wanglab/gogpt-training-data huggingface dataset:
Protein: Ribulose bisphosphate carboxylase small subunit 1B, chloroplastic (RuBisCO small subunit 1B) (P10796)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
Subcellular location: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_00860}.
Interaction partners:
- Ribulose bisphosphate carboxylase large chain
- Phosphoribulokinase, chloroplastic
- Phosphoglycerate kinase 1, chloroplastic
- Ribulose bisphosphate carboxylase large chain, catalytic domain-containing protein
- Phosphoglycerate kinase 2, chloroplastic
- Phosphoglycolate phosphatase 1A, chloroplastic
- Phosphoglycerate kinase 3, cytosolic
- Phosphoglycolate phosphatase 2
- D-glycerate 3-kinase, chloroplastic
- Putative uncharacterized mitochondrial protein AtMg00280
Sequence:
MASSMLSSAAVVTSPAQATMVAPFTGLKSSASFPVTRKANNDITSITSNGGRVSCMKVWPPIGKKKFETLSYLPDLTDVELAKEVDYLLRNKWIPCVEFELEHGFVYREHGNTPGYYDGRYWTMWKLPLFGCTDSAQVLKEVEECKKEYPGAFIRIIGFDNTRQVQCISFIAYKPPSFTDA
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (V9HWF5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE
Protein: Protein vestigial (Q26366)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in determining which thoracic imaginal disk cells will form wings and halteres, perhaps by interacting with other nuclear regulatory proteins. When in combination with scalloped (sd), it acts as a transcriptional activation complex that regulates gene expression in the wing. Binding to sd switches the DNA target selectivity of sd. Required and sufficient for cell proliferation at the dorsal/ventral (D/V) boundary of the wing imaginal disk. Also required for cell proliferation in the wing imaginal disk, mediated via activation of E2f. By interacting with Dhfr, may control genes involved in DNA replication.
Subcellular location: Nucleus.
Interaction partners:
- Scalloped, isoform Q
Sequence:
MAVSCPEVMYGAYYPYLYGRAGTSRSFYQYERFNQDLYSSSGVNLAASSSASGSSHSPCSPILPPSVSANAAAAVAAAAHNSAAAAVAVAANQASSSGGIGGGGLGGLGGLGGGPASGLLGSNVVPGSSSVGSVGLGMSPVLSGAAGHSLHSSHRTHAHSLAHAHTHPHSHTHTHTHQTKEEDLIVPRSEAEARLVGSQQHQHHNESSCSSGPDSPRHAHSHSHPLHGGGGATGGPSSAGGTGSGGGDGGGTGAIPKNLPALETPMGSGGGGLAGSGQGQAQYLSASCVVFTNYSGDTASQVDEHFSRALNYNNKDSKESSSPMSNRNFPPSFWNSNYVHPIPAPTHHQVSDLYGTATDTGYATDPWVPHAAHYGSYAHAAHAHAAHAHAYHHNMAQYGSLLRLPQQYASHGSRLHHDQQTAHALEYSSYPTMAGLEAQVAQVQESSKDLYWF
Protein: Serpentine receptor class alpha-11 (Protein sra-11) (Q20411)
Organism: Caenorhabditis elegans
Function: A G protein-coupled receptor required for olfactory imprinting a requisite in ordorant response such as benzaldehyde and isoamylalcohol.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- LIM/homeobox protein ttx-3
- Homeobox protein ceh-10
- Homeobox protein ceh-23
Sequence:
MTTNNPVCASDAHMEMYSSKLYTSALFLNLIIATTSMILTGFAIQKLFMESIINISTRMFLFCGLMCCSLHQTAYIVLRIQVIYQVFFKLSEPCNLYYPAIDCKYVTFSLVAGNTGMIFIQSAMTIDRIFATIFPKLWPKLKYWPGVVLSILMIACNYANVQIIFWGDPLTEYVPTCGQFPSKSVNRFQTFLAIALYMSIAHMVINVIILYINVLQDRQQSKSFNVNQRYQSREALKSSQAIFFLSMSQFFACLIYSVFTKVFLEFQLNLSPLQSGLVLALSYTTPYACIAIPSLIIFTFRFIKNQRLRNINELRSQTETGDECMRKIAKIWEK
Protein: Nucleoporin 210 (Q54IS9)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Uncharacterized protein
- Nuclear pore protein
- Nuclear pore complex protein nup85
- Nuclear pore complex protein
- Uncharacterized protein
- Nucleoporin 133
- Uncharacterized protein
- Nucleoporin 155
- MAP kinase phosphatase with leucine-rich repeats protein 2
- Nuclear pore protein
Sequence:
MIIINKNNDKKSLFLLLVSLIFVLFVSNVIADTDYAISPVSLLLPYSTSKYRKPYKLEANKGCFEWINTNPDLVEITPLYESAASCSPSSNDKQQNIGAPDLSLWDNSLNQPNKKCSKAVLVSVRSGTVSERNSAFIYAEEQVTGKKLQCEVFVDRISSIVIETTTKTMYKDDLEELHVRAYDSVGNVFSSIIGLEFEWSITSGNIIQIVPFRGFPLDDVALKMEQESLQTSFVLVQGVDTGRTEINTKLTEPTYKDIQHSTTISILEPLQLNPSYLLYVIPGTQIQYQLLTKKRNILENIPLPNPNYIWSSSNSKVGKVDNSGNFMALDLGRTDLKVQHKNMSDNKVQAFVNVVHPSYLAIKIEPLKSGLGPVSNWNLIENRDYILVVELYDASGHKIHSSEITFDLNIPTEYFERLPSSQIPPNTPKRSDTFYLKAIKQGLVALKASLVKVYDLNLKKYTQLLNPISVEQEVTIHSQIQLSPPIVYLPYLPNHRQYSMIRPIGGSGEYNWYTNNSAIVTVDPTGAITSQTSSGQTEVIVVDKKNPHNRDKVLVIVLQPDEIIITPSQVEVQVGQTLKLSTQLLSKQLSKGVHFDSCNLDDLEWRVDDSNANNDNNGGGGSNQERSFSLLPLQKTNTPKKEQPDLCSTREFLAIKEGSNVISVSYMGMRAKILIFAYPPLKSDQSEILLTLGSTLNVFFSGGPEPWHLERKSHFQSIVSNLTNEQNVLSIVPGNGNSFRVTCLTHTNPSKPIGIELTIGNKVTTTNPYPASPSITIPYSCRPPASIQLQVANLPKDHQIQDSSHHQQIQQQEQQQQQQQQQSTCQDTIFSIKKQKQGEIGTYKIRNDRDIPFIAQVFDDNGKPFTNYSSLVFDWKSSDQTQAKWLRDYNQNDHLSTLSLSKEQGKVIITVSILGYDQELLRQNKIRSSDLDTSKLVSSLELHLLSSVVLFPDYYTMYLNDKNHLKIEAIGGSKNFAFTSNNSKIASLSYQPNSDFVTVIPNQQGYLKVEVRDICLGSDNNKDQQQQYQQKQQKHQQQQQSNTSPSIVQISEVHSIELDVQDMVQVGDSINLIVKGFSQNGQQFDSTQYQYMNIIPHIDNPNVLSMTQSSDSQVFTLKGLDQGLVTLSVTIQNPKTSFSATSKTIQIQVFPPFRVSPSVLHLVPGGHFQIHWTGGAPIRQDVSFVSSDPSIVNLSGREDLVGELVALKVGEATIKAIAQIVDPITGKKTIIGEDKLMVYVKNMTGIRIHSSINKILVGNEAKLRVVGANGETPFTYGTVDLFFKWECLDSNIATLLPIYERANTTVEAEGSFSVRVMGKNAGSTSITVWAYSGGDKTKHLFQAASLQINVIPDIPIQTTSLLLPLNTPSSFIVNNHLDKTGIEFYPLMDGHGSSSCKDVIDIGDNKIVSLDKIGTCYVSAVRDGRMDTSKLFKINSKPFSHLELLPINPTSTVIPIGGSMSFAIYLRDDIGEVFTEYGSSAIFSSEVSNTGIISSSIDANVVTIKGIRAGLVTLHVYLKDMPHLDDYIKIFVGRLVEPHQPILHVGSMITFSIAKDQLEQRGFSLPSSDEKVWSSGDPSILQVDPITGKATAIAAGTTTINYIRNPSSQTQVVISKIGRIKVDFSDQIINNSKKRYEYNLKFFTAGSDIELSQDSTIDQNIKGICTIKESTFATAFFEKVKGKEQYRCVVQPSGVATSSIDKVTLYVEVSNAHKTYQYDTTINLPFESTFSIINVRDNKIQLSPRQSTFILNIQSSSPIFVESSDNSLLSVQQISSSGGDDQLNNLYKYAIQPMSVSTSFQNVPLLISSADGKSKTTVTVSYSKSGSTTSDQNTSYVESSTINSHPFLFSFIIIVGTLLIGLYASKKHNDKPRVYINPNSNLQTSSISSPYRTPPPHSFTSPNRSTYGSSSIYLNN
Protein: Glutamate decarboxylase alpha (GAD-alpha) (EC 4.1.1.15) (P69908)
Organism: Escherichia coli (strain K12)
Function: Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria.
Interaction partners:
- Glutamate decarboxylase beta
- Glutamate/gamma-aminobutyrate antiporter
- Protein HdeD
- Acid stress chaperone HdeA
- Glutaminase 1
- Transcriptional regulator GadE
- Outer membrane protein Slp
- Acid stress chaperone HdeB
- 4-aminobutyrate aminotransferase GabT
- HTH-type transcriptional regulator GadX
Sequence:
MDQKLLTDFRSELLDSRFGAKAISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKLGPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVVMRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT
Protein: Protein mmf1, mitochondrial (Isoleucine biosynthesis and maintenance of intact mitochondria 1) (Maintenance of mitochondrial function 1) (O43003)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in the maintenance of mitochondrial DNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12185840}. Cytoplasm {ECO:0000269|PubMed:12185840}.
Interaction partners:
- Adenine phosphoribosyltransferase
- Putative endonuclease C1F12.06c
- Altered inheritance of mitochondria protein 19 homolog
- Putative 2-hydroxyacid dehydrogenase UNK4.10
Sequence:
MLRALGSRLLVASRPAAYRSFQQSLRPVPRFFIHKMSTKTPINSPKLSSAGPYNQAIKANGVIYCSGQIPVANGKVIEGTVGDQTRQCLLNLQEVLTEAGSSLNKIVKVNIFLADMDDFAAVNKVYTEVLPDPKPARSCVAVKTVPLSTQGVKIEIECIALE
Protein: Ferroxidase HEPHL1 (EC 1.16.3.1) (Hephaestin-like protein 1) (Q6MZM0)
Organism: Homo sapiens (Human)
Function: Is a copper-binding glycoprotein with ferroxidase activity. It oxidizes Fe(2+) to Fe(3+) without releasing radical oxygen species. May be involved in the regulation of intracellular iron content.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Lactadherin
Sequence:
MPRKQPAGCIFLLTFLGLSGLVGTVTRTYYIGIVEEYWNYVPQGKNVITGKSFTEDKLATLFLERGPNRIGSIYKKAVYRRFTDGTYSIEIPKPPWLGFLGPILRAEVGDVIVIHLKNFASRPYSLHPHGVFYNKDSEGALYPDGTSGRNKNDDMVPPGKNYTYVWPVREEYAPTPADANCLTWVYHSHIDAPKDICSGLIGPLLVCKEGILNRYSGTRNDVDREFVIMFTLVDENQSWYLNENIKHFCTNPDSVDKKDAVFQRSNKMHALNGYLFGNFPEPDMCVGESVSWHLFGMGNEIDIHSIYFYGNTFISRGHRTDVVNLFPATFLTTEMIAENPGKWMITCQVSDHLQAGMLGQYNVDNCKSDIFYPKMKGQQRRYFIAAEKILWDYAPQGYNKFSGLPLNASGSDSDLYFTQGDNRIGGKYWKVRYTEFVDATFTKRKRLSAEEAHLGILGPVIKAEVGDTLLVTFANKADKVYSILPHGVIYDKASDAAPNLDGFVKPGAHVKPGETFTYKWTVPESVSPTAGDPPCLTYLYFSAVDPIKDTSSGLVGPLLVCKKGVLNADGTQKGIDKEFYLLFTVFDENLSRYFDENIQKFIWHPFSIDKEDKEFVKSNRMHAVNGYMYGNQPGLNMCKRDRVSWHLIGLGTDTDMHGIVFQGNTIHLRGTHRDSLALFPHMATTAFMQPDHAGIFRVFCATMPHLSRGMGQIYEVSSCDNRDPSEQRYGMIRTFYIAAEEVEWDYAPNKNWEFEKQHVDARGERHGDIFMNRTENWIGSQYKKVVYREYTDGEFVEIKARPPREEHLELLGPMIHAEVGNTVLIIFKNKASRPYSISAQGVEEMDSGKQFQVPMTKPGEVKTYRWNIPKRSGPGPSDPNCIPWVYYSTVNFVKDTYSGLMGPLITCRKGVLNEKGRRSDVDYEFALLFLVFNENESWYLDDNIKKYLNKDPRDFKRTDDFEESNRMHAINGKIFGNLHGLIMNEDTMTNWYLLGIGSEVDIHTIHYHAESFLFKIDKSYREDVYDLFPGTFQTIELFADHPGTWLLHCHVSDHIHAGMETTYTVLRNIDNRIPYSTTSPGVASHPATVPSNERPGKEQLYFFGKNLGPTGAKAALVILFIIGLLLLITTVILSLRLCSAMKQTDYQQVQSCALPTDAL
Protein: Polycomb group protein EMF2B (OsEMF2B) (Polycomb group protein EMBRYONIC FLOWER 2B) (Q69KN0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They act via the methylation of histones, rendering chromatin heritably changed in its expressibility (Probable). Polycomb group (PcG) protein involved in the repression of flowering under long day (LD) conditions. Regulates floret development.
Interaction partners:
- Polycomb group protein FIE1
- Polycomb group protein FIE1
- Histone-lysine N-methyltransferase CLF
- Histone-lysine N-methyltransferase EZ1
- Probable lysine-specific demethylase SE14
- Histone-binding protein MSI1
- Os06g0275250 protein
- Os02g0708500 protein
- Os02g0708600 protein
- Os03g0640201 protein
Sequence:
MCRHQPRARLSPDEQLAAEESFALYCKPVELYNIIQRRSIKNPAFLQRCLLYKIHARRKKRSLITISLSGGTNKELRAQNIFPLYVLLARPTNNVSLEGHSPIYRFSRACLLTSFHEFGNKDYTEATFVIPDVKNLATSRACSLNIILISCGRAEQTFDDNNCSGNHVEGSTLQKLEGKCFWGKIPIDLLASSLGNCVSLSLGHTVEMSSTVEMTPSFLEPKFLEDDSCLTFCSQKVDATGSFQLQVSISAQEAGAKDMSESPYSVYSYNDVPPSSLTHIIRLRSGNVLFNYKYYNNTMQKTEVTEDFSCPFCLVPCGSFKGLGCHLNASHDLFHYEFWISEECQAVNVSLKTDSWRTELLAEGVDPRHQTFSYRSRFKKRKRVEISSDKIRHVHPHIVDSGSPEDAQAGSEDDYVQRENGSSVAHASVDPANSLHGSNLSAPTVLQFGKTRKLSVERADPRNRQLLQKRQFFHSHRAQPMALEQVFSDRDSEDEVDDDIADFEDRRMLDDFVDVTKDEKLIMHMWNSFVRKQRVLADGHIPWACEAFSQFHGQELVQNPALLWCWRFFMVKLWNHSLLDARAMNACNTILEGYLNGSSDPKKN
Protein: PDZ and LIM domain protein 5 (Enigma homolog) (Enigma-like PDZ and LIM domains protein) (Q8CI51)
Organism: Mus musculus (Mouse)
Function: May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Isoforms lacking the LIM domains may negatively modulate the scaffolding activity of isoform 1. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May be required to restrain postsynaptic growth of excitatory synapses. Isoform 1, but not isoform 2, expression favors spine thinning and elongation.
Subcellular location: Postsynaptic density {ECO:0000250|UniProtKB:Q62920}. Presynapse {ECO:0000250|UniProtKB:Q62920}. Postsynapse {ECO:0000250|UniProtKB:Q62920}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q62920}. Note=Detected both at presynaptic and postsynaptic sites, exclusively at excitatory synapses, but not inhibitory synapses, in hippocampal neurons. {ECO:0000250|UniProtKB:Q62920}.
Interaction partners:
Sequence:
MSNYSVSLVGPAPWGFRLQGGKDFNMPLTISSLKDGGKASQAHVRIGDVVLSIDGISAQGMTHLEAQNKIKACTGSLNMTLQRASAAAKSEPVSVQKGEPKEVVKPVPITSPAVSKVTSTTNMAYNKAPRPFGSVSSPKVTSIPSPSSAFTPAHAATSSHASPTPVAAATPLHLSASGLHVSANLSADQCSSPPNTGKPAVNVPRQPTVTSVCSESAQELAEGQRRGSQGDIKQQNGPPRKHIVERNTEFYHIPTHSDASKKRLIEDTEDWRPRTGTTQSRSFRILAQITGTEHLTESENDNTKKANSTQEPSQQPASSGASPLSASEGPESPGSSRPSVAGLRSAAAFKPVGSTSVKSPSWQRPNQAAPSTGRISNNARSSGTGASVGPPQPSDQDTLVQRAEHIPAGKRTPMCAHCNQVIRGPFLVALGKSWHPEEFNCAHCKNTMAYIGFVEEKGALYCELCYEKFFAPECGRCQRKILGEVINALKQTWHVSCFVCVACGKPIRNNVFHLEDGEPYCETDYYALFGTICRGCEFPIEAGDMFLEALGYTWHDTCFVCSVCCESLEGQTFFSKKDKPLCKKHAHSVNF
Protein: Eukaryotic translation initiation factor 3 subunit G (eIF3g) (Eukaryotic translation initiation factor 3 RNA-binding subunit) (eIF-3 RNA-binding subunit) (Eukaryotic translation initiation factor 3 subunit 4) (Q9FI86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03006}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit K
Sequence:
MAIDTIQKTKKLRWGEIDEEEGDYDFLLPPKQMISPDQNGVKKVIEYKFNEEDKKVKITTTTRVQKRALTKQAVERRSWNKFGDAAHEESSSYLTMRSTEDIILERIRAPGSNAEQSTVSGDSMSQLGKPGAVLMVCRLCQKKGDHWTSRCPQKDLLSLMDEPLTAETSTSTITGTGRAAYVPPSMREGADRKAGGSDMRSRHDENSVRVTNLSEDTRGPDLMELFRPFGAVTRCHVAIDQKTSMSRGFGFVSFVSREDAQRAINKLNGYGYDNLILRVEWSTPKTQLDPFSFADYNNLCKLLNICHS
Protein: Angiomotin C-terminal domain-containing protein (A0A8C0SSK1)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
MRNSEEQPSGGTTVLQRLLQEQLRYGNPNENRNLLAIHQQATGNGPPFPSSSGNPGPQNDVLSPQDHHQQLVAHAARQEPQGQEIQAENIIMEKQLSPRMQNNEELPTYEEAKVQSQYFRGQQHASVGAAFYVTGVTNQKMRTEGRPSVQRLNPGKMHQDEGLRDLKQGHVRSLSERLMQMSLATSGVKAHPPVTSAPLSPPQPSDLYKTPTSSSEFYKAQGPPPSQHSLKGMEHRGPPPEYPFKGMPPQSVVCKPQEAGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARPAQDISLPLSARSSRPHSPTSSLTSGGSLSLLQSPPATRLSPAQHPLAPNQGDHSAHLPRPQQHFLPTPAHQSDHYRLPQPGLSQPPPQQHHHHHHQQQPGEAYSAMPRAQQSSASYQPMPADPFAIVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQKEKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNATALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAKSLMSISNAGSGLLSHSSTLTGTPIMEEKRDDKSWKGSLGILLGGDYRVESVPSTPSPVPPSTPLLSAHSKTGSRDCSTQTERGTEPNKTAAVAPISVPMPAASAAAAATITANAATNTATAATTTTTMVAAAPVAVAAAAAPAATASAPSPAAATALAATAVSSAPATPILAAASAAAAAAAAAAAAVAPTAAVQVASAAPAPLPASATAPVLAPQASQASASAPTQAPTPAPAAASPPAPAPAPAPALAPAEASSSPAASSGSRRLSIPSVTCSPDKTDGPVFHSNTLERKAPIQLLGQEPDAEMVEYLI
Protein: Tumor necrosis factor receptor superfamily member 18 (Glucocorticoid-induced TNFR-related protein) (CD antigen CD357) (O35714)
Organism: Mus musculus (Mouse)
Function: Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway (By similarity).
Subcellular location: [Isoform A]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform B]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform C]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform D]: Secreted.
Interaction partners:
- Tumor necrosis factor ligand superfamily member 18
- Forkhead box protein P3
- Cytotoxic T-lymphocyte protein 4
- T-lymphocyte activation antigen CD80
- T-lymphocyte activation antigen CD86
- Inducible T-cell costimulator
- T-cell surface glycoprotein CD4
- Hepatitis A virus cellular receptor 2 homolog
- CD27 antigen
- Tumor necrosis factor receptor superfamily member 5
Sequence:
MGAWAMLYGVSMLCVLDLGQPSVVEEPGCGPGKVQNGSGNNTRCCSLYAPGKEDCPKERCICVTPEYHCGDPQCKICKHYPCQPGQRVESQGDIVFGFRCVACAMGTFSAGRDGHCRLWTNCSQFGFLTMFPGNKTHNAVCIPEPLPTEQYGHLTVIFLVMAACIFFLTTVQLGLHIWQLRRQHMCPRETQPFAEVQLSAEDACSFQFPEEERGEQTEEKCHLGGRWP
Protein: Ankyrin repeat domain-containing protein 27 (VPS9 domain-containing protein) (VPS9-ankyrin-repeat protein) (Q3UMR0)
Organism: Mus musculus (Mouse)
Function: May be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and regulate endosome dynamics (By similarity). May regulate the participation of VAMP7 in membrane fusion events; in vitro inhibits VAMP7-mediated SNARE complex formation by trapping VAMP7 in a closed, fusogenically inactive conformation (By similarity). Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with Rab32, Rab38 and VAMP7. Involved in the regulation of neurite growth; the function seems to require its GEF activity, probably towards Rab21, and VAMP7 but not Rab32/38. Proposed to be involved in Golgi sorting of VAMP7 and transport of VAMP7 vesicles to the cell surface; the function seems to implicate kinesin heavy chain isoform 5 proteins, GOLGA4, RAB21 and MACF1. Required for the colocalization of VAMP7 and Rab21, probably on TGN sites (By similarity). Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with VPS29 (By similarity). Regulates the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes.
Subcellular location: Early endosome {ECO:0000250|UniProtKB:Q96NW4}. Late endosome {ECO:0000250|UniProtKB:Q96NW4}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q96NW4}. Lysosome {ECO:0000250|UniProtKB:Q96NW4}. Cell membrane {ECO:0000250|UniProtKB:Q96NW4}. Melanosome {ECO:0000269|PubMed:19403694}. Cytoplasmic vesicle {ECO:0000269|PubMed:19403694}. Note=Colocalizes with VAMP7 in transport vesicles in the shaft of hippocampal neurons. {ECO:0000269|PubMed:19745841}.
Interaction partners:
- Vesicle-associated membrane protein 7
- Ras-related protein Rab-32
- Vacuolar protein sorting-associated protein 29
- Ras-related protein Rab-21
- Ras-related protein Rab-38
- Vacuolar protein sorting-associated protein 35
- Large ribosomal subunit protein uL10m
Sequence:
MALYDEDLLKNPFYLALQKWRPDLCSKVAQIHGIVLVPCRGSLPGSVQASCQFESYVLVPTEGHFQTLDGKAVVIEGNRIKLGAGFACLLSVPILFEETFYNEKEESFSILCIAHPLERRETSEEPSAPADPFSLKTIEDVREFLGRHSEKFDKNIASFHRTFRECERKSLRHHIDSVNALYTKCLQQLLRDSHLKVLAKQEAQMNLMKQAVEMYVHHDIYDLIFKYVGTMEASEDAAFNKITRSLQDLQQKDIGVKPEFSFNIPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSSAKDELGYCLTSVEAAIEYIRQGSLSTKTPDAEGFGDRLFLKQRMNLLSQMTSTPIDCLFKHIASGNQKEVERLLSQDDQDKDAMQKMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEAHHLSSDRRPRPSEVPAQSPTRSVDSISQGSSTSSFSSISVSFRQEEVKKDYREVEKLLRAVADGDLEMVRYLLEWTEDDLDDVEDAISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCAEQDSKIMELLQVVPGCVASLDSVEEADHEGYVTVEIRRKWNPKMYNLPEEPLRRQFCLINPGGRFQERTSRETMGRDRSVPDLAGRSLQEPEKQRVTGKQSDLSDLSRYQTSEEGNKGLPERPVSRQAAPGHRPMVRRHTVNDAAILQVPEVTVHLTTHEASVPQS
Protein: Probable xyloglucan endotransglucosylase/hydrolase protein 6 (At-XTH6) (XTH-6) (EC 2.4.1.207) (Q8LF99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues (By similarity).
Subcellular location: Secreted, cell wall {ECO:0000305}. Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Glucan endo-1,3-beta-glucosidase 1
- Vacuolar protein sorting-associated protein 29
- At1g49750
Sequence:
MAKIYSPSFPGTLCLCIFTLLTLMFIRVSARPATFVEDFKAAWSESHIRQMEDGKAIQLVLDQSTGCGFASKRKYLFGRVSMKIKLIPGDSAGTVTAFYMNSDTATVRDELDFEFLGNRSGQPYSVQTNIFAHGKGDREQRVNLWFDPSMDYHTYTILWSHKHIVFYVDDVPIREYKNNEAKNIAYPTSQPMGVYSTLWEADDWATRGGLEKIDWSKAPFYAYYKDFDIEGCPVPGPTFCPSNPHNWWEGYAYQSLNAVEARRYRWVRVNHMVYDYCTDRSRFPVPPPECRA
Protein: DEAD-box ATP-dependent RNA helicase 52 (EC 3.6.4.13) (Q9M2F9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein STABILIZED1
- Cell division cycle 5-like protein
- Polyadenylate-binding protein 4
- 110 kDa U5 small nuclear ribonucleoprotein component CLO
- Tetraspanin-8
- 109 kDa U5 small nuclear ribonucleoprotein component GFL
- Annexin D2
- Polyadenylate-binding protein 2
- DExH-box ATP-dependent RNA helicase DExH16, mitochondrial
- RNA helicase
Sequence:
MSSNSWADVSESERAPSGGGWGYSRPSRTNYVPPHLRSRTPSSEFVAPSPGNNDRGGYGGANSGYGGRGQGYGGRGSGYGGRGGPVGGWNARSGGWDRRDTETNPFGNDGNADPAVNEQENTVINFEAYEDIPIETSGDNVPPPVNTFAEIDLGEALNLNIQRCKYVKPTPVQRNAIPILAAGRDLMACAQTGSGKTAAFCFPIISGIMKDQHIERPRGVRGVYPLAVILSPTRELACQIHDEARKFSYQTGVKVVVAYGGTPVNQQIRELERGVDILVATPGRLNDLLERGRVSLQMVRFLALDEADRMLDMGFEPQIRKIVQQMDMPPPGVRQTMLFSATFPREIQRLASDFLSNYIFLAVGRVGSSTDLIVQRVEFVHDSDKRSHLMDLLHAQRENGNQGKQALTLVFVETKKGADSLENWLCINGFPATTIHGDRSQQEREVALRSFKTGRTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGNSGLATAFFNDNNTTMAKPLAELMQEANQEVPDWLTRYASRASFGGGKNRRSGGRFGGRDFRRESFSRGGGGADYYGGGGGYGGVPGGGYGAMPGGYGPVPGGGYGNVPGGGYAPYGRGGGAYYGPGGYGTVPNQGYGPGVASAWD
Protein: Ubiquitin-conjugating enzyme E2 K (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme K) (Huntingtin-interacting protein 2) (HIP-2) (Ubiquitin carrier protein) (Ubiquitin-conjugating enzyme E2-25 kDa) (Ubiquitin-conjugating enzyme E2(25K)) (Ubiquitin-conjugating enzyme E2-25K) (Ubiquitin-protein ligase) (P61085)
Organism: Bos taurus (Bovine)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53 (By similarity). Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1.
Subcellular location: Cytoplasm.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ring finger protein 38
- Ring finger protein 44
- Polyubiquitin-C
- Polyubiquitin-B
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-like modifier-activating enzyme 6
- Ubiquitin-conjugating enzyme E2 variant 2
- Ubiquitin like modifier activating enzyme 7
Sequence:
MANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN