wanglab/gogpt-training-data huggingface dataset:
Protein: Plasma protease C1 inhibitor (C1 Inh) (C1Inh) (C1 esterase inhibitor) (C1-inhibiting factor) (Serpin G1) (Q6P734)
Organism: Rattus norvegicus (Rat)
Function: Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Complement C1r subcomponent
- Complement C1s subcomponent
- Mannan-binding lectin serine protease 2
- Mannan-binding lectin serine protease 1
- Complement C1q subcomponent subunit B
- Mannose-binding protein A
- Mannose-binding protein C
- Complement C1q subcomponent subunit A
- Complement factor B
- Plasma kallikrein
Sequence:
MASKLTPLTLLLLLLAGDRAFSDSEVTSHSSQDPLVVQEGSRDSVPERDGSRSPIEHTGQSSTWPTTSGSTKISNDTMDQVANESFIQHVQPAAQLPEDSPSQSPVNSSSPPSTASAPPTQAPTEPLCPEPLAWCSDSDRDSSEATLSEALTDFSVKLYHAFSATKKAETNMAFSPFSIASLLTQVLLGAGDSTKSNLEDILSYPKDFACVHQTLKAFSSKGVTSVSQIFHSPDLAIRDTYVNASLSLYGSSPRVLGPDGDANLKLINTWVAENTNHKINELLDSLPSDTRLVLLNAVYLSAKWKKTFEQKKMMASFLYKNSMIKVPMLSSKKYPLALFNDQTLKAKVGQLQLSHNLSFVIMVPQSPTHQLEDMEKALNPTVFKAILKKLELSKFQPTYVMMPRIKVKSSQDMLSIMEKLEFFDFTYDLNLCGLTEDPDLQVSSMKHETVLELTETGVEAAAASTISVARNLLIFEVQQPFLFLLWDQRHKFPVFMGRVYDPRA
Protein: Dynein light intermediate chain (Q9VZ20)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU366047}.
Interaction partners:
- Dynein heavy chain
- Dynein light chain Tctex-type
- Protein bicaudal D
- Cytoplasmic dynein 1 intermediate chain
- Dynein heavy chain, cytoplasmic
- Dynein light chain roadblock
- Dynactin subunit 2
- GH16657p
- FI21737p1
- Sperm-specific dynein intermediate chain 1, isoform A
Sequence:
MAMNSGTQTNALTSSFTMKKKDAAAEKENLWSAILNEVQTQGSTKLPSNKSVLVLGDNATGKTTLIAKLQGVEDPKKGSGLEYAYIDVKDEYRDDMTRLGVWVLDGDPGHTNLLHYALNETNYAHTLVILTVSMTQPWGWLEQLNHWIKVLGQHIDSLQLDAKEKEAARQRLTTTWQSYCEVGDDLDPGSPVKRTMRNNSIDEDDLLPLTEDALITNLGLDIVVVVTKTDYMTTLEKEYEYRDEHFDFIQQWIRNFCLRHGTSLFYTSVKEDKNCDVLYKYLTHRIYGLPFRTPALVVEKDAVLIPAGWDSLKKISILYENMHGVKAENPYTDIIKSPPTRKAVSNREAEVQTEDEQAFLARQQEILKQGDQVRGESPLRSQGVGSNKSGPRTPGTTGQSSPKKIDPKLTPATPGAEGVLANFFNSLLHKKSGSPGTGGPGGAGNPAGPGRTANGTDAVMTPEKLAVRTDAAAELDRLSRSVKKEIDMSQSEC
Protein: Complement C4 [Cleaved into: Complement C4 beta chain; Complement C4 alpha chain; C4a anaphylatoxin; Complement C4 gamma chain] (P08649)
Organism: Rattus norvegicus (Rat)
Function: Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0C0L4}. Synapse {ECO:0000250|UniProtKB:P0C0L4}. Cell projection, axon {ECO:0000250|UniProtKB:P0C0L4}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0C0L4}.
Interaction partners:
- Membrane cofactor protein
- Complement C1s subcomponent
- Complement C1r subcomponent
- Mannan-binding lectin serine protease 2
- C4b-binding protein alpha chain
- Mannan-binding lectin serine protease 1
- Complement C1q subcomponent subunit A
- Mannose-binding protein A
- Mannose-binding protein C
- Complement C4A.
Sequence:
MRLLWGLAWAFSFFASSLQKPRLLLFSPSVVNLGTPLSVGVQLLDAPAGQEVKGSVYLRNPTSGPCSPKKDFKLSSGNDFVLLRLEVPLKDVRSCGLFGLRRAPHIQLVAHSPWLKNTASKATETQGVNLLFSSRRGHIFVQTDQPIYNPGQRVRYRVFALDQKMRPSTDTLTVTVENSHGLRVRKKEVFAPTSIFQDDFIIPDISEPGTWKISARFSDGLESNRSTHFEVKKYVLPNFEVKLTPWKPYILTVPSYREEIQLDVQARYVYGKPVQGVAYTRFALMDEQGKKSFLRGLETQTKLVEGQTHISISRDQFQAALGKVNTEIGDLEGLRLYAAVAVIESPGGEMEEAELTSWPFVSSAFSLDLSHTKQHLVPGAPFLLQALVREMSGSEASDVPVKVSATLLSGSDSKVLDFQQNTNGIGQVSFSIHVPPTITELRLLVSAGSLYPAVAKLTVQAPPSRGPGFLSIEPLDLRSPRVGDTFVLSLRTVGIPMPTFSHYYYMIISRGQIMAMSREPRRALTSISVLVDHHLAPSFYFVAYFYHQGLPVANSLLINVQPGDCEGKLELKVDGAKEYRNGDSMKLQLQTDSEALVALGAVDTALYAVGGRSHKPLDMSKVFEVMNSYNLGCGPGGGDDALQVFQTAGLAFSDGDRLTQTKENLSCPKEKKSRQKRNVNFQKAISEKLGQYSSPDTKRCCQDGMTKLPMARTCEQRAARVPQPACREPFLSCCKFAEDLRRNQTRSQAGLARAQDMLQEEDLIDEDDILVRSFFPENWLWRVEPVDRSKLLTVWLPDSLTTWEIHGVSLSKSKGLCVAKPTRVRVFREFHLHLRLPISVRRFEQLELRPVLYNYLSEDVTVSVHVSPVEGLCLAGGGLLAQQVSVPAGSARPVAFSVVPTAAASIPLKVVARGSFTIGDAVSKILQIEKEGAIHREEIVYNLDPLNNLGRSLEIPGSSDPNVIPDGDFSSFVRVTASEPLETLGSEGALSPGGVASLLRLPRGCAEQTMIYLAPTLTASHYLDRTEQWSKLPPETKDHAVDLIQKGHMRIQQFRKKDGSFGAWLHRDSSTWLTAFVLKILSLAQEQIGDSPEKLQETAGWLLGQQLDDGSFHDPCPVIHRGMQGGLVGTDETVALTAFVVIALHHGLAVFQDENSQQLKKRVEASITKANSFLGQKASAGLLGAHASAITAYALTLTKASEDLQNVAHNSLMAMAEETGENLYWGSAIGSQDNVVSSTPAPRNPSEPVPQAPALWIETTAYGLLHLLLREGKGEMADKVATWLTHQGSFQGGFRSTQDTVVTLDALSAYWIASHTTEEKALNVTLSSMGRNGYKSHLLQLNNHQVKGLEEELKFSLGSTINVKVGGNSKGTLKILRTYNVLDMKNTTCQDLRIEVTVTGYVEYTREANEDYEYDYDMPAADDPSVHSQPVTPLQLFEGRRSRRRREAPKAADEQESRVQYTVCIWRNGNLGLSGMAIADITLLSGFQALRADLEKLTSLSDRYVSHFETDGPHVLLYFDSVPTTRECVGFGALQEVAVGLVQPASAVLYDYYSPDHKCSVFYAAPTKSKLLSTLCSADVCQCAEGKCPRQRRSLERGVEDKDGYRMKFACYYPRVEYGFQVKVLREDSRAAFRLFETKITQVLHFTKDAKASIGQTRNFLVRASCRLRLEPSKEYLIMGMDGVTSDLKGDPQYLLDSNTWIEEMPSERLCRSTRQRAACGQLNDFLQEYSSQGCQV
Protein: Serine/threonine-protein kinase SAPK2 (EC 2.7.11.1) (Osmotic stress/abscisic acid-activated protein kinase 2) (stress-activated protein kinase 2) (OsSAPK2) (Q0D4J7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May play a role in signal transduction of hyperosmotic response (Probable). Can phosphorylate BZIP46 in vitro. Together with ABI5, PP2C30 and PYL5, is part of an abscisic acid (ABA) signaling unit that modulates seed germination and early seedling growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22071266}. Nucleus {ECO:0000269|PubMed:22071266, ECO:0000269|PubMed:28000033}.
