wanglab/gogpt-training-data huggingface dataset:
Protein: NADP-reducing hydrogenase subunit HndD (EC 1.12.1.3) (Hydrogen dehydrogenase (NADP(+))) (Q46508)
Organism: Solidesulfovibrio fructosivorans (Desulfovibrio fructosivorans)
Function: Catalyzes the reduction of NADP in the presence of molecular H(2) to yield NADPH.
Interaction partners:
Sequence:
MSMLTITIDGKTTSVPEGSTILDAAKTLDIDIPTLCYLNLEALSINNKAASCRVCVVEVEGRRNLAPSCATPVTDNMVVKTNSLRVLNARRTVLELLLSDHPKDCLVCAKSGECELQTLAERFGIRESPYDGGEMSHYRKDISASIIRDMDKCIMCRRCETMCNTVQTCGVLSGVNRGFTAVVAPAFEMNLADTVCTNCGQCVAVCPTGALVEHEYIWEVVEALANPDKVVIVQTAPAVRAALGEDLGVAPGTSVTGKMAAALRRLGFDHVFDTDFAADLTIMEEGSEFLDRLGKHLAGDTNVKLPILTSCCPGWVKFFEHQFPDMLDVPSTAKSPQQMFGAIAKTYYADLLGIPREKLVVVSVMPCLAKKYECARPEFSVNGNPDVDIVITTRELAKLVKRMNIDFAGLPDEDFDAPLGASTGAAPIFGVTGGVIEAALRTAYELATGETLKKVDFEDVRGMDGVKKAKVKVGDNELVIGVAHGLGNARELLKPCGAGETFHAIEVMACPGGCIGGGGQPYHHGDVELLKKRTQVLYAEDAGKPLRKSHENPYIIELYEKFLGKPLSERSHQLLHTHYFKRQRL
Protein: Apelin receptor early endogenous ligand (Protein Elabela) (ELA) (Protein Toddler) (P0DP76)
Organism: Rattus norvegicus (Rat)
Function: Endogenous ligand for the apelin receptor (APLNR). Hormone required for mesendodermal differentiation, blood vessels formation and heart morphogenesis during early development and for adult cardiovascular homeostasis. Drives internalization of APLNR. Acts as a motogen by promoting mesendodermal cell migration during gastrulation by binding and activating APLNR. Acts as an early embryonic regulator of cellular movement with a role in migration and development of cardiac progenitor cells. May act as a chemoattractant for the activation of angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis. Positively regulates sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel sprouting. Plays a role in placental vascular development; promotes placental trophoblast invasion and spiral artery remodeling in the uterus (By similarity). Involved in the regulation of maternal cardiovascular homeostasis to prevent gestational hypertension and for potent cardioprotective functions during heart failure. Mediates myocardial contractility in an ERK1/2-dependent manner.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0DMC4}. Secreted, extracellular space {ECO:0000250|UniProtKB:P0DMC4}. Note=Found in blood plasma. Found in serum of pregnant mice, peaking at midgestation; indicating a maternal and zygotic origin of circulating APELA during pregnancy. {ECO:0000250|UniProtKB:P0DMC3, ECO:0000250|UniProtKB:P0DMC4}.
Interaction partners:
Sequence:
MRFQPLFWVFFIFAMSLLFITEEKSVNFPRRRKLYRHNCFRRRCISLHSRVPFP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q587H5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Serine/threonine-protein phosphatase
Sequence:
MPFAANVVQNTNDHSHTGDKGNEGDIVKVGEGVSLQSSTLDIVKSVGEGSAAGEAPGTSFRTIAAGAMGSRAKGAWEVTSTSGKPTTSSEKGDTAGFAESPGNNPNFLRSPLQRVLVPKTSSRGTNRLDGRNPLGEGAVRKDGDKSSGSCVKPSVNGDNKCDTIGSLARRAPPGLTMGRSELGSARDEWPVQSPRGVWPHPALSGKSSPNFYGSPVNTSTRAPFFSPLPAAALPPSNTVPGTLKRQLYNVDTANEEMMMPNNSFASTIVTSGSRCDNRDPAFSDCGEAGIFTPKRVGRDSRSATPTRWYNTSFHGNYAGGPMRRTSTAERGKLSAANEQNGERREVQSATVSPGLGPTTVEVYDTSISSRTGNAIKEQRSLSPNVQPACFYPINWSSCPSRDNDDSNAGDRISVPGAVLVPVDSDATNRDPQEGAPTNSCQLHNHCLNRTDSEWWFKDPTIFLLNVNLIKLLELREEMERLNEQRSVDRPHSAYERRGREASLHSSHSIMLAGMLEKLESIQFQIAYSILDIKNVLLKHHFAKWSNTGVRDCVSNVVSAWDAHGPASKEFKEASYILLDLVSAEERGSITYTNVHRMWNALGTSRTASCAATAFCFVSLLCFVVVAAAGTLPGWVCAAVASIGALLMVSVVTITSVQLHYSSVSARVWGFSHNEMLKRVEAVQQNLYDGGEGATGVPVGYSDLVAVQKAPGSSSTCFQLGKTSSQGHMLPQQDAPRDDCARDCGPLSSRNSFYSRSQLRIPNDTTGILRKVPSMSNVKCSSGASNGAISSGRSEKQAGSLRDSSPCLRRADRQENDWWNQPAGGRWNDDSFNRCSPMERVPVGHADNPLVAGGSGREWQEALSEQKRECDTAVRKQIGRRQSVDGDRAAANVLAVPSEFNHGEERPRQFRGAQRPQSRGVDSEVERMLRDAASKAALNSAYVAPMNIFSDEASPGSSLLLTSATGMQGNLLGTGSDGLPITAFVYCLDDVVASTLLANLWNRSIYVMQRSGLEDIDMTYKSCAVQTKVILVHAPDVDGAHLDVVLSWMKGGERLVFFFASSSEFIPSCIPKASQLVLPLTSHDIGRLFSSSLTDEMASKSLFGLSRNLQIPSYTLGRRLGGGAFGAVFEATMDDLNGRCAVKVMCLRGNKRDNGARNNGKGVRMPEVVREIEVMRMLNHPNLVRYLFCNWDGKCVSIFMELCPGGTLSDAITNGDIQGADHIISILRDVINGVVYLHDHHITHRDLKPENILFRDGRAKVSDFGTAVQRDSGLKNTRGTLAYMAPEVLLGEPYGKACDVWSIGCIVAEALGISTNCSNKCAAQDAQHQKQQRPVTDQQFSPTNQGLAELCERYRTMDERETRVFDCDDPTVCDFLQHCLHRNPEKRPSPKELLEHPLLNARCGSAVWEWVESVIARQRAMPLRRRTSTVILTSVAVNKGAGIGRDDDTDGADGMGGGEGGGLHTTYISRVASMSAASLQSISEEGQNSASWGTSFGDQGVV
Protein: Importin subunit alpha-6 (Karyopherin subunit alpha-5) (O15131)
Organism: Homo sapiens (Human)
Function: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates nuclear import of STAT1 homodimers and STAT1/STAT2 heterodimers by recognizing non-classical NLSs of STAT1 and STAT2 through ARM repeats 8-9. Recognizes influenza A virus nucleoprotein through ARM repeat 7-9 In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.
Subcellular location: Cytoplasm.
Interaction partners:
- Importin subunit beta-1
- Nuclear pore complex protein Nup153
- Nuclear pore complex protein Nup50
- Astrotactin-2
- WD repeat-containing and planar cell polarity effector protein fritz homolog
- Mirror-image polydactyly gene 1 protein
- Acidic leucine-rich nuclear phosphoprotein 32 family member B
- Speckle-type POZ protein-like
- Protein hinderin
- TBC1 domain family member 8B
Sequence:
MDAMASPGKDNYRMKSYKNKALNPQEMRRRREEEGIQLRKQKREEQLFKRRNVYLPRNDESMLESPIQDPDISSTVPIPEEEVVTTDMVQMIFSNNADQQLTATQKFRKLLSKEPNPPIDQVIQKPGVVQRFVKFLERNENCTLQFEAAWALTNIASGTFLHTKVVIETGAVPIFIKLLNSEHEDVQEQAVWALGNIAGDNAECRDFVLNCEILPPLLELLTNSNRLTTTRNAVWALSNLCRGKNPPPNFSKVSPCLNVLSRLLFSSDPDVLADVCWALSYLSDGPNDKIQAVIDSGVCRRLVELLMHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALPCLLHLLSSPKESIRKEACWTVSNITAGNRAQIQAVIDANIFPVLIEILQKAEFRTRKEAAWAITNATSGGTPEQIRYLVALGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQESKQNGIGINPYCALIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGVEEDDPSIVPQVDENQQQFIFQQQEAPMDGFQL
Protein: Headcase protein homolog (hHDC) (Q9UBI9)
Organism: Homo sapiens (Human)
Function: May play an important role in some human cancers. May be part of the regulatory mechanism in the development of epithelial tube networks such as the circulatory system and lungs.
Interaction partners:
- E-selectin
- Sorting nexin-20
- P-selectin glycoprotein ligand 1
- Alpha-
- P-selectin
Sequence:
MPNPKNSKGGRKNKRANSSGDEQENGAGALAAAGAAGAAAGGALAAAAGCGAAAAGAPGAGGAAGAGGAGTGAANAAAAAGAAAAGDAKNEAPCATPLICSFGRPVDLEKDDYQKVVCNNEHCPCSTWMHLQCFYEWESSILVQFNCIGRARSWNEKQCRQNMWTKKGYDLAFRFCSCRCGQGHLKKDTDWYQVKRMQDEKKKKSGSEKNTGRPPGEAAEEAKKCRPPNKPQKGPSHDLPRRHSMDRQNSQEKAVGAAAYGARSPGGSPGQSPPTGYSILSPAHFSGPRSSRYLGEFLKNAIHLEPHKKAMAGGHVFRNAHFDYSPAGLAVHRGGHFDTPVQFLRRLDLSELLTHIPRHKLNTFHVRMEDDAQVGQGEDLRKFILAALSASHRNVVNCALCHRALPVFEQFPLVDGTLFLSPSRHDEIEYDVPCHLQGRLMHLYAVCVDCLEGVHKIICIKCKSRWDGSWHQLGTMYTYDILAASPCCQARLNCKHCGKPVIDVRIGMQYFSEYSNVQQCPHCGNLDYHFVKPFSSFKVLEAY
Protein: Protein MSS18 (P08593)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in splicing of intron aI5-beta of the mitochondrial COX1 transcript.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- ATP-dependent RNA helicase SUV3, mitochondrial
- Mitochondrial RNA-splicing protein MRS1
- Intron-encoded DNA endonuclease aI5 beta
- Protein PET54
Sequence:
MGLPEVNFLRKNCILVELKLFYQTVYPPKELYWNNRITAELSTFSNIKYARPTFAVNNGTFQRTRPKLDLVLASSDIRKLATVLFNLKALIMNTKGEEPTLTTMTSVQTNEEKNDNLEQKYSSLLDRWNGKVEVHDSPFLQLQRDSNLLFAERPVRYVSTTEGEGVDISSEEFFRLEEEQCRRNYDVLVDEHSTPSVGMKDGQYGPNIIHFEPSLYHTYSSLPMSMKFWLNGLEDDETTMMNIDEKSAENLDILLHGFKGFSNKRVKG
Protein: EB1 (Microtubule-associated protein RP/EB family member 1b) (Q9W6M6)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Mitotic spindle assembly checkpoint protein MAD2A
- Dynactin subunit 1
- Dynactin subunit 1
- Mitotic checkpoint protein BUB3
Sequence:
MAVNVYSTSVTSDNLSRHDMLAWINESLQMNLTKIELLCSGAAYCQFMDMLFPGCVPLKKVKFSAKLEHEYIHNFKILQAGFKRMGVDKIIPVDKLIKGKFQDNFEFVQWFKKFFDANYDGKDYDPVEARQGQDTMPVPNPVMPALNKPKKILNAAPQRAAVAKVAPKMTPSSARRPGAGGDDERAELIQEVNILKSTIQDMEKERDFYFGKLRNIELICQEKESEGDPTLQRIVDILYATDEGFVIPDAEAEDQEEF
Protein: Small cell adhesion glycoprotein (S4R466)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004361}; Single-pass type III membrane protein {ECO:0000256|ARBA:ARBA00004361}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004497}; Single-pass type III membrane protein {ECO:0000256|ARBA:ARBA00004497}.
