wanglab/gogpt-training-data huggingface dataset:
Protein: chitin synthase (EC 2.4.1.16) (Q6FXN4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- UDP-N-acetylglucosamine diphosphorylase
- Chitin biosynthesis protein CHS5
- Chitin synthase export chaperone
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- DNA topoisomerase 2
- 1,3-beta-glucan synthase
Sequence:
MVGYEDDDYYVGFSRDQESFIRSRNGNSLSMKRTSMPTRQGSLVRPERNRFDDPNNPHHYYVKTAEQQRSHLSVLPSSTGVAPGIARNSGSQRSDRSRLGRLGRSYYNGEEDDFYYPMQDLSKDRSGDSRYNPEADYPDRTALNSDDVANKNDNEGYEDEENDFDNSTDVENHLISNRPTSELKPKAESTRSLWMIYCYVVTFWAVPPLLSLFGMPEKARQRAWREKMGLLSIIAYIGAIVAYITFGFTKTVCGEQKLRLKNNSVSKEFSIINGQAFKLDSGTHPELLGLEVDSTGLYGPWSAAGKDASFLFQNVNGNCHGLITPKEDCTIPHNDNGDLAWYFPCKLFNQDGSSKPNFTVEYSPGWDCHTSDAEREAFYSLKSAAEVYFTWDGIKNSSRNLAVFNGHVLDLDLLDWLETDQLNVPSMFDDLKTSSLQGYDLSLILSTDHEKKVARCLTEIIRVGEVDSKSVGCIASDVVLYVSLVFILSVVVTKFLIACYFRWFVARNQGAYPVDNKTMDQHLKQVEDWSENIYSQGPIKTVQPEQRPKRKTRRRRSTIDLIRKKSSNFLNLTESVIDFDGGDGDGTDGPAISGMTTMTLQNNWNTNNLNKETQAKNSSPFFSYGNNSKINQLDASIIHPDIVQQPPVDFMPFGYPLAHTICFVTCYSEDEIGLRTTLDSLSTTDYPNSHKLIMVVCDGLIKGSGNDLTTPEIALGMMDDFITQPDDVLPYSYVAVASGTKRHNMAKIYAGFYKYDDSTVPVEKQQRVPMITIVKCGTPEEQGSAKPGNRGKRDSQVILMSFLQKITFDERMTELEYQLLRNIWQITGLMAEFYETVLMVDADTKVYPDSLTHMMAEMVRDPLIMGLCGETKIANKGQSWVTAIQVFEYYISHHQAKAFESVFGSVTCLPGCFSIYRIKSPKGADGYWVPILSNPDIVERYSDNVTDTLHKKNLLLLGEDRYLSSLMLKTFPKRKQVFVPKAACKTIAPDEFKVLLSQRRRWINSTVHNLFELVLIKDLCGTFCFSMQFVILIELIGTLVLPLAICFTIYVVIFAIVSHPTPIITLILLAIILGLPGMIVVITATSWSYLGWMFCYLIALPIWNFVLPSYAYWKFDDFSWGDTRTIAGGNKGAGGHGEEDGEFDHSKVKMRTWREFAREESDI
Protein: Neurolysin, mitochondrial (EC 3.4.24.16) (Endopeptidase 24.16) (Microsomal endopeptidase) (MEP) (Mitochondrial oligopeptidase M) (Neurotensin endopeptidase) (Soluble angiotensin-binding protein) (SABP) (Q02038)
Organism: Sus scrofa (Pig)
Function: Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:9182559}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:9182559}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:9182559}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:9182559}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:9182559}.
Interaction partners:
- Neurotensin/neuromedin N
Sequence:
MIVRCLSAARRLHRVGGSGILLRMTLGREAMSPLQAMSSYTVDGRNVLRWDLSPEQIKRRTEELIAQTKQVYDDIGMLDIEEVTYENCLQALADVEVKYIVERTMLDFPQHVSSDKEVRAASTEADKRLSRFDIEMSMREDIFLRIVRLKETCDLGKIKPEARRYLEKSVKMGKRNGLHLPEQVQNEIKAMKKRMSELCIDFNKNLNEDDTFLVFSKAELGALPDDFIDSLEKTDDNKYKITLKYPHYFPVMKKCCIPETRRKMEMAFNTRCKEENTIILQELLPLRAKVAKLLGYSTHADFVLEMNTAKSTHHVTAFLDDLSQKLKPLGEAEREFILNLKKKECEEKGFEYDGKINAWDLHYYMTQTEELKYSVDQEILKEYFPIEVVTEGLLNIYQELLGLSFEQVTDAHVWNKSVTLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPGCLLPDGSRMMSVAALVVNFSQPRAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDTDSLRRLSKHYKDGSPITDDLLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNTSLDAASEYAKYCTEILGVAATPGTNMPATFGHLAGGYDGQYYGYLWSEVFSMDMFYSCFKKEGIMNPEVGMKYRNLILKPGGSLDGMDMLQNFLKREPNQKAFLMSRGLHAP
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial (Q38B54)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- NB-ARC domain-containing protein
- Adrenodoxin reductase, putative
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase complex I subunit
- NADH dehydrogenase subunit NI8M
- NADH dehydrogenase 1 alpha subcomplex subunit 13
Sequence:
MRSVGGAVGATCCLVPSVGTQRRQYHAFQFAGFHGWKIPYEGKTKVTKEELDNIRFFTQRSKDKWDYHRVDENINSSSEFRKTHDRPEFEQGMREDNSTTDHGDLHTPKKYRLYEHFDEYTKPGVNKKVAACYAVKEQWDAEEFYYPGEAWKKNRPGFRSVPKELLNRQTWYHWSDTIMKWDEIQPTIRTRSWNPDWPPPGYKVPSMHCKKEFVFGVEDPAVVSEVERYNWYRSWSDSNLRCGWKDIWLFGVLFGAMYYMARNALDIVSMRAMMSNMFYPGRQFIRSFGTPRDWETDVFWWQRPLEEFPNQGEVWYINESRYKYINYIKKRDAMERALAEAEMNAV
Protein: Spermatogenesis-defective protein 39 homolog (hSPE-39) (VPS33B-interacting protein in apical-basolateral polarity regulator) (VPS33B-interacting protein in polarity and apical restriction) (Q9H9C1)
Organism: Homo sapiens (Human)
Function: Proposed to be involved in endosomal maturation implicating in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical RAB11A-dependent recycling pathway and in the maintenance of the apical-basolateral polarity. May play a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes; the functions seems to be independent of VPS33B. May play a role in vesicular trafficking during spermatogenesis (By similarity). May be involved in direct or indirect transcriptional regulation of E-cadherin (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Early endosome {ECO:0000269|PubMed:19109425}. Recycling endosome {ECO:0000269|PubMed:19109425, ECO:0000269|PubMed:22753090}. Late endosome {ECO:0000269|PubMed:19109425}. Note=Colocalizes in clusters with VPS33B at cytoplasmic organelles (PubMed:19109425).
Interaction partners:
- Vacuolar protein sorting-associated protein 33B
- Vacuolar protein sorting-associated protein 33A
- Vacuolar protein sorting-associated protein 16 homolog
- Ras-related protein Rab-11A
- Vacuolar protein sorting-associated protein 45
- Syntaxin-12
- Vam6/Vps39-like protein
- Syntaxin-8
- Syntaxin-7
- Neurobeachin-like protein 2
Sequence:
MNRTKGDEEEYWNSSKFKAFTFDDEDDELSQLKESKRAVNSLRDFVDDDDDDDLERVSWSGEPVGSISWSIRETAGNSGSTHEGREQLKSRNSFSSYAQLPKPTSTYSLSSFFRGRTRPGSFQSLSDALSDTPAKSYAPELGRPKGEYRDYSNDWSPSDTVRRLRKGKVCSLERFRSLQDKLQLLEEAVSMHDGNVITAVLIFLKRTLSKEILFRELEVRQVALRHLIHFLKEIGDQKLLLDLFRFLDRTEELALSHYREHLNIQDPDKRKEFLKTCVGLPFSAEDSAHIQDHYTLLERQIIIEANDRHLESAGQTEIFRKHPRKASILNMPLVTTLFYSCFYHYTEAEGTFSSPVNLKKTFKIPDKQYVLTALAARAKLRAWNDVDALFTTKNWLGYTKKRAPIGFHRVVEILHKNNAPVQILQEYVNLVEDVDTKLNLATKFKCHDVVIDTYRDLKDRQQLLAYRSKVDKGSAEEEKIDALLSSSQIRWKN
Protein: Probable conserved transmembrane transport protein MmpL13a (O06545)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Probable conserved transmembrane transport protein MmpL13b
- Anti-sigma-L factor RslA
- Probable transport protein MmpL6
Sequence:
MLQRIARLAIAAPRRIIGFAVFVFIAAAVFGVPVADSLSPGGFQDPRSESARAIEVLTDKFGQSGQKMLIVVTAAAGADSPPAREVGTDIVEVLRRSPLVYNVTSPWTVPPTAAADLLSTDGKSGLIVVNVKGGENDAQNHAQTLSDEVAHDRDGVTVRAGGSAMEYAQINRQNKDDLLVMELIAIPLSFLVLIWVFGGLLAAGLPMAQAVLAVVGSMAVLRLVTFATEVSTFALNLSTALGLALAIDYTLLIVSRYRDELAEGSDRDEALIRTMALRGARCCFRRSPWRCRCRRLRCSRCTF
Protein: Peptide receptor GPCR (Q2HPH2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MDMEYITSSSGNITATTEADFSSSLGESNVTEYNTTEMDANESAGEDEEMLRIAFFIGHFVHQYYIPVLCCTGSIGNILSVFVFFRTKLRKLSSSFYLAALAVSDTCFLAGLFAQWLNFLNVDIYNQNYFCQFFTFFSYLASFCSVWFVVAFTVERFIAVIYPLKRQTMCTVRRAKIVLFCLTLVGCLHCLPYIVIAKPVFMPKLNTTICDLNSEYKEQLALFNYWDTIVVYAVPFTTIAVLNTCTGCTVWKFATVRRTLTMHKMKPQTNSMPPNSSNSSGGASSAVASYRLSASLKRQKSTGTHPSGQHNVANRQTDDQEQQQQSQQHQINNCQHHCEITQKPARRKVQNSSQLKVTKMLLIVSTVFVCLNLPSCLLRIEAYWETESARNQNSTIALQYIFHAFFITNFGINFVLYCVSGQNFRKAVLSIFRRVSSAQREAGNTQVTVSEYCRNTGTSTRRRMMTQHCWNEMHELHPLK
Protein: Antimicrobial peptide 6 (XT-6) (P84386)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Has antimicrobial activity against Gram-positive bacterium S.aureus and Gram-negative bacterium E.coli and strong activity against yeast C.albicans. Enhances the antibacterial activity of XT3. Has strong hemolytic activity against human red blood cells.
Subcellular location: Secreted {ECO:0000269|PubMed:11738090}.
Interaction partners:
Sequence:
GFLGSLLKTGLKVGSNLL
Protein: Caldesmon 1 (Q3TUS1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLSGSGSQGRRCLATLSQIAYQRNDDDEEEAARERRRRARQERLRQKQEEESLGQVTDQVEAHVQNSVPDEESKPASSNTQVEGDEEAALLERLARREERRQKRLQEALERQKEFDPTITDGSLSGPSRRMQNDSAENETAEGEEKRESRSGRYEVEETEVVIKSYQKNSYQDAEDKKKEEKEEEEQEKLKGGSLGENQIKDEKIKKDKEPKEEVKSFLD
Protein: Protein S100-A4 (Metastasin) (Metastatic cell protein) (PEL98) (Placental calcium-binding protein) (Protein 18A2) (Protein Mts1) (S100 calcium-binding protein A4) (P07091)
Organism: Mus musculus (Mouse)
Function: Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy. Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9. Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis. Modulates also the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels (By similarity). Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes. In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P26447}. Nucleus {ECO:0000250|UniProtKB:P26447}. Cytoplasm {ECO:0000269|PubMed:8051043}.
Interaction partners:
- Annexin A2
- Myosin-9
- Cellular tumor antigen p53
- Annexin A1
- Fibroblast growth factor 2
- Pro-epidermal growth factor
- Advanced glycosylation end product-specific receptor
- Protein S100-A10
- Protein S100-A6
- Vimentin
Sequence:
MARPLEEALDVIVSTFHKYSGKEGDKFKLNKTELKELLTRELPSFLGKRTDEAAFQKVMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGCPDKEPRKK
Protein: Large ribosomal subunit protein eL32B (60S ribosomal protein L32-B) (O42935)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL39
- Elongation factor 3
- Large ribosomal subunit protein eL30A
Sequence:
MAAINIVKKRTKPFKRHQSDLFKRVGESWRKPRGIDSCVRRRFRGTISMPKIGYGNNKKTRYCMPNGLKAFLVRNVSDVELLLMHNKTYAAEIASNVSARKRVEIVEKARALGVKVTNAGAKVRSQE
Protein: Nucleotide triphosphate diphosphatase NUDT15 (EC 3.6.1.9) (MutT homolog 2) (mMTH2) (Nucleoside diphosphate-linked moiety X motif 15) (Nudix motif 15) (Nucleoside diphosphate-linked to another moiety X hydrolase 15) (Nudix hydrolase 15) (Q8BG93)
Organism: Mus musculus (Mouse)
Function: May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives (By similarity). Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides to prevent their incorporation into DNA, is unclear. Through the hydrolysis of thioguanosine triphosphates may participate in the catabolism of thiopurine drugs (By similarity). May also have a role in DNA synthesis and cell cycle progression by stabilizing PCNA (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro.
Interaction partners:
- ADP-sugar pyrophosphatase
- 8-oxo-dGDP phosphatase NUDT18
- NAD-capped RNA hydrolase NUDT12
- Inosine triphosphate pyrophosphatase
- Thiopurine S-methyltransferase
- Bis
- Oxidized purine nucleoside triphosphate hydrolase
- Uridine diphosphate glucose pyrophosphatase NUDT14
- NAD
- m7GpppN-mRNA hydrolase NUDT17
Sequence:
MAANAEPRRRPGVGVGVVVLSCEHPRCVLLGKRKGSFGAGSFQLPGGHLEFGETWEECAQRETWEEAGLHLKNVCFASVVNSFVEKENYHYVTILMKGEVDMTHDSEPRNMEPEKNESWEWVPWEEFPPLDQLFWALRCLKEQGYDPFKEDLNHLEGYRGEHLERTTKTP
Protein: Large ribosomal subunit protein uL3c (50S ribosomal protein L3-1, chloroplastic) (Q9SKX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Large ribosomal subunit protein uL6c
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein eL38z/eL38y
- At1g43860
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein uL4c
Sequence:
MAIAMAVVSFPSLLNKTTLSSSLFTPTFLPAKSSSLLIKSSPKTRFVVSSSMEAGIGVMGSKLGMMSFFEEDGTVVPVTVVGFREGNIVTQIKTLATDGYDAVQIGYRRVRDKKLTKPETGHLQKAGTIPMRHLQEFRLTNIEGFEPNQKLVFDEIFKEGDLVDVAGTTIGKGFQGGIKRHHFKRGQMTHGSKSHRALGSIGAGTTPGRVYKGKKMPGRMGGTRTKIRKLKIVKVDKELNVVMIKGALPGKPGNLLRITPAKIVGVNIPKN
Protein: Putative histone-lysine N-methyltransferase PRDM6 (EC 2.1.1.361) (PR domain zinc finger protein 6) (PR domain-containing protein 6) (Q9NQX0)
Organism: Homo sapiens (Human)
Function: Putative histone methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. Promotes the transition from differentiated to proliferative smooth muscle by suppressing differentiation and maintaining the proliferative potential of vascular smooth muscle cells. Also plays a role in endothelial cells by inhibiting endothelial cell proliferation, survival and differentiation. It is unclear whether it has histone methyltransferase activity in vivo. According to some authors, it does not act as a histone methyltransferase by itself and represses transcription by recruiting EHMT2/G9a. According to others, it possesses histone methyltransferase activity when associated with other proteins and specifically methylates 'Lys-20' of histone H4 in vitro. 'Lys-20' methylation represents a specific tag for epigenetic transcriptional repression.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q3UZD5}.
Interaction partners:
- PR domain zinc finger protein 14
- Protein CBFA2T2
Sequence:
MLKPGDPGGSAFLKVDPAYLQHWQQLFPHGGAGPLKGSGAAGLLSAPQPLQPPPPPPPPERAEPPPDSLRPRPASLSSASSTPASSSTSASSASSCAAAAAAAALAGLSALPVSQLPVFAPLAAAAVAAEPLPPKELCLGATSGPGPVKCGGGGGGGGEGRGAPRFRCSAEELDYYLYGQQRMEIIPLNQHTSDPNNRCDMCADNRNGECPMHGPLHSLRRLVGTSSAAAAAPPPELPEWLRDLPREVCLCTSTVPGLAYGICAAQRIQQGTWIGPFQGVLLPPEKVQAGAVRNTQHLWEIYDQDGTLQHFIDGGEPSKSSWMRYIRCARHCGEQNLTVVQYRSNIFYRACIDIPRGTELLVWYNDSYTSFFGIPLQCIAQDENLNVPSTVMEAMCRQDALQPFNKSSKLAPTTQQRSVVFPQTPCSRNFSLLDKSGPIESGFNQINVKNQRVLASPTSTSQLHSEFSDWHLWKCGQCFKTFTQRILLQMHVCTQNPDRPYQCGHCSQSFSQPSELRNHVVTHSSDRPFKCGYCGRAFAGATTLNNHIRTHTGEKPFKCERCERSFTQATQLSRHQRMPNECKPITESPESIEVD
Protein: Myosin light chain kinase isoform-III (O01652)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SLLVLPAIRGNSSSSSLAARSCILTRPEDCTALIGGHVRLSVHYEPFPGTKVIWYKACHPIVESSNVTIRTTSQKSTLYITDISADDSGKYTVEVMNDYGVEAAAASVAVEGPPEPPSGQPSVSLGPDRVAVAWCGPPYDGGCMITGFIIEMQTIGDENCDEDSWQQVTRVVDSLAYTVKNLQPERQYRFRVRAENIHGRSAPGQASELVQITNTPQRSTSSDASDRFGQATVSVQSGGDFKSRFEIIEELGKGRFGIVYKVQERGQPEQLLAAKVIKCIKSQDRQKVLEEISIMRALQHPKLLQLAASFESPREIVMVMEYITGGELLQRVVADDFTLTEMDCILFLRQVCDGVAYMHGQSVVHLDLKPENIMCHTRTSHQIKIIDFGLAQRLDTKAPVRVLFGTPEFIPPEIISYEPIGFQSDMWSVGVICYVLLSGLSPFMGDTDVETFSNITRADYDYDDEAFDCVSQEAKDFISQLLVHRKEDRLTAQQCLASKWLSQRPDDSLSNNKICTDKLKKFIIRRKWQQRSREGAVEAHPVYPAKASHPRCVPCPALRCLSDPLRRRG
Protein: Integrin, alpha V (L7RXH0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET
Protein: PH and SEC7 domain-containing protein 1 (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6) (Exchange factor for ARF6) (Exchange factor for ARF6 A) (Pleckstrin homology and SEC7 domain-containing protein 1) (Q9ESQ7)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide exchange factor for ARF6 (By similarity). Induces cytoskeletal remodeling (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:A5PKW4}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:A5PKW4}. Cleavage furrow {ECO:0000250|UniProtKB:A5PKW4}. Note=Distributed uniformly on the plasma membrane, as well as throughout the cytoplasm during metaphase. Subsequently concentrated at patches in the equatorial region at the onset of cytokinesis, and becomes distributed in the equatorial region concurrent with cleavage furrow ingression. In later cytokinesis phases, fades away from the cleavage furrow and becomes uniformly distributed throughout the plasma membrane. {ECO:0000250|UniProtKB:A5PKW4}.
Interaction partners:
- ADP-ribosylation factor 6
Sequence:
MPHSGLLKSPVPFLPGTSPSADGPDSFSCMFEAIMESHRAKGTSYSSLASLEALASPGPTQSPFFTFEMPPQPPAPRPDPPAPAPLAPLEPDSGTSSVADGPWTQRREVEESDAGATLAPRKELPSPSHSEDSLGLGAAPLGSEPPLSQLVSDSDSELDSTERLALGSTDTLSNGQKADLEAAQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTGMTLDQALRVFLKELALMGETQERERVLAHFSQRYFQCNPEALSSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLEGLNDGGDFPRELLKALYSSIKNEKLQWAIDEEELRRSLSELADPNPKVIKRVSGGSGSSSSPFLDLTPEPGAAVYKHGALVRKVHADPDCRKTPRGKRGWKSFHGILKGMILYLQKEEYQPGKALSEAELKNAISIHHALATRASDYSKRPHVFYLRTADWRVFLFQAPSLEQMQSWITRINVVAAMFSAPPFPAAVSSQKKFSRPLLPSAATRLSQEEQVRTHEAKLKAMASELREHRAAHLGKKARGKEAEEQRQKETYLEFEKSRYGTYAALLRVKMKAASEELDAIEAALAQAGSTEEGCPPPHSSPSLQPNPTSQPRAQRPGSEARAGAGSTRPKP
Protein: Receptor expression enhancing protein A, isoform I (A0A0B4JCU3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Atlastin
- Spastin
- ADP-ribosylation factor-like protein 6-interacting protein 1
- Seipin
- Protein spartin
- Reticulon-like protein
- Reticulon-like protein
- Fatty acid 2-hydroxylase
Sequence:
MRPIYQQEPPLFYQRPANLRRLRHPPGTVYGRSYSLEDQPEDVIPVYPKFIYAPQQQQQQQRAPYPLYQLGDSLSSLDSDFPENEYAGAYIVEDRVPLANAPTPKVVQNLNALGRMLELLQRCPLPCLSFNTACICSLIVIFLAPRTCAQSLLFPAFRLFCGTLYPAYASYKAVRTKDVKEYVKWMMYWIVFAFFTCIETFTDIFISWLPFYYEVKVALVFWLLSPATKGSSTLYRKFVHPMLTRHEQEIDEYVNQAKERGYSAVLQLGSKGVNYATNVLMQTAIKGGGNLVQTIKRSYSLSDLSEPDMHRTQDELDDVMMSSMTSSAVVMRSTATGARLLRPRNQTPVGRSGSGTRHSTGMYFTEVDVTAKNAGDFNYNIRSQDDISSGYSSAEPVSGLSRTSSMTNASKARAKSKRNELLEEMRDEVYLDNQLYFQGVQRKSSVPEAEELKIVESSESIQSQELEKVLKEENIDAEDEAFFETLPLIEEHINEVVANYGRDEKLLPQERKHNSIEEEQFEDALFEEPQKCVSDEVDAKNIEEILTDRSQNQTPNGSAETTDSGTPSQNKPYVHPPIDPFLLVLSASASAPDPFMPERPRPMSPREMRETLEEIKHSFRAQLEAEPSVSASPSPSLRPKANHGKGRAPPPPLPPKKHSLSPQPDAISQTSTGSVERKSGIGQLFKNIKANVLRNKANPSQQQPEDEQLAAKETQI
Protein: Proto-oncogene c-Rel (p68) (P16236)
Organism: Gallus gallus (Chicken)
Function: Proto-oncogene that may play a role in differentiation and lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- NF-kappa-B inhibitor alpha
- Nuclear factor NF-kappa-B p105 subunit
- NFKB inhibitor beta.
- Transcription factor p65
- CREB binding protein.
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MAGISEPYIEIFEQPRQRGMRFRYKCEGRSAGSIPGEHSTDNNKTFPSIQILNYFGKVKIRTTLVTKNEPYKPHPHDLVGKDCRDGYYEAEFGPERRVLSFQNLGIQCVKKKDLKESISLRISKKINPFNVPEEQLHNIDEYDLNVVRLCFQAFLPDEHGNYTLALPPLISNPIYDNRAPNTAELRICRVNKNCGSVKGGDEIFILCDKVQKDDIEVRFVLDNWEAKGSFSQADVHRQVAIVFRTPPFLRDITEPITVKMQLRRPSDQEVSEPMDFRYLPDEKDPYGNKAKRQRSTLAWQKLIQDCGSAVTERPKAAPIPTVNPEGKLIKKEPNMFSPTLMLPGLGTLTSSSQMYPPCSQMPHQPAQLGPGKQDTLPSCWQQLFSSSPSASSLLSMHPHNSFTAEVPQPGAQGSSSLPAFHDNPLNWPDEKDSSFYRNFGSTNGMGAAMVSAADMQSASSNSIVHATHQASATAASIVNMETNDMNCTSLNFEKYTQVLNVSNHRQQLHQAPAACPPVAAPGSTPFSSQPNLADTAVYNSFLDQEVISDSRLSTNPLQNHQNSLTLTDNQFYDTDGVHTDELYQSFQLDTNILQSYNH
Protein: Inorganic triphosphatase (PPPase) (EC 3.6.1.25) (Q82UI9)
Organism: Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
Function: Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.
Interaction partners:
- Guanylate cyclase
- Guanylate cyclase
- SpoT bifunctional enzyme
- Nucleoside diphosphate kinase
- Pyruvate kinase
- CHAD domain-containing protein
- ParA family ATPase
- GTP cyclohydrolase FolE2
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
Sequence:
MTEIERKFLVATFPDGELHAVPLRQGYLTTPTDSIELRLRQQGTEYFMTLKSEGGLSRQEYEIQIDVTQFEMLWPATEGRRVEKTRYSGKLPDGQLFELDVFAGHLSPLMLVEVEFLSEDAAQAFIPPPWFGEEVTEDKRYKNKALALSIP