEPAVEDIANYLYHQDPPFEVRGAHKWLKYKSHS
Protein: 5-hydroxytryptamine receptor 2A (5-HT-2) (5-HT-2A) (Serotonin receptor 2A) (P35363)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions from intracellular stores. Affects neural activity, perception, cognition and mood. Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21645528}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:11960784}. Cell projection, axon {ECO:0000250|UniProtKB:P14842}. Cytoplasmic vesicle {ECO:0000269|PubMed:11960784}. Membrane, caveola {ECO:0000250|UniProtKB:P14842}. Presynapse {ECO:0000250|UniProtKB:P14842}.
Interaction partners:
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 2C
- 5-hydroxytryptamine receptor 2B
- 5-hydroxytryptamine receptor 1B
- Metabotropic glutamate receptor 2
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Guanine nucleotide-binding protein subunit alpha-11
- Sodium-dependent serotonin transporter
- Voltage-dependent L-type calcium channel subunit alpha-1D
- 5-hydroxytryptamine receptor 1A
Sequence:
MEILCEDNISLSSIPNSLMQLGDDSRLYPNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLSSFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPTLAYKSSQLQVGQKKNSQEDAEPTANDCSMVTLGNQHSEEMCTDNIETVNEKVSCV
Protein: Enhancer of rudimentary homolog (Mer) (P84089)
Organism: Mus musculus (Mouse)
Function: May have a role in the cell cycle.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P84090}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D1
- Protein arginine N-methyltransferase 5
- Methylosome protein WDR77
- Polymerase delta-interacting protein 3
- Protein arginine N-methyltransferase 1
Sequence:
MSHTILLVQPTKRPEGRTYADYESVNECMEGVCKMYEEHLKRMNPNSPSITYDISQLFDFIDDLADLSCLVYRADTQTYQPYNKDWIKEKIYVLLRRQAQQAGK
Protein: Ribonuclease III family protein (A0A1I9LL75)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVILSASSTVRAALDTQPRLPYNPNAPRKVKKIPNGNSFLPPPSPAPSPGISISVADLLKRPSSKEITVDVDDTYMGYETWSPSPPKLEKPRSVFNPASLAFIGDSIYELYARRHFLFPPLSIEDYNDRVRAVVRCEAQYALLNKLVDDDFLTKEERDILRWGKNLGSARTRTRRRAGNAVYNKASSLETLIGYLYLTNGKRLEKIMEKLGFSSDSSTEIVIEETNPKPSESSNLPNFILSELNLPPPLNSIINFIIWWIRWKLHKS
Protein: 60S ribosomal protein L28 (Q8IHU0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 60S ribosomal protein L5, putative
- 40S ribosomal protein S29, putative
- 40S ribosomal protein S15A, putative
- Large ribosomal subunit protein eL22
- Large ribosomal subunit protein eL42
- 60S ribosomal protein L39
- Large ribosomal subunit protein uL22
- 40S ribosomal protein S11
- 60S ribosomal protein L27a, putative
- 60S ribosomal protein L14, putative
Sequence:
MSNVSNALVWELTRKSNCFIKKNKAGKKGVFLCDPLNVNYKNTPSSSGLVKSNSTNVTLKDGKVVFSVKTSKESNVVNQHFKAKNMKNVEKLLQQHGSFEKAKNKEKLLKKYKRLSKLYETSHKKTN
Protein: Myomesin-1 (190 kDa titin-associated protein) (Myomesin family member 1) (P80473)
Organism: Bos taurus (Bovine)
Function: Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent.
Subcellular location: Cytoplasm, myofibril, sarcomere, M line {ECO:0000250}.
Interaction partners:
Sequence:
QSMSTLHQEEAFEKADQLSLKKTLEETEAFHKKLNEDHLLHAPEPVIKPGTAYKNQVPINVQAHPGKYIIESRYGVHTLEINDDTRFHSGASTLPPSXYASRFEIHFQPEIQXYRNGVPIDAEXXGAPAIPKYNDYIIITXKQPAVDGGSPILGYFIDVGIGXPSRVSEPVAALDPAEKARLKSRPSAPXTGQIIVTEEEPSEEAGTENXQRVNTELPVKXSNNAGVXEPEETGGAEITGYYVNYREVIDGVPGRXREANIKAISDEAYKXEEXTIAVPGPPHMTFKNRARVVGGLPDVVTIQEGKLLASDEHXNLKYGSEISDFTVSVFIPEEEARSVA
Protein: S-adenosyl-L-methionine-dependent methyltransferases superfamily protein (Q9SU88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSKTANFLSLRSNPLPPIFSSTGNSPFLRASSALNLPTTASKPFHSWIRASSRRRLVLGGFGGASLWMNNNMSGKFGGKSFIASARQTNPSPVEQALNKVDWPETFPFKEEDFQRYDESSDSTFYEAPRFVTHIDDPAIAALTKYYSKVLPQSDTPGVSILDMCSSWVSHYPPGYRQERIVGMGMNEEELKRNPVLTEYIVQDLNLNSNLPFEDNSFQVITNVVSVDYLTKPLEVFKEMNRILKPGGLALMSFSNRCFFTKAISIWTSTGDADHALIVGSYFHYAGGFEAPQAVDISPNPGRSDPMYVVYSRKLPMV
Protein: TipE homolog 2, isoform A (TipE-like protein 2) (Q9VZG9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKKSSTLTTTTSMPASPTLSAQTLSASKISLNSSRCGSAGSGCGSASGSMRSACQSPVRPGSGCVDAIKAKREEIEMDTLLEKAKFYTSVCLGTTAILSVFTFLFLIPFVVDPAISTIIADYDPVPVTCIVIDHIYAEGIKNCSWSSCREGCTSSLTKCHQLFVNYTRIPFSEWERNPRDLDTVNWDVSYTKFLINSEGCGYPPTTNCSIFARQYGFSHIGEPFPCFYSRAYPEVVIGRYSWENNLYHLILSLIIPNVLFAISIGVLSYWYCPCCEKACNKSSRVYAEKFPTKEDKLLCHSDEDDDMEY
Protein: E3 ubiquitin-protein ligase ARK2C (EC 2.3.2.27) (Arkadia-like protein 2C) (Ark2C) (RING finger protein 165) (E9QAU8)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that acts as a regulator of motor axon elongation. Required for efficient motor axon extension in the dorsal forelimb by enhancing the transcriptional responses of the SMAD1/SMAD5/SMAD8 effectors, which are activated downstream of BMP. Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD6, SMAD7, SKI and SNON isoform of SKIL.
Subcellular location: Nucleus {ECO:0000269|PubMed:23610558}.
Interaction partners:
- Lipoxygenase homology domain-containing protein 1
Sequence:
MVLVHVGYLVLPVFGSVRNRGAPFQRSQHPHATSCRHFHLGPPQPQQLAPDFPLAHPVQSQPGLSAHMAPAHQHSGTLHQSLTPLPTLQFQDVTGPSFLPQALHQQYLLQQQLLEAQHRRLVSHPRRNQDRVSVHPHRLHPSFDFGHQLQTPQPRYLAEGTDWDLSVDAGLSPAQFQVRPIPQHYQHYLATPRMHHFPRNSSSTQMVVHEIRNYPYPQLHFLALQGLNPSRHTSAVRESYEELLQLEDRLGNVTRGAVQNTIERFTFPHKYKKRRPQDSKGKKDEGEESDTDEKCTICLSMLEDGEDVRRLPCMHLFHQLCVDQWLAMSKKCPICRVDIETQLGADS
Protein: Ras-related protein Rap-1A (EC 3.6.5.2) (Ras-related protein Krev-1) (P62835)
Organism: Mus musculus (Mouse)
Function: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes (By similarity). Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction {ECO:0000269|PubMed:19635461}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Early endosome {ECO:0000250}. Late endosome {ECO:0000250}. Note=Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Colocalized with RAPGEF2 in the perinuclear region (By similarity). Localized with RAPGEF2 at cell-cell junctions. {ECO:0000250}.
Interaction partners:
- Krev interaction trapped protein 1
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Ral guanine nucleotide dissociation stimulator
- RAS guanyl-releasing protein 2
- Rap guanine nucleotide exchange factor 2
- RAF proto-oncogene serine/threonine-protein kinase
- Rap1 GTPase-activating protein 1
- SH3 and multiple ankyrin repeat domains protein 3
- Ras association domain-containing protein 5
- Serine/threonine-protein kinase B-raf
Sequence:
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKSCLLL
Protein: COP9 signalosome complex subunit 10 (Q12348)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes. The CSN complex is involved in the regulation of the mating pheromone response.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:14562095}. Nucleus {ECO:0000305|PubMed:14562095}.
Interaction partners:
- COP9 signalosome complex subunit 5
- Cop9 signalosome complex subunit 11
- COP9 signalosome complex subunit 9
- Cop9 signalosome-interactor 1
- 26S proteasome regulatory subunit RPN5
- Cop9 signalosome complex subunit 12
- Suppressor of kinetochore protein 1
Sequence:
MSDEDNNYDDFMLSDDEGMESIEMEEETDDEDKQNIEINEDNSQDDQDRGAARHKQHEQGTFEKHDRVEDICERIFEQGQALKEDERYKEARDLFLKIYYKEEFSSDESIERLMTWKFKSLIEILRLRALQLYFQKNGAQDLVLQILEDTATMSVFLQRIDFQIDGNIFELLSDTFEVLAPKWERVFLFDIEKVDRENMICKIDFQKNFMDQFQWILRKPGKDCKLQNLQRIIRKKIFIAVVWYQRLTMGNVFTPEISSQIEILVKDNECSSFEENNDLESVSMLLQYYILEYMNTARINNRRLFKKCIDFFEMLISKSLTFSQESGLMVILYTSKIVFILDSDSENDLSFALMRYYDRKEELKNMFLYILKHLEEMGKLRERDITSLFHKFILSGFIFTSMILEAISTDKINPFGFEQVKIALGSPIVNVLEDVYRCFAQLELRQLNASISLIPELSVVLSGIIQDIYYLAQTLKLWRKIARLYSCISISDIISMLQISDDNEMTRDDLLTILMRSIMKNRSVVYFKLDLTSDLVYFGDENKVMLPRCSKEEFRLMISPKDEETTEKARLIDFEYVNDVAIYNNPTRIRTKSSKEFFNTLRKSRETVKLPRVSNQSNEDTFLPSYMKFSNKYLELCKLASNNLE
Protein: 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7 (17-beta-hydroxysteroid dehydrogenase 7) (17-beta-HSD 7) (3-keto-steroid reductase) (EC 1.1.1.270) (Dihydrotestosterone oxidoreductase) (EC 1.1.1.210) (Estradiol 17-beta-dehydrogenase 7) (EC 1.1.1.62) (PRL receptor-associated protein) (PRAP) (Q62904)
Organism: Rattus norvegicus (Rat)
Function: Bifunctional enzyme involved in steroid-hormone metabolism and cholesterol biosynthesis. Catalyzes the NADP(H)-dependent reduction of estrogens and androgens and regulates the biological potency of these steroids (By similarity). Converts estrone (E1) to a more potent estrogen, 17beta-estradiol (E2). Converts dihydrotestosterone (DHT) to an inactive form. Participates also in the post-squalene cholesterol biosynthesis, as a 3-ketosteroid reductase (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P56937}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Methylsterol monooxygenase 1
- Lathosterol oxidase
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- Lanosterol 14-alpha demethylase
- Lanosterol synthase
- Squalene synthase
- Delta
- Ergosterol biosynthesis 28 homolog
- Very-long-chain 3-oxoacyl-CoA reductase
- 3-beta-hydroxysteroid-Delta
Sequence:
MRKVVLITGASSGIGLALCGRLLAEDDDLHLCLACRNLSKAGAVRDALLASHPSAEVSIVQMDVSNLQSVVRGAEEVKRRFQRLDYLYLNAGIMPNPQLNLKAFFCGIFSRNVIHMFSTAEGLLTQNDKITADGFQEVFETNLFGHFILIRELEPLLCHSDNPSQLIWTSSRNAKKSNFSLEDIQHAKGQEPYSSSKYATDLLNVALNRNFNQKGLYSSVTCPGVVMTNLTYGILPPFVWTLLLPVIWLLRFFAHAFTVTPYNGAEALVWLFHQKPESLNPLTKYLSGTTGLGTNYVKGQKMDVDEDTAEKFYKTLLELEKQVRITIQKSDHHS