Interaction partners:
Sequence:
MTTPILQPTEALSPEDGASTALIAVVITVVFLTLLSVVILIFFYLYKNKGSYVTYEPTEGEPSAIVQMESDLAKGSEKEEYFI
Protein: Transposon Ty1-JR1 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (P47098)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSHYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: DNA-directed RNA polymerase I subunit RPA34 (A34.5) (DNA-directed RNA polymerase I subunit G) (RNA polymerase I-associated factor PAF49) (Q76KJ5)
Organism: Mus musculus (Mouse)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Involved in UBTF-activated transcription, presumably at a step following PIC formation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15226435}. Note=Accumulates in the nucleolus of exponentially growing cells.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
Sequence:
MAGTQACSATRFSCPPHFTEMSPDSEPSRFSLEALTGPDTELWLIQAPADFAPQCLNGRRVPLSGSKTVKGKLDGKKHRYRVFTSSPQAREATLLASSSEAGGRLTCAPAPSGSLRIMEGPQEYLLSRVPLQLIPTSLPPQIPAGLRPRFSAFGGSPPVTGPGSASALRSPTSGKRKSTRKGTDASSDTQEAVNRHGAMEVKTALGNLGVSVKKRKRYFMQEEMEAKTMEPVAELPVPSATSSKKRKKSKGTETSQVEHTEPVAQTEPPEGTFLFPTKKRKRQKEADGTEEVDGIVADSQPQVIVEAQEETILLSPTKKRRKEKRQNLGMEAEMGPPGVLMVTEHSEHGLQAEVALVSPKKTKKKKGKRVGETEAALPDDFEPQGALAPSKKKERGARL
Protein: COP9 signalosome complex subunit 2 (Signalosome subunit 2) (FUSCA protein 12) (FUSCA12) (P68353)
Organism: Brassica oleracea (Wild cabbage)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. It is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes (By similarity).
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
Sequence:
KSAVTRNYSEKKNERLWFKKNYDHAGNQRRIQKWNTQLK
Protein: UPF0603 protein Rv2345 (P9WFJ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May play a role in septum formation.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein Rv2248
- Uncharacterized membrane protein Rv3835
- HTH-type transcriptional regulator Rv0792c
- PPE family protein
- Deoxyguanosinetriphosphate triphosphohydrolase-like protein
- Probable cytochrome c oxidase subunit 1
- Cytochrome bc1 complex cytochrome b subunit
- Cytochrome c oxidase subunit 2
- Cytochrome bc1 complex Rieske iron-sulfur subunit
- Probable cytochrome c oxidase subunit 3
Sequence:
MRLVRLLGMVLTILAAGLLLGPPAGAQPPFRLSNYVTDNAGVLTSSGRTAVTAAVDRLYADRRIRLWVVYVENFSGQSALNWAQRTTRTSELGNYDALLAVATTGREYAFLVPSAMPGVSEGQVDNVRRYQIEPALHDGDYSGAAVAAANGLNRSPSSSSRVVLLVTVGIIVIVVAVLLVVMRHRNRRRRADELAAARRVDPTNVMALAAVPLQALDDLSRSMVVDVDNAVRTSTNELALAIEEFGERRTAPFTQAVNNAKAALSQAFTVRQQLDDNTPETPAQRRELLTRVIVSAAHADRELASQTEAFEKLRDLVINAPARLDLLTQQYVELTTRIGPTQQRLAELHTEFDAAAMTSIAGNVTTATERLAFADRNISAARDLADQAVSGRQAGLVDAVRAAESALGQARALLDAVDSAATDIRHAVASLPAVVADIQTGIKRANQHLQQAQQPQTGRTGDLIAARDAAARALDRARGAADPLTAFDQLTKVDADLDRLLATLAEEQATADRLNRSLEQALFTAESRVRAVSEYIDTRRGSIGPEARTRLAEAKRQLEAAHDRKSSNPTEAIAYANAASTLAAHAQSLANADVQSAQRAYTRRGGNNAGAILGGIIIGDLLSGGTRGGLGGWIPTSFGGSSNAPGSSPDGGFLGGGGRF
Protein: Nuclear factor of activated T-cells, cytoplasmic 1 (NF-ATc1) (NFATc1) (NFAT transcription complex cytosolic component) (NF-ATc) (NFATc) (O88942)
Organism: Mus musculus (Mouse)