Interaction partners:
- Probable protein phosphatase 2C 30
- bZIP transcription factor 23
- Probable protein phosphatase 2C 6
- bZIP transcription factor ABI5 homolog
- Probable protein phosphatase 2C 68
- Probable protein phosphatase 2C 8
- bZIP transcription factor TRAB1
- protein-serine/threonine phosphatase
- Probable protein phosphatase 2C 37
- protein-serine/threonine phosphatase
Sequence:
MERYEVIKDIGSGNFGVAKLVRDVRTKELFAVKFIERGQKIDENVQREIMNHRSLRHPNIVRFKEVVLTPTHLAIVMEYAAGGELFERICSAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSIAPRLKICDFGYSKSSLLHSQPKSTVGTPAYIAPEVLARKEYDGKVADVWSCGVTLYVMLVGAYPFEDPDEPRNFRKTITRILSVQYMVPDYVRVSMECRHLLSRIFVANPEQRITIPEIKNHPWFLKNLPIEMTDEYQMSVQMNDINTPSQGLEEIMAIIQEARKPGDGSKFSGQIPGLGSMELDDVDTDDIDVEDSGDFVCAL
Protein: Asporin (Periodontal ligament-associated protein 1) (PLAP-1) (Q99MQ4)
Organism: Mus musculus (Mouse)
Function: Binds calcium and plays a role in osteoblast-driven collagen biomineralization activity (By similarity). Critical regulator of TGF-beta in articular cartilage and plays an essential role in cartilage homeostasis and osteoarthritis (OA) pathogenesis. Negatively regulates chondrogenesis in the articular cartilage by blocking the TGF-beta/receptor interaction on the cell surface and inhibiting the canonical TGF-beta/Smad signal. Negatively regulates periodontal ligament (PDL) differentiation and mineralization to ensure that the PDL is not ossified and to maintain homeostasis of the tooth-supporting system. Inhibits BMP2-induced cytodifferentiation of PDL cells by preventing its binding to BMPR1B/BMP type-1B receptor, resulting in inhibition of BMP-dependent activation of SMAD proteins. Inhibits the interaction between TGFB1 and TGF-beta receptor type II in the presence of heparin/heparan sulfate in vitro.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Periostin
- Transforming growth factor beta-1 proprotein
- Mimecan
- Collagen alpha-1
- Osteomodulin
- Collagen alpha-2
- Lumican
Sequence:
MKEYVMLLLLAVCSAKPFFSPSHTALKNMMLKDMEDTDDDDNDDDDNSLFPTKEPVNPFFPFDLFPTCPFGCQCYSRVVHCSDLGLTSVPNNIPFDTRMVDLQNNKIKEIKENDFKGLTSLYALILNNNKLTKIHPKTFLTTKKLRRLYLSHNQLSEIPLNLPKSLAELRIHDNKVKKIQKDTFKGMNALHVLEMSANPLENNGIEPGAFEGVTVFHIRIAEAKLTSIPKGLPPTLLELHLDFNKISTVELEDLKRYRELQRLGLGNNRITDIENGTFANIPRVREIHLEHNKLKKIPSGLQELKYLQIIFLHYNSIAKVGVNDFCPTVPKMKKSLYSAISLFNNPMKYWEIQPATFRCVLGRMSVQLGNVGK
Protein: SH2 domain-containing protein 1B2 (EAT-2-related transducer) (ERT) (EAT-2B) (Q45HK4)
Organism: Mus musculus (Mouse)
Function: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family. In SLAM signaling may cooperate with Sh2d1a/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction through Cd244/2b4. However, conflicting results are reported which may reflect the use of different strain backgrounds. Proposed to act as an inhibitor of Cd244-mediated NK cell function including cytotoxicity and IFN-gamma production, the latter found also by triggering Klra4 and Klrk1 next to Cd244. Seems to positively regulate Cd244- and Cd84-dependent NK cell functions implicating Cd244-mediated phosphorylation of Vav1.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Natural killer cell receptor 2B4
- SH2 domain-containing protein 1B
- Signaling lymphocytic activation molecule
- SLAM family member 5
Sequence:
MDLPYYHGCLTKRECEALLLKGGVDGNFLIRDSESVPGALCLCVSFKKLVYNYRIFREKNGYYRIETEPSTPKTIFPNLEELISKFKTPGQGMVVHLSNPIMRSGFCPGARRLNLEANVYENTDEEYVDVLP
Protein: Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184) (G5EGA6)
Organism: Caenorhabditis elegans
Function: Catalyzes the reduction of isatin, 4-oxonon-2-enal, 9,10-phenanthrenequinone, menadione, 2,3-hexaenadione, 3,4-hexanedione and 2,3-heptanedione.
Interaction partners:
- Alcohol dehydrogenase class-3
- Alcohol dehydrogenase 1
- Alcohol dehydrogenase 2
- alcohol dehydrogenase
- Probable aldehyde oxidase gad-3
- DeHydrogenases, Short chain
- O-acyltransferase
- PNPLA domain-containing protein
- Fatty acid synthase
- Beta,beta-carotene 9',10'-oxygenase
Sequence:
MPSNCRRFEGKVAIVTAATKGIGLAIAERLLDEGASVVIGSRNQKNVDEAIEYLKNKGLTKVAGIAGHIASTDDQKKLVDFTLQKFGKINILVNNHGINPAFGHILEVSDQVWDKLFEVNVKAGFQMTKLVHPHIAKEGGGAIIFNASYSAYKSPPGIAAYGVTKTTLVGLTRALAMGLAKDNIRVNGIAPGVIKTKMSQVLWDGGEDAEKELTDIQEIALGRLGVPDDCAGTVAYLASDDSSYITGEMIIIAGGVQARL
Protein: Protein hugin [Cleaved into: Hug-gamma; Hug-peptide; PK-2 (Drm-PK-2) (Myotrophin-2) (Drm-MT2) (MT-2) (Pyrokinin-2)] (Q9VG55)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probably has a role in larval molting.
Subcellular location: Secreted {ECO:0000269|PubMed:12204246}.
Interaction partners:
- Pyrokinin 2 receptor 2, isoform A
- Pyrokinin 2 receptor 1
- Cardio acceleratory peptide 2b
- Allatostatins MIP
- Diuretic hormone 44, isoform A
- Neuropeptide F
- Leucokinin
- Pyrokinin-1 receptor
- Short neuropeptide F
- Drosulfakinins
Sequence:
MCGPSYCTLLLIAASCYILVCSHAKSLQGTSKLDLGNHISAGSARGSLSPASPALSEARQKRAMGDYKELTDIIDELEENSLAQKASATMQVAAMPPQGQEFDLDTMPPLTYYLLLQKLRQLQSNGEPAYRVRTPRLGRSIDSWRLLDAEGATGMAGGEEAIGGQFMQRMVKKSVPFKPRLGKRAQVCGGD
Protein: DNA N-6-adenine-methyltransferase (DAM) (EC 2.1.1.72) (ORF13) (Orphan methyltransferase M.HinHP1Dam) (M.HinHP1Dam) (P51715)
Organism: Haemophilus phage HP1 (strain HP1c1) (Bacteriophage HP1)
Function: Methyltransferase that methylates adenine residues in the ssDNA and dsDNA sequence 5'-GATC-3'. May prevent degradation of viral DNA by the host restriction-modification antiviral defense system (Probable).
Interaction partners:
Sequence:
MMTKSNTKKSDKDLWATPWWVFHYAEQYFNIKFDLDTCAMEHNTKVKNFITPEQNTLTADWQGRYCWMNPPYSNPLPFVLRAISQSVLHNKTVVMLLNVDGSTKWFDMCVRNAKEIVYITNSRIPFINNETGEETDQNNKPQMLVLFEPKAPYGSLKSSYVSLHEMKEKGMLQ
Protein: Basic/leucine zipper protein (Q08418)
Organism: Oryza sativa (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSPSRRSSSPESNTSGGGGGADERKRKRMLSNRESARRSRARKQQRLEELIAEAARLQAENARVEAQIGAYAGELSKVDGENAVLRARHGELAGRLQALGSVLEILQVAGAPVDIPEIPDDPLLRPWQPPFAAQPIVATAMADAFQF
Protein: Tetraspanin-6 (Q9C7C1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the regulation of cell differentiation.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- MLO-like protein 8
- MLO-like protein 10
- Eukaryotic translation initiation factor 3 subunit L
- Protein HIGH ARSENIC CONTENT 1, mitochondrial
- Pheophorbide a oxygenase, chloroplastic
Sequence:
MYRFSNTVIGVLNLLTLLASIPIIGTALYKARSSTTCENFLQTPLLVIGFIILIVSLAGFIGACFNVAWALWVYLVVMIFLIATLMGLTLFGLVVTSQGGGVEVPGRIYKEYRLGDYHPWLRERVRDPEYWNSIRSCILSSKTCTKIESWTTLDYFQRDMTSVQSGCCKPPTACTYEAGVVDGGGDCFRWNNGVEMLCYECDACKAGVLEEIRLDWRKLSVVNILVLVLLIAVYAAGCCAFHNTRHAAHPYHPSDDNRMTRVRPRWDYYWWRWWHEKKEQLY
Protein: Stress-associated endoplasmic reticulum protein 1 (Ribosome-attached membrane protein 4) (Q9Y6X1)
Organism: Homo sapiens (Human)
Function: Interacts with target proteins during their translocation into the lumen of the endoplasmic reticulum. Protects unfolded target proteins against degradation during ER stress. May facilitate glycosylation of target proteins after termination of ER stress. May modulate the use of N-glycosylation sites on target proteins (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9R2C1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R2C1}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9R2C1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R2C1}.
Interaction partners:
- X-box-binding protein 1
- Guided entry of tail-anchored proteins factor 1
- Protein transport protein Sec61 subunit beta
- ATPase GET3
- Small glutamine-rich tetratricopeptide repeat-containing protein alpha
Sequence:
MVAKQRIRMANEKHSKNITQRGNVAKTSRNAPEEKASVGPWLLALFIFVVCGSAIFQIIQSIRMGM
Protein: At2g01870 (Expressed protein) (Transmembrane protein) (Q9SIS7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable NAD
Sequence:
MVVVLGLQSLKWYTHGRIMETKKKRHLMRIVQATEREDSFQIDRDKAREALKQLDQQIESQADEKPRIINKTSSDVVRTNNDPIMFEEPPEISGSFLTSSAFVLLALTLFYNILFITVIKPSMDGPESVPEENSVAMSDSDIVKFPLSSLPENTFKQ
Protein: GATOR2 complex protein MIOS (Missing oocyte meiosis regulator homolog) (Q9NXC5)
Organism: Homo sapiens (Human)
Function: As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:28199306}.
Interaction partners:
- GATOR2 complex protein WDR59
- GATOR1 complex protein NPRL3
- Protein SEC13 homolog
- GATOR2 complex protein WDR24
- GATOR1 complex protein NPRL2
- Nucleoporin SEH1
- GATOR1 complex protein DEPDC5
- KICSTOR complex protein kaptin
- Ras-related GTP-binding protein A
- Ras-related GTP-binding protein C
Sequence:
MSGTKPDILWAPHHVDRFVVCDSELSLYHVESTVNSELKAGSLRLSEDSAATLLSINSDTPYMKCVAWYLNYDPECLLAVGQANGRVVLTSLGQDHNSKFKDLIGKEFVPKHARQCNTLAWNPLDSNWLAAGLDKHRADFSVLIWDICSKYTPDIVPMEKVKLSAGETETTLLVTKPLYELGQNDACLSLCWLPRDQKLLLAGMHRNLAIFDLRNTSQKMFVNTKAVQGVTVDPYFHDRVASFYEGQVAIWDLRKFEKPVLTLTEQPKPLTKVAWCPTRTGLLATLTRDSNIIRLYDMQHTPTPIGDETEPTIIERSVQPCDNYIASFAWHPTSQNRMIVVTPNRTMSDFTVFERISLAWSPITSLMWACGRHLYECTEEENDNSLEKDIATKMRLRALSRYGLDTEQVWRNHILAGNEDPQLKSLWYTLHFMKQYTEDMDQKSPGNKGSLVYAGIKSIVKSSLGMVESSRHNWSGLDKQSDIQNLNEERILALQLCGWIKKGTDVDVGPFLNSLVQEGEWERAAAVALFNLDIRRAIQILNEGASSEKGDLNLNVVAMALSGYTDEKNSLWREMCSTLRLQLNNPYLCVMFAFLTSETGSYDGVLYENKVAVRDRVAFACKFLSDTQLNRYIEKLTNEMKEAGNLEGILLTGLTKDGVDLMESYVDRTGDVQTASYCMLQGSPLDVLKDERVQYWIENYRNLLDAWRFWHKRAEFDIHRSKLDPSSKPLAQVFVSCNFCGKSISYSCSAVPHQGRGFSQYGVSGSPTKSKVTSCPGCRKPLPRCALCLINMGTPVSSCPGGTKSDEKVDLSKDKKLAQFNNWFTWCHNCRHGGHAGHMLSWFRDHAECPVSACTCKCMQLDTTGNLVPAETVQP
Protein: Glutamate-rich protein 4 (A6NGS2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MELWRQLNQAGLVPPGLGPPPQALREVSPVEIPGQTLRTAGADTGGACDSLLWIREELGNLRRVDVQLLGQLCSLGLEMGALREELVTILEEEEESSKEEEEDQEPQRKQEEEHLEACPAPHPPDFEMMI
Protein: G-protein coupled receptor 143 (Ocular albinism type 1 protein) (P51810)
Organism: Homo sapiens (Human)
Function: Receptor for tyrosine, L-DOPA and dopamine. After binding to L-DOPA, stimulates Ca(2+) influx into the cytoplasm, increases secretion of the neurotrophic factor SERPINF1 and relocalizes beta arrestin at the plasma membrane; this ligand-dependent signaling occurs through a G(q)-mediated pathway in melanocytic cells. Its activity is mediated by G proteins which activate the phosphoinositide signaling pathway. Also plays a role as an intracellular G protein-coupled receptor involved in melanosome biogenesis, organization and transport.
Subcellular location: Melanosome membrane {ECO:0000269|PubMed:10471510, ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:16524428, ECO:0000269|PubMed:16621890, ECO:0000269|PubMed:17081065}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:16524428, ECO:0000269|PubMed:16621890}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:18828673}; Multi-pass membrane protein {ECO:0000255}. Note=Distributed throughout the endo-melanosomal system but most of endogenous protein is localized in unpigmented stage II melanosomes. Its expression on the apical cell membrane is sensitive to tyrosine (PubMed:18828673). {ECO:0000269|PubMed:18828673}.
Interaction partners:
- Melanoma antigen recognized by T-cells 1
- FERM domain-containing protein 7
- Tyrosinase
- Argininosuccinate synthase
- Protein Shroom2
- P protein
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase [NADP
- Melanocyte protein PMEL
Sequence:
MASPRLGTFCCPTRDAATQLVLSFQPRAFHALCLGSGGLRLALGLLQLLPGRRPAGPGSPATSPPASVRILRAAAACDLLGCLGMVIRSTVWLGFPNFVDSVSDMNHTEIWPAAFCVGSAMWIQLLYSACFWWLFCYAVDAYLVIRRSAGLSTILLYHIMAWGLATLLCVEGAAMLYYPSVSRCERGLDHAIPHYVTMYLPLLLVLVANPILFQKTVTAVASLLKGRQGIYTENERRMGAVIKIRFFKIMLVLIICWLSNIINESLLFYLEMQTDINGGSLKPVRTAAKTTWFIMGILNPAQGFLLSLAFYGWTGCSLGFQSPRKEIQWESLTTSAAEGAHPSPLMPHENPASGKVSQVGGQTSDEALSMLSEGSDASTIEIHTASESCNKNEGDPALPTHGDL
Protein: Mediator of RNA polymerase II transcription subunit 7b (Q9LZD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 10a
- Mediator of RNA polymerase II transcription subunit 10b
- Mediator of RNA polymerase II transcription subunit 22a
- Mediator of RNA polymerase II transcription subunit 22b
Sequence:
MATATYPPPPPYYRLYKDFSENTDSAPEPPPPIEGTYVCFGGNYTTEDVLPSLEEQGVPQLYPKDSNLDYKKELRSLNRELQLHILELADVLVDRPSQYAKRIGEISSIFKNLHHLLNSLRPHQARATLIHIMELQIQQRKQAVEDIKRRREEAQGLLKDAFVTLDGQ
Protein: N-acetyltransferase, putative (Q38FJ2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNRAARIIPPHRYRTADGEQFTIRHIRNRTAYNSEWVEVRERLVSGASLLPQVLDVASDSSLSVIFIAVGSEESAETGIMGYVVVNMSFIASKTVSVAWISVLNRFRGRHVGRSLLHHVDSFCRANMINHIEAMRTDGLTNLFKKCGFRLSASPVIFKSKAQRKDVQLPSQPQVPYCITSGAVTLRCTTAEDRKGWSLCILEACSYLSGCTELVVNAFSADFRVSAVNSETKRIIGIVSIDSTGWIPLIACLQEYRGQGLGSFMMFIAMEWLRRQGGSEVTLSPLNASVVNFYKRWSFVVDKKSAGKRKRCDDGIPILVRRLSEGERFLPDGYELEDFVHFASSKQNDTLRVAGSG
Protein: Adenylate kinase 2, mitochondrial (AK 2) (EC 2.7.4.3) (ATP-AMP transphosphorylase 2) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) [Cleaved into: Adenylate kinase 2, mitochondrial, N-terminally processed] (P54819)
Organism: Homo sapiens (Human)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis.
Subcellular location: Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03168}.
Interaction partners:
- Adenosine kinase
- Adenine phosphoribosyltransferase
- Adenylosuccinate lyase
- Pyruvate kinase PKM
- Cancer-related nucleoside-triphosphatase
- Pyruvate kinase PKLR
- Deoxycytidine kinase
- Nucleoside diphosphate kinase, mitochondrial
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Thiamine pyrophosphokinase 1
Sequence:
MAPSVPAAEPEYPKGIRAVLLGPPGAGKGTQAPRLAENFCVCHLATGDMLRAMVASGSELGKKLKATMDAGKLVSDEMVVELIEKNLETPLCKNGFLLDGFPRTVRQAEMLDDLMEKRKEKLDSVIEFSIPDSLLIRRITGRLIHPKSGRSYHEEFNPPKEPMKDDITGEPLIRRSDDNEKALKIRLQAYHTQTTPLIEYYRKRGIHSAIDASQTPDVVFASILAAFSKATCKDLVMFI
Protein: LIM domain only 4a (LIM domain transcription factor LMO4a isoform X2) (A0A2R8RLI6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MVNSRVESSAVAVTGGSGGAVRSCAGCGGRISDRFLLFSMDRYWHTRCLKCSCCQAQLGEIGSTCFSKGGMILCRNDYIRLFGHSGACSACGQSIPASEMVMRAQGNVYHLKCFTCATCRNRLVPGDRFHYVNGTIFCEHDRPGGALLSSHLTPLQSNTLLPDQKV
Protein: Protein phosphatase inhibitor 2 (IPP-2) (Q9DCL8)
Organism: Mus musculus (Mouse)
Function: Inhibitor of protein-phosphatase 1.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Sequence:
MAASTASHRPIKGILKNKTSAASPPVVPSAEQPRPIVEEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPNTPYHNMIGDDEDAYSDSEGNEVMTPDILAKKLAAAEGSEPKYRTREQESSGEEDNDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDDEDEEMAETADGDSMNVEESSQGSTTSDHLQHKSQSS
Protein: Metal tolerance protein C2 (AtMTPc2) (AtMTP5) (Q6ICY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in sequestration of excess metal in the cytoplasm into vacuoles to maintain metal homeostasis.
Subcellular location: Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Tonoplast.
Interaction partners:
- Metal tolerance protein C4
- Metal tolerance protein C1
- Metal tolerance protein 12
- Metal tolerance protein 11
- Metal tolerance protein 9
- Metal tolerance protein 10
- Putative metal tolerance protein C3
- IAA-alanine resistance protein 1
- Protein PLANT CADMIUM RESISTANCE 6
Sequence:
MERSISFNPRGDNELPDDRSSDVGYAANDRRLAYSRSFQQSHGPRTPAVTEAAKPFLDRTVSSIDMPPDIYSVDGSDVFFGEGKDVDMAKVSVLEMVWEVFGVVTSGNRQMKRLFLLIALNVLYSTTELSIGIFTGRVGLVSDAFHLTFGCGLLTFSLFAMATSRKKPDHAYSYGYKRLEVLSAFTNALFLMFMSFSLAVEALHAFIQDESEHKHYLIVSAVTNLLVNLLGVWFFRNYARVNIAYRKAEDMNYHSVCLHVISDSIRSAGLILASWLLSLGVENAEVLCLGLVSVTVFMLVMPLFKATGGVLLQMAPPNIPSSALSKCLRQITSREDVTEVLQARFWEVVPGHTVGSLRLQVKSGIDERPLLQYVYDVYHDLGVQDLTLQTDYT