wanglab/gogpt-training-data huggingface dataset:
Protein: Natural killer cell receptor 2B4 (NK cell activation-inducing ligand) (NAIL) (NK cell type I receptor protein 2B4) (NKR2B4) (h2B4) (SLAM family member 4) (SLAMF4) (Signaling lymphocytic activation molecule 4) (CD antigen CD244) (Q9BZW8)
Organism: Homo sapiens (Human)
Function: Heterophilic receptor of the signaling lymphocytic activation molecule (SLAM) family; its ligand is CD48. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Acts as activating natural killer (NK) cell receptor. Activating function implicates association with SH2D1A and FYN. Downstreaming signaling involves predominantly VAV1, and, to a lesser degree, INPP5D/SHIP1 and CBL. Signal attenuation in the absence of SH2D1A is proposed to be dependent on INPP5D and to a lesser extent PTPN6/SHP-1 and PTPN11/SHP-2. Stimulates NK cell cytotoxicity, production of IFN-gamma and granule exocytosis. Optimal expansion and activation of NK cells seems to be dependent on the engagement of CD244 with CD48 expressed on neighboring NK cells (By similarity). Acts as costimulator in NK activation by enhancing signals by other NK receptors such as NCR3 and NCR1. At early stages of NK cell differentiation may function as an inhibitory receptor possibly ensuring the self-tolerance of developing NK cells. Involved in the regulation of CD8(+) T-cell proliferation; expression on activated T-cells and binding to CD488 provides costimulatory-like function for neighboring T-cells (By similarity). Inhibits inflammatory responses in dendritic cells (DCs) (By similarity).
Subcellular location: Membrane {ECO:0000305|PubMed:10359122}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:11034353}. Note=Receptor engagement results in a recruitment to lipid drafts essential for the subsequent tyrosine phosphorylation of the ITSMs. {ECO:0000269|PubMed:11034353}.
Interaction partners:
- CD48 antigen
- SH2 domain-containing protein 1A
- SH2 domain-containing protein 1B
- Tyrosine-protein kinase Fyn
- SLAM family member 6
- Natural cytotoxicity triggering receptor 1
- Histone-lysine N-methyltransferase EZH2
- Natural killer cells antigen CD94
- CD160 antigen
- Tyrosine-protein phosphatase non-receptor type 11
Sequence:
MLGQVVTLILLLLLKVYQGKGCQGSADHVVSISGVPLQLQPNSIQTKVDSIAWKKLLPSQNGFHHILKWENGSLPSNTSNDRFSFIVKNLSLLIKAAQQQDSGLYCLEVTSISGKVQTATFQVFVFESLLPDKVEKPRLQGQGKILDRGRCQVALSCLVSRDGNVSYAWYRGSKLIQTAGNLTYLDEEVDINGTHTYTCNVSNPVSWESHTLNLTQDCQNAHQEFRFWPFLVIIVILSALFLGTLACFCVWRRKRKEKQSETSPKEFLTIYEDVKDLKTRRNHEQEQTFPGGGSTIYSMIQSQSSAPTSQEPAYTLYSLIQPSRKSGSRKRNHSPSFNSTIYEVIGKSQPKAQNPARLSRKELENFDVYS
Protein: Serpin family H member 1 (E9PJH8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSLLLLSAFCLLEAALAAEVKKPAAAAAPGTAEKLSPKAATLAERSAGLAFSLYQAMAKDQAVENILVSPVVVASSLGLVSLGGKATTASQAKAVLSAEQLRDEEVHAGLGELLRSLSNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVMMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLIILMPHHVEPLERLEKLLTKEQLKIWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFELDTDGNPFDQDIY
Protein: Protein AF-17 (ALL1-fused gene from chromosome 17 protein) (P55198)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein AF-10
- Protein AF-9
- Protein ENL
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- AF4/FMR2 family member 1
- RNA polymerase II elongation factor ELL
- LIM and SH3 domain protein 1
- Afadin
- Histone-lysine N-methyltransferase 2A
- Septin-6
Sequence:
MKEMVGGCCVCSDERGWAENPLVYCDGHACSVAVHQACYGIVQVPTGPWFCRKCESQERAARVRCELCPHKDGALKRTDNGGWAHVVCALYIPEVQFANVLTMEPIVLQYVPHDRFNKTCYICEEQGRESKAASGACMTCNRHGCRQAFHVTCAQMAGLLCEEEVLEVDNVKYCGYCKYHFSKMKTSRHSSGGGGGGAGGGGGSMGGGGSGFISGRRSRSASPSTQQEKHPTHHERGQKKSRKDKERLKQKHKKRPESPPSILTPPVVPTADKVSSSASSSSHHEASTQETSESSRESKGKKSSSHSLSHKGKKLSSGKGVSSFTSASSSSSSSSSSSGGPFQPAVSSLQSSPDFSAFPKLEQPEEDKYSKPTAPAPSAPPSPSAPEPPKADLFEQKVVFSGFGPIMRFSTTTSSSGRARAPSPGDYKSPHVTGSGASAGTHKRMPALSATPVPADETPETGLKEKKHKASKRSRHGPGRPKGSRNKEGTGGPAAPSLPSAQLAGFTATAASPFSGGSLVSSGLGGLSSRTFGPSGSLPSLSLESPLLGAGIYTSNKDPISHSGGMLRAVCSTPLSSSLLGPPGTSALPRLSRSPFTSTLPSSSASISTTQVFSLAGSTFSLPSTHIFGTPMGAVNPLLSQAESSHTEPDLEDCSFRCRGTSPQESLSSMSPISSLPALFDQTASAPCGGGQLDPAAPGTTNMEQLLEKQGDGEAGVNIVEMLKALHALQKENQRLQEQILSLTAKKERLQILNVQLSVPFPALPAALPAANGPVPGPYGLPPQAGSSDSLSTSKSPPGKSSLGLDNSLSTSSEDPHSGCPSRSSSSLSFHSTPPPLPLLQQSPATLPLALPGAPAPLPPQPQNGLGRAPGAAGLGAMPMAEGLLGGLAGSGGLPLNGLLGGLNGAAAPNPASLSQAGGAPTLQLPGCLNSLTEQQRHLLQQQEQQLQQLQQLLASPQLTPEHQTVVYQMIQQIQQKRELQRLQMAGGSQLPMASLLAGSSTPLLSAGTPGLLPTASAPPLLPAGALVAPSLGNNTSLMAAAAAAAAVAAAGGPPVLTAQTNPFLSLSGAEGSGGGPKGGTADKGASANQEKG
Protein: Small ribosomal subunit protein uS10m (28S ribosomal protein S10, mitochondrial) (MRP-S10) (S10mt) (P82670)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10938081, ECO:0000269|PubMed:24799711}.
Interaction partners:
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein mS31
Sequence:
MAVRAVFGALGRRLWQGSKNFSVSSSRSNIAKNDGFLLSTSMKWVQFSNLHVDVPKDLTKPTITISDEPDTLYKRLSVLVKGHDKAVLDSYEYFAVLAAKELGISVKVHEPPRKIERFTLLKSVHIFKKHRVQYEMRTLYRCLELEHLTGSTADVYLEYIQRNLPEGVAMEVTKTRLEQLPEHIKKPVWETTPEEKGDSKS
Protein: AP-1 complex subunit gamma (B0R024)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- Adaptor-related protein complex 1 subunit mu 2
- AP-1 complex subunit mu-1
- AP complex subunit beta
- AP complex subunit beta
- AP-3 complex subunit sigma-2
- AP complex subunit beta
- Adaptor-related protein complex 5 subunit mu 1
- AP complex subunit sigma
- AP complex subunit sigma
- AP-2 complex subunit mu-B
Sequence:
MTPSVRLQEMIRVIRSARTQGEERGIIQKECAEIRAQFRQTDNGERSHSLAKLLYVHMLGYPAHFGQMECVRLIASPRYSEKRIGYLGAMMLLDEKQDASLLITNSIKNDLSHSSQYVQSLALCTLACMGSSEMCRDLAPEIERLLRASTSYIKKKATLCAVHIIRKVPELAELFTPSARSLLSEKNHGVLHGAVVLITELCERNAETLDKFRKAVPELVTIMKGLVTSSYSPEHNVAGISDPFLQVRILRLLRILGHNNDSASDAMNDLLAQVATNTDSSKTAGSAVLYETVLTIMDINSESGLRVLAVNILGRFLLNNDRNIRYISMTSLQKIVQTDHNAVQRHRGTIVDCLKDQDTSVKRRALELSLALVSPVNIRSMMKELLIFLSSCPVELRSQTASGIFNAAERYSPSKRWHIDTILHVLTTAGGDVRDETVPNLIQLITTASELHCYTVHKLYRALVKDISQQSLVQVACWCIGEYGDLLLKGECEEIEPVQVTEDDVLDALETVLQSHMSAPATRGFALTATMKLSTRITDNVDRIRSIVSIYGSCIDLELQQRAVEYNALFKKYDHMRAAVLERMPLMEKNSPGHTNGDSSGEIKEPEPAKTKPVEPILLSEPANQVCDLLDLLGGTDTPVQPSSAPTSTATTTSSADLLDLLGGLEPTPVPAVTVYEKNGVSLKIQCDSQTDTDITVTLIASNSTQNDISNFTLQAAVPKSVQLQMKAPSGNVIAAHGLGQVTQTVLLNNPNKVSLKMRVRVSYSDQGTMLQDTVQIDSFPSPSWNSQPSIGVL
Protein: Proliferation-associated protein 2G4 (Q6AYD3)
Organism: Rattus norvegicus (Rat)
Function: May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site). Together with PTBP1 is required for the translation initiation on the foot-and-mouth disease virus (FMDV) IRES (By similarity). Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:16832058}. Nucleus, nucleolus {ECO:0000269|PubMed:16832058}. Note=Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization. {ECO:0000250|UniProtKB:Q9UQ80}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:16832058}.
Interaction partners:
- GTP-binding protein 4
- Pescadillo homolog
- Nucleolar GTP-binding protein 2
- WD repeat-containing protein 18
- Ribosome assembly factor mrt4
- Ribosome production factor 2 homolog
- Large ribosomal subunit protein uL14
- Probable ribosome biogenesis protein RLP24
- 60S ribosomal export protein NMD3
- Protein SDA1 homolog
Sequence:
MSGEDEQQEQTIAEDLVVTKYKMGGDIANRVLRSLVEASSSGVSVLSLCEKGDAMIMEETGKIFKKEKEMKKGIAFPTSISVNNCVCHFSPLKSDQDYILKEGDLVKIDLGVHVDGFIANVAHTFVIGVAQGSQVTGRKADVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSHQLKQHVIDGEKTIIQNPTDQQKKDHEKAEFEVHEVYAVDVLVSSGEGKAKDAGQRTTIYKRDPSKQYGLKMKTSRAFFSEVERRFDAMPFTLRAFEDEKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNGPMRITSGPFEPDLYKSEMEVQDAELKALLQSSASRKTQKKKKKKASKTAENATSGETLEENGAGD
Protein: Uncharacterized transporter YHL008C (P38750)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVDDSNYLTPHETALAVVATAMKKARLQLDTLLINSILGGVLFSSGSFLLVAVYSEDPDIVARNPGIVNLITGVNFAMGLFYVVMMGADLFNSNILFFSVGVLRKAVTIYDLMISWVVSWLGNIAGSLFVSYLFGHLSGISSQKLWIIGSRQIIEQKVSYSFVQTFLKGIACNFFVCLAIYLQLMAKPIHVKFILMSFPIIDFIGIGFTHVVGDMSASFIAMLNGANVSVGKYIWKLLIPASLGNIVGGLFFSAVVPFYLHLVVVERDRKRLSLPEYEARDEQPELNMDSRVVRIQKNECDDDATETGEDLENLTEKGFASIYNTNHDNSSYFTGRSLNSLRSIPSSVITSDNVTMESDLGEPVQFIPKSNSTTRSPHLGLPHNLPHNHSIKSINRHRINKRHSLRSPPGVFPVRGMGEPLEREKTIEDATYDPKENELFLRRAETHNSAYVKNKKKEDDNLLRLVKTEEDREQKEYEKNGGYNILENKPGTRLEKIITHLAENVSSREVTPPILPRTTQDTFPHNAPASSPAYTDDAHSLRKANSTTLGGLFRAVSKEFHSSKDAESPDDLLKKMAAVGINRNARITANNVAGIVNLNKEDLDSTTRRQKITEPKNFYNRHTSPQL
Protein: Ferroportin (Ferroportin-1) (Iron-regulated transporter 1) (Solute carrier family 40 member 1) (Q9NP59)
Organism: Homo sapiens (Human)
Function: Major iron transporter that plays a key role in balancing cellular and systemic iron levels. Transports iron from intestinal, splenic, and hepatic cells into the blood to provide iron to other tissues (By similarity). Controls therefore dietary iron uptake, iron recycling by macrophages, and release of iron stores in hepatocytes (By similarity). When iron is in excess, hepcidin/HAMP levels increase resulting in a degradation of ferroportin/SLC40A1 limiting the iron efflux to plasma.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10882071, ECO:0000269|PubMed:15692071, ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:24304836, ECO:0000269|PubMed:29237594, ECO:0000269|PubMed:30247984}; Multi-pass membrane protein {ECO:0000269|PubMed:32814342}. Basolateral cell membrane {ECO:0000269|PubMed:29792530}; Multi-pass membrane protein {ECO:0000269|PubMed:32814342}. Note=Localized to the basolateral membrane of hepatocytoma WIF-B cells. {ECO:0000269|PubMed:29792530}.
Interaction partners:
- Hepcidin
- Hephaestin
- Natural resistance-associated macrophage protein 2
- Ceruloplasmin
- Transferrin receptor protein 2
- Plasma membrane ascorbate-dependent reductase CYBRD1
- Transferrin receptor protein 1
- Ferritin light chain
- Hereditary hemochromatosis protein
- Hemojuvelin
Sequence:
MTRAGDHNRQRGCCGSLADYLTSAKFLLYLGHSLSTWGDRMWHFAVSVFLVELYGNSLLLTAVYGLVVAGSVLVLGAIIGDWVDKNARLKVAQTSLVVQNVSVILCGIILMMVFLHKHELLTMYHGWVLTSCYILIITIANIANLASTATAITIQRDWIVVVAGEDRSKLANMNATIRRIDQLTNILAPMAVGQIMTFGSPVIGCGFISGWNLVSMCVEYVLLWKVYQKTPALAVKAGLKEEETELKQLNLHKDTEPKPLEGTHLMGVKDSNIHELEHEQEPTCASQMAEPFRTFRDGWVSYYNQPVFLAGMGLAFLYMTVLGFDCITTGYAYTQGLSGSILSILMGASAITGIMGTVAFTWLRRKCGLVRTGLISGLAQLSCLILCVISVFMPGSPLDLSVSPFEDIRSRFIQGESITPTKIPEITTEIYMSNGSNSANIVPETSPESVPIISVSLLFAGVIAARIGLWSFDLTVTQLLQENVIESERGIINGVQNSMNYLLDLLHFIMVILAPNPEAFGLLVLISVSFVAMGHIMYFRFAQNTLGNKLFACGPDAKEVRKENQANTSVV
Protein: Tetraspanin family protein (F4JM26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSSEYILSVKTTFFCFVRNHQRLFLRRSLLRSLISISRIVIEKMRHNCCHVSFASILKILNFLQAFIGISIIIYSIWMLDQYNHHVPVDPPPSQPPAASSPDSSYSFSNSIIEINSVSDSLKNPIDFVSGIVLGSGGGDSGFNLRSLDLPAPWFIYCFMAIGILVCIVTIIGFIAAEAINGCCLCFYSILKTLLIIIEAALVGFIVIDRHWEKDLPYDPTGELNSLRAFIEENIDICKWVGIVVVAIQLLSLLLALVLRAMVSPRQSELDDEDDFENPMSRARDNLLGPQANQTSSGSSNIDNWRSRIREKYGLINSQSHTPSA
Protein: Zinc finger CCCH domain-containing protein 32 (AtC3H32) (Zinc finger CCCH domain-containing protein ZFN-like 1) (Q84W91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Zinc finger MYM-type-like protein
- Zinc finger MYM-type-like protein
- Zinc finger CCCH domain-containing protein 21
- Zinc finger CCCH domain-containing protein 53
- Zinc finger CCCH domain-containing protein 5
- Protein FAR1-RELATED SEQUENCE 3
Sequence:
MYARNPPLNGSQSAQAPDWTPADADTGLQESMWRLGLGSDSYPERPGAPDCAYYMRTGVCGYGNRCRYNHPRDRASVEATVRATGQYPERFGEPPCQFYLKTGTCKFGASCKFHHPKNAGGSMSHVPLNIYGYPVREGDNECSYYLKTGQCKFGITCKFHHPQPAGTTVPPPPASAPQFYPSVQSLMPDQYGGPSSSLRVARTLLPGSYMQGAYGPMLLTPGVVPIPGWSPYSAPVSPALSPGAQHAVGATSLYGVTQLTSTTPSLPGVYPSLSSPTGVIQKEQAFPERPGEPECQYYLKTGDCKFGTSCKFHHPRDRVPPRANCVLSPIGLPLRPGVQRCTFYVQNGFCKFGSTCKFDHPMGTIRYNPSASSLADAPVAPYPVSSLLGALAAAPSSSSTELIAGGAKDAYMTGVPTSRSTSNISAGLIFSQSGGSIPFSELQLSSQSSLPLTGSRITRQGREIRRSF
Protein: TP53-regulated inhibitor of apoptosis 1 (p53-inducible cell-survival factor) (p53csv) (A9ULB4)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. The triap1:prelid1 complex probably functions as a phosphatidic acid (PA) transporter across the mitochondrion intermembrane space to provide PA for cardiolipin CL synthesis in the inner membrane. Likewise, the triap1:prelid3a complex mediates the transfer of phosphatidic acid (PA) between liposomes (in vitro) and probably functions as a PA transporter across the mitochondrion intermembrane space (in vivo). Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis (By similarity). Required for pronephros development; probably involved at an early stage in the formation of pronephric components derived from the somatic layer.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:O43715}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O43715}.
Interaction partners:
- PRELI domain-containing 1
- Signal recognition particle 14 kDa protein
- Diacylglycerol kinase.
Sequence:
MNSVGEECTDMKREYDQCFNRWFAEKFLKGECSGDPCTELFRRYRDCVQKAIKDKDIPVDGVDFMGPSKSKTESDGSS
Protein: Abasic site processing protein HMCES (EC 4.-.-.-) (Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein) (ES cell-specific 5hmC-binding protein) (Peptidase HMCES) (EC 3.4.-.-) (SRAP domain-containing protein 1) (Q96FZ2)
Organism: Homo sapiens (Human)
Function: Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Acts as an enzyme that recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue. The HMCES DNA-protein cross-link is then degraded by the proteasome. Promotes error-free repair of abasic sites by acting as a 'suicide' enzyme that is degraded, thereby protecting abasic sites from translesion synthesis (TLS) polymerases and endonucleases that are error-prone and would generate mutations and double-strand breaks. Has preference for ssDNA, but can also accommodate double-stranded DNA with 3' or 5' overhang (dsDNA), and dsDNA-ssDNA 3' junction. Also involved in class switch recombination (CSR) in B-cells independently of the formation of a DNA-protein cross-link: acts by binding and protecting ssDNA overhangs to promote DNA double-strand break repair through the microhomology-mediated alternative-end-joining (Alt-EJ) pathway (By similarity). Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity).
Subcellular location: Chromosome {ECO:0000269|PubMed:30554877}. Note=Recruited to chromatin following DNA damage (PubMed:30554877). Localizes to replication forks (PubMed:30554877). {ECO:0000269|PubMed:30554877}.
Interaction partners:
Sequence:
MCGRTSCHLPRDVLTRACAYQDRRGQQRLPEWRDPDKYCPSYNKSPQSNSPVLLSRLHFEKDADSSERIIAPMRWGLVPSWFKESDPSKLQFNTTNCRSDTVMEKRSFKVPLGKGRRCVVLADGFYEWQRCQGTNQRQPYFIYFPQIKTEKSGSIGAADSPENWEKVWDNWRLLTMAGIFDCWEPPEGGDVLYSYTIITVDSCKGLSDIHHRMPAILDGEEAVSKWLDFGEVSTQEALKLIHPTENITFHAVSSVVNNSRNNTPECLAPVDLVVKKELRASGSSQRMLQWLATKSPKKEDSKTPQKEESDVPQWSSQFLQKSPLPTKRGTAGLLEQWLKREKEEEPVAKRPYSQ
Protein: Prenyl-diphosphate phosphatase (EC 3.6.1.76) (Nudix hydrolase MM_2582) (Prenyl-phosphatase) (Q8PTX6)
Organism: Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Function: Hydrolyzes homoallylic isopentenyl diphosphate (IPP), its allylic isomer dimethylallyl diphosphate (DMAPP) and short-chain prenyl diphosphates geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) to their corresponding monophosphate forms with high activity. The preferred substrate is IPP. ADP, NADPH, Ap5A and thiamine diphosphate (TPP) are weakly hydrolyzed. No hydrolysis with ATP, dNTPs, 8-OH-dGTP, NAD+, FAD or acetyl-CoA. The likely physiological role of this enzyme is to provide a substrate dimethylallyl phosphate (DMAP) for prenylated flavin mononucleotide (prenyl-FMN) synthase MM_1871 involved in the biosynthesis of prenyl-FMN, a coenzyme required in the archaea-specific mevalonate pathway.
Interaction partners:
Sequence:
MISEVDMDDNFLGLRARDEFYSGKHIHRASQLILLDPENRILLQKRSPGKFWFPNRYTYSVSGTVADESYEACIAREMLEEIGISVPFRRLFKIPCIRENKGAYHTIFSGRCSEEAASLIRHDLEEATSIEWVELEELHRAVKAEPGNYTPALREGIIKIFKEGCEKYLF
Protein: Astrocytic phosphoprotein PEA-15 (15 kDa phosphoprotein enriched in astrocytes) (B1AKZ4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEDELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA
Protein: Cyclic di-GMP binding protein VCA0042 (Q9KNC3)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: May act as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. Increasing levels of c-di-GMP lead to decreased motility (Potential). Binds bis-(3'-5') cyclic diguanylic acid (c-di-GMP) with a dissociation constant of 170 nM in the presence of 10 mM KCl and with 100 nM in its absence. Binds 1 to 2 c-di-GMP per subunit. Only 1 c-di-GMP is seen in the wild-type crystal, while 2 are seen in the mutant. Depending on the concentration of K(+) stoichiometries of 1:1, 1.43:1 and 2:1 are determined by isothermal titration calorimetry.
Subcellular location: Bacterial flagellum basal body {ECO:0000305}.
Interaction partners:
- cyclic-guanylate-specific phosphodiesterase
Sequence:
MNSRPAEKIDNNDGQTETPRSKTVSTINSTDALAMVEHSSELTLSITTPVGTKFVCRTPFIGTHTDKFLLVEMPKISADDLQYFFQEGFWMNIRAISPRGEGALIHFRSQLMHILQEPVPMAFLSIPNTMQVSQLRKEPRFELNLAGKVLFDEHRGDCELRDLSRSGCRFITPPLGKTYQVGDLVALEIFSDLRGTKTFPPLTGKICNLQRSLHHARYGLEFNEEGRNNAKNLLAQLKFNGTKLTLNAEKKA
Protein: High affinity immunoglobulin epsilon receptor subunit alpha (Fc-epsilon RI-alpha) (FcERI) (IgE Fc receptor subunit alpha) (P20489)
Organism: Mus musculus (Mouse)
Function: Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P12319}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P12319}.
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit gamma
- High affinity immunoglobulin epsilon receptor subunit beta
- Tyrosine-protein kinase SYK
- Tyrosine-protein kinase Fyn
- Mast cell carboxypeptidase A
- Chymase
- Mast cell protease 4
- Tryptase beta-2
- Tyrosine-protein kinase Lyn
- Mast cell protease 8
Sequence:
MVTGRSAQLCLALLFMSLDVILTATEKSVLTLDPPWIRIFTGEKVTLSCYGNNHLQMNSTTKWIHNGTVSEVNSSHLVIVSATVQDSGKYICQKQGLFKSKPVYLNVTQDWLLLQTSADMVLVHGSFDIRCHGWKNWNVRKVIYYRNDHAFNYSYESPVSIREATLNDSGTYHCKGYLRQVKYESDKFRIAVVKAYKCKYYWLQLIFPLLVAILFAVDTGLLLSTEEQFKSVLEIQKTGKYKKVETELLT
Protein: PspK (H2BJK0)
Organism: Streptococcus pneumoniae
Interaction partners:
Sequence:
MNNKNIIPMSLASVAILATSFVANQPVTVKAEMASTASASSAVEQAKSKVAEAEKDVSKGQEIYDEAQKKVQEKADVIRKIDEERQIINGEVQKAYLELRQAQEEKNKYPGRQEYTKKFDEANKKVDEITKKQKAKDEEYTKKMYESIPDVGPLLTKLKAEKDKLAAAKRQLEKAKVAEKTEKEAKVKKLETELDQAREKVKKQAEEDKRNYPTNTLKTLELEIAESYVKVKEAELELAKEEARELQDEDKFKQAKEKVESEKAEAKRLEELKTDRKKAAEEAKRKAEEAKQKAEEEAKRKAEEEAKRKAEEEAKRKAEEEAKRKAEEAKRKAEEEAKRKAEEEAKRKAEEEAKRKAEEAKQKAEEAKQKAEEEAKRKAEEEAKRKAEEEAKRKAEEEAKRKAEEAKRKAEEAKQKAEEAKRKAEEAKRKAEEAKQKAEEAKRKAEEEAKQKAEEAKRKAEEAKRKAEEEAKRKAEEEAKRKAEEAKRKRVDSPVFAGTSLDNTYQAPAAKKGKQELPSTGAKDNVALASLGFLGLFLGALPFVKHKN
Protein: Probable pectinesterase/pectinesterase inhibitor 39 [Includes: Pectinesterase inhibitor 39 (Pectin methylesterase inhibitor 39); Pectinesterase 39 (PE 39) (EC 3.1.1.11) (Pectin methylesterase 39) (AtPME39)] (O81415)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular location: Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Pectinesterase inhibitor 5
- Pectate lyase
- Pectate lyase
- Probable pectate lyase 3
- Probable pectate lyase 12
- Probable pectate lyase 5
- Probable pectate lyase 13
Sequence:
MINNHPIREKPKHIIFNLLSLIFFLIFLSTVVSSQSPSYTTHKTQRLTETKTIPELIIADLNLTILKVNLASSNFSDLQTRLFPNLTHYERCAFEDCLGLLDDTISDLETAVSDLRSSSLEFNDISMLLTNVMTYQDTCLDGFSTSDNENNNDMTYELPENLKEIILDISNNLSNSLHMLQVISRKKPSPKSSEVDVEYPSWLSENDQRLLEAPVQETNYNLSVAIDGTGNFTTINDAVFAAPNMSETRFIIYIKGGEYFENVELPKKKTMIMFIGDGIGKTVIKANRSRIDGWSTFQTPTVGVKGKGYIAKDISFVNSAGPAKAQAVAFRSGSDHSAFYRCEFDGYQDTLYVHSAKQFYRECDIYGTIDFIFGNAAVVFQNSSLYARKPNPGHKIAFTAQSRNQSDQPTGISILNCRILAAPDLIPVKENFKAYLGRPWRKYSRTVIIKSFIDDLIHPAGWLEGKKDFALETLYYGEYMNEGPGANMAKRVTWPGFRRIENQTEATQFTVGPFIDGSTWLNSTGIPFSLGF