Function: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription. Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and programmed death of T-lymphocytes as well as lymphoid and non-lymphoid cells (By similarity). Required for osteoclastogenesis and regulates many genes important for osteoclast differentiation and function.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19626032, ECO:0000269|PubMed:24970700, ECO:0000269|PubMed:28341745, ECO:0000269|PubMed:32741026}. Nucleus {ECO:0000269|PubMed:19626032, ECO:0000269|PubMed:21514407, ECO:0000269|PubMed:23990468, ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563, ECO:0000269|PubMed:28341745, ECO:0000269|PubMed:32741026}. Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. Translocation to the nucleus is increased in the presence of calcium in pre-osteoblasts (PubMed:21514407). The subcellular localization of NFATC plays a key role in the regulation of gene transcription (By similarity). Nuclear translocation of NFATC1 is enhanced in the presence of TNFSF11 (PubMed:26644563). Nuclear translocation is decreased in the presence of FBN1 which can bind and sequester TNFSF11 (PubMed:24039232). {ECO:0000250|UniProtKB:O95644, ECO:0000269|PubMed:21514407, ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563}.
Interaction partners:
- Protein phosphatase 3 catalytic subunit alpha
- Calcineurin subunit B type 1
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Nuclear factor of activated T-cells, cytoplasmic 2
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase 9
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Transcription factor GATA-4
- Glycogen synthase kinase-3 beta
- Mitogen-activated protein kinase 3
Sequence:
MPNTSFPVPSKFPLGPPAAVCGSGETLRPAPPSGGTMKAAEEEHYSYVSPSVTSTLPLPTAHSALPAACHDLQTSTPGISAVPSANHPPSYGGAVDSGPSGYFLSSGNTRPNGAPTLESPRIEITSYLGLHHGSGQFFHDVEVEDVLPSCKRSPSTATLHLPSLEAYRDPSCLSPASSLSSRSCNSEASSYESNYSYPYASPQTSPWQSPCVSPKTTDPEEGFPRSLGACHLLGSPRHSPSTSPRASITEESWLGARGSRPTSPCNKRKYSLNGRQPSCSPHHSPTPSPHGSPRVSVTEDTWLGNTTQYTSSAIVAAINALTTDSTLDLGDGVPIKSRKTALEHAPSVALKVEPAGEDLGTTPPTSDFPPEEYTFQHLRKGAFCEQYLSVPQASYQWAKPKSLSPTSYMSPSLPALDWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLTLQLFIGTADDRLLRPHAFYQVHRITGKTVSTTSHEIILSNTKVLEIPLLPENNMRAIIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPNGRTLSLQVASNPIECSQRSAQELPLVEKQSTDSYPVIGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPAQVSFYVCNGKRKRSQYQRFTYLPANGNSVFLTLSSESELRGGFY
Protein: Probable sigma-70 factor, ECF subfamily (Q9I265)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable transmembrane sensor
- Secretin/TonB short N-terminal domain-containing protein
- Probable sigma-70 factor, ECF subfamily
- Probable sigma-70 factor, ECF subfamily
- Secretin/TonB short N-terminal domain-containing protein
- Probable transcriptional regulator
- Probable transmembrane sensor
- Probable oxidoreductase
- Probable aldehyde dehydrogenase
- Probable transmembrane sensor
Sequence:
MGMDQTRNRLVGLMFQNDYSWLSGRLRRYLGCPHSAEDIASETFLKVLALPDPASIREPRALLTTIARRLMYDGWRRQDLERAYLESLAGLPEALAPSAEEQAQVVETLLRLERMLAGLSPKARAAFIHSQIGGLTYVEIACLLEVSVSRIHQYMVEGFKQCYQVLAE
Protein: Uncharacterized protein (Q385H3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFSKSVALVFAIAFVMEVVRAAAPDPAPGGATEKEFPLVWVCLGITVVGIGIALYVAHRRPDELHIPGASDEETEEMTRADGPENNENPGANETAADDGAKKEQATV
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q38CP2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MNYWIAATGALALAAAITAQGTTLLHNPKAQVTTTCGASHYMRHLTRQAESALERGLTNAKGALEKSNKLRVVAAYKTGGAATAASILAANLASETAKALETIKTETSNFLEGFTAAAELAGQQTIVSEIKSAQVQDVNTLTAAQAVTTPGIIQVKPTLAPAATAACFNDDGSPVSDAEAAQPNQGEPTLKFFVVSANTPGTTHNELLTIWGHGSTGTAPSTGCQNEATFIGIKGGDFLKTAAVTTTRLASSAGKTYPAITSTTTIPNDKTLNKAVTAIRKLETAVEALDAISDVSSPEDVAARPELKEAIAKALDGDKATYANSATKAKVDSFMAETFGKEPTIVKNTIVKDLKDLKPPKSAVGGNGENKLETINDPKELANAATYYTVKKFVDEQEQKKKNQANRSCPTNTDKTTEPAKSADECKKHTTAKDCKKEAGCDFDDKKPEGERCFPKPETEKKDDKSFSSNVRVSVPHVFAAFAALLF
Protein: Thiamine biosynthesis regulatory protein (P38141)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Positive regulator of thiamine biosynthesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- F-actin-capping protein subunit beta
- Thiamine metabolism regulatory protein THI3
- Protein PDC2
- Thiamine thiazole synthase
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20
- Nuclear migration protein JNM1
- Endoplasmic reticulum membrane protein complex subunit 10
- Actin-like protein ARP10
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI5
- Thiamine transporter
Sequence:
MVNSKRQQRSKKVASSSKVPPTKGRTFTGCWACRFKKRRCDENRPICSLCAKHGDNCSYDIRLMWLEENIYKVRKHSLISSLQARKSKSKPLCQKISKSRFKQMTHFRQLSPPTSDCEDSVHEASKETTLPNDNTFTISVRRLKIYNNAVASVFGSMTNRDYTQKRIDKKLDELLNMVENDISVVNLNCSKHGPYSVFRANPAAVTSALTDQLPSPGHSMSSAEETTTAALSSPPEDSTSLIDIIQGKIFGILWFNCYGNMILNRQEYTTWFINKMRNSLTTEFIRFLGKIIDDPDINMASCLFKECIARWSCVDWQSIAITMLVIIHGYTCPNLTKLLRVWFLQQKLLRFSMYPLVNFIINNTQDLDVLYHCNGLLGNADLFEDPYQDELTSELHVLVTERLVNSWKDTILQQLCSCQDTTLSCSQLRYWQLQLKCNQQFYKDVYAMQD
Protein: Non-selective voltage-gated ion channel VDAC2 (VDAC-2) (B36-VDAC) (Outer mitochondrial membrane protein porin 2) (P81155)
Organism: Rattus norvegicus (Rat)
Function: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity). The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (By similarity). The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity). Binds various lipids, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterol cholesterol (By similarity). Binding of ceramide promotes the Binding of ceramide promotes the mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P45880}. Membrane {ECO:0000250|UniProtKB:P45880}. Note=May localize to non-mitochondrial membranes. {ECO:0000250|UniProtKB:P45880}.
Interaction partners:
- Non-selective voltage-gated ion channel VDAC3
- ADP/ATP translocase 1
- Non-selective voltage-gated ion channel VDAC1
- Creatine kinase S-type
- Creatine kinase U-type, mitochondrial
- Cytochrome c, somatic
- ADP/ATP translocase 2
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- ADP/ATP translocase
- Translocator protein
Sequence:
MAECCVPVCQRPICIPPPYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVSGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSAYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRSNFAVGYRTGDFQLHTNVNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSFNAGGHKLGLALELEA