wanglab/gogpt-training-data huggingface dataset:
Protein: Phenylalanine--tRNA ligase beta subunit, cytoplasmic (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) (Q9SGE9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277, ECO:0000305|PubMed:16297076}.
Interaction partners:
- Phenylalanine--tRNA ligase alpha subunit, cytoplasmic
- Phenylalanine--tRNA ligase, chloroplastic/mitochondrial
- UBQ, helicase-c and DEAD-like helicase domain-containing protein
- Leucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, chloroplastic/mitochondrial
- Elongation factor 1-delta 1
- Elongation factor 1-delta 2
- Isoleucine--tRNA ligase, cytoplasmic
- Eukaryotic translation initiation factor 3 subunit K
- ATP binding / aminoacyl-tRNA ligase/ nucleotide binding protein
Sequence:
MPTISVGRDRLFAALGESYTQEKFEELCFSFGIELDDVTTEKAIIRKEKHIDEEADDDEEIIYKIEIPANRPDLLCLEGLAQSLRVFIEKQEIPTYTLADISKDKILQMNVKPETSKIRPFVVCAVLRGVTFDEARYNSFIDLQDKLHQNICRRRSLVAIGTHDLDTLQGPFTYEALPPTDINFVPLKQTKSFRADELIEFYKSDMKLKKFLHIIENSPVFPVLYDSKRTVLSLPPIINGAHSAITLQTKNVFIECTATDLTKAKIVLNTMVTTFSEFCARKFEIEPVEVTYDDGKSYIYPDLAVYDMEVPLSFITDSIGVSLKVEQVTSLLTRMQLQAEQAKSSDNQCAIKVHVPPSRSDVLHPCDVMEDVAIAYGFNNIPTRKPASIKPLTLNELTDLLRIEIAMCVYTEVVTWLLCSHKENFAMLNREDVNSAVIVGNPRSADFEAMRRALMPGLLKTVGHNNKYPKPIKIFEISDVVMLDESKDVGASNRRHLAALYCGATSGFELIHGLVDRIMEVMAIPFLTIHENNVPINEKDGYYVKLSQEPEFLPGRQASIIVRGKHIGNFGIVHPEVLNNFDIPDPCSYLELDIEAIL
Protein: Uncharacterized protein (Q386T7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DUF4460 domain-containing protein
- Ubiquitin-like domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Small ribosomal subunit protein mS29
- Uncharacterized protein
- Phosphotyrosine protein phosphatase I domain-containing protein
- Methyltransferase
- Uncharacterized protein
Sequence:
MPPSQTVEYEEDFGHNLMIHREYISKRCRDRVSFELSALSYSNLELRRGQEHLAGIMNRERRGVSVGASGAPDDQVQMQTDVDANSREVLSARYLFNERRLQFCDRFQNFFQSKLENSAASDSNGHEKQHLFSLMEACAVIFGCETEAARETYYRMFLGLDSETLLEEDEALRNRIADAKLVQRVLENNKGRQEVTQSPKLQQQQDQGKPLHAVSSGTSLLNDCEEERFISSIPELSLFEDETEARANGFVEGEDDVKANNGDLTAGSFSSPASSVNLPEEFEEYAPLYKAYITHAVGKGPVASYDISTLGSTGLTAERRRWRTLMEKIVREDYHTMTEVEQMDAIVLNEQLHTVKFFDLKIGDAIRDILQLLQRETGVGSSVNRDTPVGISPNNPERRV
Protein: MRG domain-containing protein (Q9XWQ4)
Organism: Caenorhabditis elegans
Interaction partners:
- Beclin homolog
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase unc-51
- Autophagy-related protein 13 homolog
- Autophagy-related protein 11 C-terminal domain-containing protein
- t-SNARE coiled-coil homology domain-containing protein
- Protein lgg-1
- Soluble NSF attachment protein 29
- Autophagy-related protein 101
Sequence:
MDSLRGVESRSAPVVLHRIRRHSHTVTGVPIPGISADGIGSPTDHAHTPPGVLTKIDTIQTKKSSIGSSVGLISAQFSERKMNCKNCNKKTNCCCKKCTLEKLKIYSRRENITQRYEEKERLQAEILAFIDPTESLKEQITIKEDRLIKLHIAVENAKMRIAMKQSEVNKLDTTPHSKPSQFDAVFTSQSNFISRADIKKKEKSERLTKLEEEVAKKRLKYCIHACRIFPVQVYDVNVESVTVKSKNSKNWAVVNDSELQKGLRIAIRNSYINDKLRAKLANQLSNGTISLPLDLHPPFAAFTNTLQLVHLLSVIFNFRPPETLSHHDLCIRERWTKESLNRDWSTLCDAVIYLCIFIGMSHTKLKYTDPHHNLIALASFVVNDYNNINRIGSRPMCDLSEVHALIEAQRPEDCQKKDELDESWTFVD
Protein: Probable nitrite reductase [NAD(P)H] small subunit NirD (O53675)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- assimilatory sulfite reductase
- Probable respiratory nitrate reductase
- Probable nitrite extrusion protein 1 NarK1
- Nitrate reductase-like protein NarX
- Nitrate reductase alpha subunit
- Nitrate/nitrite transporter
- Nitrate reductase-like protein NarX
- Probable integral membrane nitrite extrusion protein NarK3
- Probable nitrate/nitrite transporter NarK2
- Glutamine synthetase
Sequence:
MTLLNDIQVWTTACAYDHLIPGRGVGVLLDDGSQVALFRLDDGSVHAVGNVDPFSGAAVMSRGIVGDRGGRAMVQSPILKQAFALDDGSCLDDPRVSVPVYPARVTPEGRIQVARVAV
Protein: Calpastatin (Calpain inhibitor) (Sperm BS-17 component) (P20810)
Organism: Homo sapiens (Human)
Function: Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
Interaction partners:
- Calpain-2 catalytic subunit
- Calpain-1 catalytic subunit
- Calpain small subunit 1
- Calpain-8
- Calpain small subunit 2
- Calpain-3
- Spectrin alpha chain, non-erythrocytic 1
- Talin-1
- Calpain-9
- Calpain-7
Sequence:
MNPTETKAIPVSQQMEGPHLPNKKKHKKQAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPPEPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSQSDKDLDDALDKLSDSLGQRQPDPDENKPMEDKVKEKAKAEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD
Protein: Potassium channel Cha6605_3372 (Transmembrane protein 175) (CmTMEM175) (K9UJK2)
Organism: Chamaesiphon minutus (strain ATCC 27169 / PCC 6605)
Function: Potassium channel. The channel is permeable for K(+), Rb(+) and Cs(+), while it is unable to conduct Na(+).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000269|PubMed:28723891}.
Interaction partners:
Sequence:
MVEAPEQSETGRIEAFSDGVFAIAITLLVLEIKVPQHKIVETVGLVSSLLSLWPSYLAFLTSFASILVMWVNHHRIFSLVARTDHAFFYWNGLLLMLVTFVPFPTALLAEYLIHPQARVAASVYAGIFLAIAIVFNRLWKHAATADRLLAQKADRHEVDAITKQYRFGPGLYLVAFALSFISVWLSVGVCFVLAIYFALRSNA
Protein: Tryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2) (Interferon-induced protein 53) (IFP53) (Tryptophanyl-tRNA synthetase) (TrpRS) (hWRS) [Cleaved into: T1-TrpRS; T2-TrpRS] (P23381)
Organism: Homo sapiens (Human)
Function: Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase
- Serine--tRNA ligase, cytoplasmic
- NADH dehydrogenase 1 beta subcomplex subunit 3
- Methionine--tRNA ligase, mitochondrial
- Glutamine--tRNA ligase
Sequence:
MPNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGMSSGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDRTDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKLSFDFQ
Protein: Adhesion G protein-coupled receptor E4 (EGF-like module receptor 4) (EGF-like module-containing mucin-like hormone receptor-like 4) (F4/80-like-receptor) (Seven-span membrane protein FIRE) (Q91ZE5)
Organism: Mus musculus (Mouse)
Function: May mediate the cellular interaction between myeloid cells and B-cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12023293}; Multi-pass membrane protein.
Interaction partners:
- Complement decay-accelerating factor, GPI-anchored
- Complement decay-accelerating factor transmembrane isoform
Sequence:
MLMGATRDMGSRCLLHASVPGMLLIWSILQMMNISASCPQCNENASCFNSTHCVCKEGFWTGSENRRIIEPHEKCQDINECLLKELVCKDVSYCRNKIGTYICSCVVKYPLFNWVAGIINIDHPDCYVNKSKNTGSKTHTLGVLSEFKSKEEVAKGATKLLRKVEHHILNENSDIPKKDENPLLDIVYETKRCKTMTLLEAGNNTMKVDCTSGFKEHNSGGETAVAFIAYKSLGNLLNGSFFSNEEGFQEVTLNSHIVSGAIRSEVKPVLSEPVLLTLQNIQPIDSRAEHLCVHWEGSEEGGSWSTKGCSHVYTNNSYTICKCFHLSSFAVLMALPHEEDGVLSALSVITYVGLSLSLLCLFLAAITFLLCRPIQNTSTTLHLQLSICLFLADLLFLTGINRTKPKVLCSIIAGMLHYLYLASFMWMFLEGLHLFLTVSNLKVANYSNSGRFKKRFMYPVGYGLPAFIVAVSAIAGHKNYGTHNHCWLSLHRGFIWSFLGPAAAIILINLVFYFLIIWILRSKLSSLNKEVSTLQDTKVMTFKAIVQLFVLGCSWGIGLFIFIEVGKTVRLIVAYLFTIINVLQGVLIFMVHCLLNRQVRMEYKKWFHRLRKEVESESTEVSHSTTHTKMGLSLNLENFCPTGNLHDPSDSILPSTEVAGVYLSTPRSHMGAEDVNSGTHAYWSRTISD
Protein: L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (AASD-PPT) (EC 2.7.8.7) (P50113)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the transfer of a 4'-phosphopantetheine moiety from coenzyme A to a serine residue of acceptor proteins, such as alpha-aminoadipate reductase. Necessary for alpha-aminoadipate reductase activity.
Interaction partners:
- L-2-aminoadipate reductase
- Dephospho-CoA kinase CAB5
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Homoisocitrate dehydrogenase, mitochondrial
- Orotidine 5'-phosphate decarboxylase
- Histone H4
- Zinc finger protein FZF1
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase homolog
Sequence:
MVKTTEVVSEVSKVAGVRPWAGIFVVEIQEDILADEFTFEALMRTLPLASQARILNKKSFHDRCSNLCSQLLQLFGCSIVTGLNFQELKFDKGSFGKPFLDNNRFLPFSMTIGEQYVAMFLVKCVSTDEYQDVGIDIASPCNYGGREELELFKEVFSEREFNGLLKASDPCTIFTYLWSLKESYTKFTGTGLNTDLSLIDFGAISFFPAEGASMCITLDEVPLIFHSQWFNNEIVTICMPKSISDKINTNRPKLYNISLSTLIDYFIENDGL
Protein: Karyopherin subunit alpha 1 (C9J4U1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQISNMEMAPGGVITSDMIEMIFSKSPEQQLSATQKFRKLLSKEPNPPIDEVISTPGVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRIVIQAGAVPIFIELLSSEFEDVQEQAVWALGNIAGDSTMCRDYVLDCNILP
Protein: Synaptogyrin homolog 1 (O76735)
Organism: Caenorhabditis elegans
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Ras-related protein Rab-3
- Serine/threonine-protein kinase dyf-5
- Myb_DNA-bind_5 domain-containing protein
- Actin-related protein 2/3 complex subunit
- Serpentine receptor class delta-45
- Uncharacterized protein C03B1.6
- Uncharacterized protein
- G-protein coupled receptors family 1 profile domain-containing protein
- C-type lectin domain-containing protein
- Lipid droplet-associated hydrolase
Sequence:
MENVRAYGAGLAGANFDKNTFFKKPTVLFRCAALLFGLILWYSVSKGGWHKPSDAIHPVCLYGRSSSTCSFATAVGFFAVCGAIVLIVLDAKMDQISSVPTRRRAVLADLVVSAIFTAIFLIGFFTFWSKLSAFEVDEDDENPIKTNNAKFGILSALLSFLAWGGAAFFAWRRYEEGNQATHEPNYDEHFGQVSTDVQDGYGYGGDSTGIGHVGAPPPQSSYQSGAAPQTMQQPPSNPYTQSEGYGY
Protein: Myosin binding protein C, slow-type (D3YU50)
Organism: Mus musculus (Mouse)
Interaction partners:
- Troponin T, fast skeletal muscle
- Troponin C, skeletal muscle
- Troponin I, fast skeletal muscle
- Myozenin-1
- Myosin regulatory light chain 11
- Myosin-2
- Alpha-actinin-3
- Myosin-1
- Myosin-4
- Alpha-actinin-2
Sequence:
MPEPTKKEENEVSAPAPPPEEWSLGESPAGGEEQDKQNANSQLSTLFVEKPQTGSVKVGANITFVAKVRAEDLLRKPTVKWFKGKWMDLASKAGKHLQLKETFERQTRVYTFEMQIIKAKENYAGNYRCEVTYKDKFDSCSFDLEVHESTGTTPNIDIRSAFKRSGEGQEDAGELDFSGLLKRREVKQQEEEPEIDVWELLKNANPNEYEKIAFQYGITDLRGMLKRLKRMRRVEKKSAAFAKILDPAYQVDKGGKVRFVVELADPKLEVKWFKNGQEIRPSTKYIFEHKGNERIMFINNCSLTDDSEYYVTAGDEKCSTELFVREPPIMVTKQLEDMNAYCGERVEMEVEVSEDDANVKWFKNGEEIFPGPKSRYKIKVEGKKHTLIIEGATKADSAEYSAMTTGGQSSAKLSVDLRPLKITTPLTDQTVKLGKEVCLKCEISENVPGKWTKNGLPVQEGERLKVVHKGRIHKLVIANALIEDEGEYVFTPDAYNVPLSAKVHVIDPPKIILDGLDADNTVTVIAGSKLRLEIPVTGEPPPKAIWSRADKAIMEGSGRIRAESYPDSSTLVIDVAERDDSGVYNINLKNEAGEAHASIKIKVVDIPDPPVAPNVTEVGDDWCIMNWEPPAYDGGSPILGYFIERKKKQSSRWMRLNFDLCKETTFEPKKMIEGVAYEVRIFAVNAIGISKPSMPSKPFVPLAVTSPPTLLAVDSVTDSSVTMKWRPPDQIGAAGLDGYVLEYCFEGTEDWIVANTDLIDKTKFTINGLPTDAKIFVRVKAINAAGASEPKYYSQPILVKEIIEPPKIRIPRHLKQTYIRRVGEAVNLVIPFQGKPRPELTWKKDGEEIDKNQINIRNSETDTIIFIRKAERSHSGKYDLQVKVDKYVENASIDIQIVDRPGPPQTVTIEDVWGENVALTWTPPKDDGNAAITGYTIQKADKKSMEWFTVIEHYHRTNATITELVIGNEYYFRVFAENMCGLSEDATMTKESAVIAKDGKIYKNPVYEDFNFTEAPMFTQPLVNTYAIAGYNATLNCSVRGNPKPKITWMKNKVAIVDDPRYRMFSNQGVCTLEIRKPSPYDGGTYCCKAVNDLGTVEIECKLEVKVIYQGVNTPGQPVSLEGQQQS
Protein: Perforin-1 (P1) (Cytolysin) (Lymphocyte pore-forming protein) (PFP) (P14222)
Organism: Homo sapiens (Human)
Function: Pore-forming protein that plays a key role in granzyme-mediated programmed cell death, and in defense against virus-infected or neoplastic cells. Plays an important role in killing other cells that are recognized as non-self by the immune system, e.g. in transplant rejection or some forms of autoimmune disease. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes. Perforin pores allow the release of mature caspase-7 (CASP7) into the extracellular milieu (By similarity).
Subcellular location: Cytolytic granule {ECO:0000269|PubMed:20038786, ECO:0000269|PubMed:24088571}. Secreted. Cell membrane {ECO:0000269|PubMed:20889983, ECO:0000269|PubMed:21037563}; Multi-pass membrane protein {ECO:0000269|PubMed:20889983, ECO:0000269|PubMed:21037563}. Endosome lumen {ECO:0000269|PubMed:20038786}. Note=Stored in cytolytic granules of cytolytic T-lymphocytes and secreted into the cleft between T-lymphocyte and target cell (PubMed:20038786). Inserts into the cell membrane of target cells and forms pores (PubMed:20889983). Membrane insertion and pore formation requires a major conformation change (PubMed:20889983). May be taken up via endocytosis involving clathrin-coated vesicles and accumulate in a first time in large early endosomes (PubMed:20038786). {ECO:0000269|PubMed:20038786, ECO:0000269|PubMed:20889983}.
Interaction partners:
- Granzyme B
- Granulysin
- Granzyme A
- Tumor necrosis factor ligand superfamily member 6
- T-cell surface glycoprotein CD8 alpha chain
- Serglycin
- Natural killer cells antigen CD94
- Interferon gamma
- T-cell surface glycoprotein CD4
- Granzyme H
Sequence:
MAARLLLLGILLLLLPLPVPAPCHTAARSECKRSHKFVPGAWLAGEGVDVTSLRRSGSFPVDTQRFLRPDGTCTLCENALQEGTLQRLPLALTNWRAQGSGCQRHVTRAKVSSTEAVARDAARSIRNDWKVGLDVTPKPTSNVHVSVAGSHSQAANFAAQKTHQDQYSFSTDTVECRFYSFHVVHTPPLHPDFKRALGDLPHHFNASTQPAYLRLISNYGTHFIRAVELGGRISALTALRTCELALEGLTDNEVEDCLTVEAQVNIGIHGSISAEAKACEEKKKKHKMTASFHQTYRERHSEVVGGHHTSINDLLFGIQAGPEQYSAWVNSLPGSPGLVDYTLEPLHVLLDSQDPRREALRRALSQYLTDRARWRDCSRPCPPGRQKSPRDPCQCVCHGSAVTTQDCCPRQRGLAQLEVTFIQAWGLWGDWFTATDAYVKLFFGGQELRTSTVWDNNNPIWSVRLDFGDVLLATGGPLRLQVWDQDSGRDDDLLGTCDQAPKSGSHEVRCNLNHGHLKFRYHARCLPHLGGGTCLDYVPQMLLGEPPGNRSGAVW
Protein: Palmitoyl thioesterase CPT1C (EC 3.1.2.22) (Carnitine O-palmitoyltransferase 1, brain isoform) (CPT1-B) (Carnitine O-palmitoyltransferase I, brain isoform) (CPTI-B) (Carnitine palmitoyltransferase 1C) (Carnitine palmitoyltransferase I) (CPT I-C) (F1LN46)
Organism: Rattus norvegicus (Rat)
Function: May play a role in lipid metabolic process.
Subcellular location: Synapse {ECO:0000250|UniProtKB:Q8BGD5}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8BGD5}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BGD5}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18192268}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the soma and dendritic and axonal projections. {ECO:0000250|UniProtKB:Q8BGD5}.
Interaction partners:
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Carnitine O-palmitoyltransferase 1, liver isoform
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Glutamate receptor 1
- Long-chain-fatty-acid--CoA ligase 1
- Fatty acid CoA ligase Acsl3
- Monoacylglycerol lipase ABHD6
- Long-chain-fatty-acid--CoA ligase 5
- Long-chain-fatty-acid--CoA ligase 6
- Long-chain-fatty-acid--CoA ligase 4
Sequence:
MAEAHQASSLLSSLSSDGAEVELSSSVWQEIYLSALRSWKRNLWRVWNDFLAGVVPATPLSWLFLFSTIQLACLLQLDPSLGLMEKIKELLPDWGGQHHQLQGLLAAAVFASCLWGTLIFTLHVALRLLLSHHGWLLEPHGTMSSPTKTWLALVRIFSGRHPRLFSFQRALPRQPVPGAQETVRKYLESMRPVLRDDAFDSVVALANDFLRLQAPRLQLYLQLKSWCASNYVSDWWEEFVYLRSRGSLVNSTYYMMDFLYVTPTPLQAARAGNAVHTLLLYRHLLNRQEIPPTLLMGMRPLCSAQYERMFNTTRIPGVEKDYLCHLQDSQHVAVFHQGRFFRVGTHSSNGLLSPRALEQQFQYILDDPSPACPLEEHLAALTAAPRSMWAQVRESVKTHAATALETVEGAAFFVSLDSEPAGLTRENPAASLDTYAHTLLTGQGHDRWFDKSFTLIVFSNGKLGLSVEHSWADCPVAGHLWEFTLATECFQLGYATDGHCKGHPDPALPKPQRLQWDLPKQIQPSISLALRGAKTLSGNIDCHVFPFFHFGKSFIKGCHVSSDSFIQLVLQLAHFRDRGQFCLTYESAMTRLFLEGRTETVRSCTREACQFVRAMENKERTDQQCLALFREAVDKHQALLKAAMSGQGIDRHLFALYIMSRLLHMQSPFLTQVQSQQWLLSTSQIPVQQTHLFDVHNYPDYVSSGGGFGPAHDHGYGVSYIFMGENAISFHISSKQSSTETDSHRLGQHIEDALLDVASLFQAGQQFKRQFTGLGESSGWKYSNLSCKTVDPNIPKSSTNL
Protein: Inhibitor of growth protein (Q9VEF5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU361213}.
Interaction partners:
- Paired amphipathic helix protein Sin3a
- Histone deacetylase HDAC1
- FI07430p
- BRMS1 transcriptional repressor
- Sin3A-associated protein 130, isoform C
- BRCA2-interacting transcriptional repressor EMSY
- Chromatin assembly factor 1 p55 subunit
- PHD finger protein 12
- Hat-trick, isoform D
- NuA4 complex subunit EAF3 homolog
Sequence:
MINPIASESEAINSATYVDNYIDSVENLPDDVQRQLSRIRDIDVQYRGLIRDVDHYYDLYLSLQNSADAGRRSRSISRMHQSLIQAQELGDEKMQIVNHMQEIIDGKLRQLDTDQQNLDLKEDRDRYALLDDGTPSKLQRLQSPMREQGNQAGTGNGGLNGNGLLSAKDLYALGGYAGGVVPGSNAMTSGNGGGSTPNSERSSHVSNGGNSGSNGNASGGGGGELQRTGSKRSRRRNESVVNNGSSLEMGGNESNSANEASGSGGGSGERKSSLGGASGAGQGRKASLQSASGSLASGSAATSSGAAGGGGASGAGVVGGNNSGKKKKRKVRGSGASNANASTREETPPPETIDPDEPTYCVCNQISFGEMILCDNDLCPIEWFHFSCVSLVLKPKGKWFCPNCRGERPNVMKPKAQFLKELERYNKEKEEKT
Protein: Up-regulated during septation protein 1 (Q9P6S3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in septation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:20460254}. Cell tip {ECO:0000269|PubMed:16823372}.
Interaction partners:
- WD repeat-containing protein slp1
Sequence:
MGFHGCLSTDEYEPELIEKYGNPEPPSSSILINTRPVNPFLSTFVYVGKASSSEDVSISTGEEEMRTLLVASAVKDAKGWVYLSGKDVEEIKQKIKNLQGLLGVSIKKLAVEAKIREAAKNLMVAQAKEKKGKHKQSTIEHYEQCSRRVRELSSKIWLIERKLAEFYMHLLKHMVAVCIAELKPGSCSKVSSPVSAITADESATGFRDEEIMNNEEIEQLVERMSRILEIAQSMGNSIREPSVLDAVQMNAGERLLEQVRHLELILKQIYEKKLEEDADAKDIAPRAIVNFWRLLTELFRGDNDTPEKSNALPDDELDKHLKSDFDIESFCFLLHHLLSLYQTQKKELASSNELLASVRDENTKKLKELQDIIEEQSKHMARLHREGFSEAAENNDKPKETMPCTYDSSLADDHSDTSNLSKDKANTLCAQCSVYLSEKYQQQQSLLQLESNIQQLENEKKAAKLIEKDLLSQISHVKLQFEQQIKAHHYAKDQVRNLNDEMVALRAELEVVKAMNSQPDDPDSDYAIKQNNALQNRLEALTRENELLQSRVTTLEMEKEVQEKNSATVSNLTLKQLQMENIFASLNLENSFDFGMPLMGPYTQQNLQLEDEISEISSPSYSSDDDRKTISETQPAPKQNINEEFENSTSTDGSETNKNEQGNSLSTPDNEPRLRKESLSSDVLLDGSEKPAQAELTINSENFPVDCSLPVQTGADVVVPDTTDEEVITSEPVKLEQPINENSNVEEAEKDYQPSEKDDKSLIGGILSTVEMTQSTDVNDEIENTLTIPVEVEHSDNIDKGSEENDLGKEAVDEANNNQNDVLESVVVEQSTTTDDCENKVYEGQMNDKNSSLDMVNACEGINQTAIGFVEKPDKVTELIDEAEENIDISQDISMTETNAVDDEVQAENSILQDEVEETRQDDIEKDELEDIKEVKEDENLTTLEETIEIPANDIEVQDPEQCSCMNSTENDNITTENSSEIVQVIHTEDDSLHFDDNVSTDSVSLGNKSRISMDSMRNDCEAFLPKKEKFGSLRTLHSFESSMRRVSTSAA
Protein: Endoplasmin (EC 3.6.4.-) (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Heat shock protein family C member 4) (Tumor rejection antigen 1) (gp96 homolog) (P14625)
Organism: Homo sapiens (Human)
Function: Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000305|PubMed:12475965}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P41148}. Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}.
Interaction partners:
- DnaJ homolog subfamily B member 11
- Hypoxia up-regulated protein 1
- Calreticulin
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase A4
- Protein OS-9
- Prolow-density lipoprotein receptor-related protein 1
- Peptidyl-prolyl cis-trans isomerase B
- Protein disulfide-isomerase A6
- Heat shock 70 kDa protein 4
Sequence:
MRALWVLGLCCVLLTFGSVRADDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVLDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEEETAKESTAEKDEL
Protein: Double C2-like domain-containing protein alpha (Doc2-alpha) (P70611)
Organism: Rattus norvegicus (Rat)
Function: Calcium sensor which most probably regulates fusion of vesicles with membranes. Binds calcium and phospholipids. May be involved in calcium dependent neurotransmitter release through the interaction with UNC13A. May be involved in calcium-dependent spontaneous release of neurotransmitter in absence of action potentials in neuronal cells. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Lysosome {ECO:0000269|PubMed:18354201}.
Interaction partners:
- Protein unc-13 homolog A
- Myeloid leukemia factor 2
- Ras-related protein Rab-27A
- Protein unc-13 homolog B
- Secretagogin
Sequence:
MRGRRGDRMTINIQEHMAINVCPGPIRPIRQISDYFPRRGPGPEGGGGGRGFGEAPAHLAPLALAPPAALLGATTPDDGAEVDSYDSDDTTALGTLEFDLLYDQASCMLHCRILRAKGLKPMDFNGLADPYVKLHLLPGACKANKLKTKTQRNTLNPVWNEELTYSGITDDDITHKVLRISVCDEDKLSHNEFIGEIRVPLRRLKPSQKKHFNICLERQVPLPSPSSMSAALRGISCYLKELEQAEQGPGLLEERGRILLSLSYSSRRHGLLVGIVRCAHLAAMDVNGYSDPYVKTYLRPDVDKKSKHKTCVKKKTLNPEFNEEFFYEMELSTLATKTLEVTVWDYDIGKSNDFIGGVSLGPGARGEAQKHWRDCLHQPDTAVERWHTLTSELPPAAGALPLA
Protein: Plant invertase/pectin methylesterase inhibitor superfamily protein (Ripening-related protein-like) (Q9LVA4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cell wall / vacuolar inhibitor of fructosidase 2
- Cell wall / vacuolar inhibitor of fructosidase 1
Sequence:
MAKQYLFVLLSISYLLSLELTAATAASQTGASKKAINFIQSSCKTTTYPALCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKLCGSAKDQDQFAYHMSNAQTWTSAALTDENTCSDGFSGRVMDGRIKNSVRARIMNVGHETSNALSLINAFAKTY