wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein kinase-interacting protein (Tip) (P22575)
Organism: Saimiriine herpesvirus 2 (strain 488) (SaHV-2) (Herpesvirus saimiri)
Function: Plays a critical role in virus induced T-cell transformation. Binds to T-cell-specific tyrosine kinase LCK SH2 and SH3 domains, thereby activating its kinase activity. Once phosphorylated by host LCK, forms a complex with at least STAT 1 and 3, resulting on the phosphorylation of STAT3 and presumably STAT1, and their migration into the nucleus to induce transcription of target genes. Stimulates host ILF3/NF-AT-90 activity. Association with host NXF1/TAP transduces the signal up-regulating surface expression of adhesion molecules as well as activating NF-kappa-B activity. Acts synergistically with StpC to stimulate NF-kappa-B activity and interleukin-2 gene expression. Activation of NF-kappa-B protects lymphocytes from apoptosis, thereby facilitating viral induced cell transformation. May cause down-regulation of host LCK and cell apoptosis when stably overexpressed ex vivo. Interaction with WDR48 induce degradation of T-cell receptor in a lysosome-dependent fashion, when both proteins are overexpressed. The biological effect of this interaction remains controversial since no T-cell receptor degradation is observed in infected cells.
Subcellular location: Host cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MANEGEEIELTEFPETEKERKDEEKLSSCSEETTNTSSSSGSDHVPVPIEVNVIIQNSSRTEDELQNSKEIELTGFQGKLSSCSEETTAPSSSYSSKQASVFIEENGDNETSTYRPQNVLTNLNSLYTTFEDARAQGKGMVRHKSEDLQSFLEKYPPDFRKPKRDLSATWDPGMPTPPLPPRPANLGERQASTVRLHVKESNCKQPRERKANERNIVKDLKRLENKINVIICLVVVILAVLLLVTVLSILHIGMKS
Protein: DNA-directed RNA polymerase subunit omega (RNAP omega subunit) (EC 2.7.7.6) (RNA polymerase omega subunit) (Transcriptase subunit omega) (P0A800)
Organism: Escherichia coli (strain K12)
Function: Promotes RNA polymerase (RNAP) assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- RNA polymerase sigma factor RpoD
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta'
- RNA polymerase-associated protein RapA
- Transcription termination/antitermination protein NusG
- Small ribosomal subunit protein uS2
- Transcription termination/antitermination protein NusA
- RNA polymerase-binding transcription factor DksA
- Guanylate kinase
Sequence:
MARVTVQDAVEKIGNRFDLVLVAARRARQMQVGGKDPLVPEENDKTTVIALREIEEGLINNQILDVRERQEQQEQEAAELQAVTAIAEGRR
Protein: Myosin 28B1, isoform C (EC 5.6.1.8) (Q8IPH7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDAGYSPRKGEYVWVKPQNTTSEFAVPFGARIVRTEKTQTLVCDDRNKQFWVPAGDVLKAMHITSQEDVEDMITLGDLQEYTILRNLQNRYAKQLIYTYTGSMLVAINPYQILPIYTNREIQLYRNKSLAELPPHIFAISDNAFQRLQRLKENQCVVISGESGAGKTESTKLILQYLAAISGKHSWIEQQIIEANPIMEAFGNAKTVRNDNSSRFGKYIEIRFTPQGAIQGARIQQYLLEKSRIVFQSRDERNYHIFYCMLAGLSTAERERLKLQEQSPSQYHYLAQGGCFTLPGRGDAKDFADIRAAMKVLSFKPEEVWSILSLLAAILHLGNLRFTATEVANLATAEIDDTPNLQRVAQLLGIPISALNAALTQRTIFVHGEHVTTSLSKEAAIEGRDAFVKSLYDGIFVRIVRRINETINKQVDQPMNSIGVLDIFGFENFDNNSFEQLCINYANENLQQFFVGHIFKMEQDEYQNEHINWQHIEFQDNQQILDLIGMKPMNLMSLIDEESKFPKGTDQTLLEKLHVQHGNRSIYVKGKTTQTSLFGIRHYAGVVMYNPLGFLEKNRDSFSGDLRTLVQRSTNKYLVDIFPHEMPMDTAKKQPTLCVKFRNSLDMLMRTLSQAHPYFIRCIKPNEYKEPKNFDKELCVRQLRYSGMMETARIRRAGYPIRHAYRAFVERYRLLVPPVGPLEQCDCRKLARQICEVALPADSDRQYGKTKLFLRDEDDASLELQRSQLMLKSIVTIQRGIRRVLFRRYMKRYREAIITVQRYWRGRLQRRKYQVMRQGFHRLGACIAAQQLTTKFTMVRCRTIKLQALSRGYLVRKDFQKKLLERRKQNQLKKEELLKLAKMKEAEELLRLQQLKEQKEREQREQQEKRLQEEQRLKAEAAARNALAMAAVQQKRRTKPVKQEAPKAPTLQARNSLPPPPTTLIVAAPLPTRPASAVTRINTIPESPGTIDVESSKQMVDDVFRFLNDEPDVSGPLGPNVKEKSMMFEQALRLRRDVPTKLLSRPVNYYEAAPRKIVNQTRL
Protein: mRNA-capping enzyme subunit alpha (GTP--RNA guanylyltransferase) (GTase) (mRNA guanylyltransferase) (EC 2.7.7.50) (P40997)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.
Subcellular location: Nucleus.
Interaction partners:
- mRNA-capping enzyme subunit beta
- Transcription elongation factor spt5
- mRNA cap guanine-N
- DNA-directed RNA polymerase II subunit rpb1
- SAGA complex subunit Sgf73
- Uncharacterized mitochondrial carrier C19G12.05
- Anthranilate phosphoribosyltransferase
- Probable prephenate dehydrogenase [NADP
- Nuclear cap-binding protein subunit 2
- Pyrroline-5-carboxylate reductase
Sequence:
MAPSEKDIEEVSVPGVLAPRDDVRVLKTRIAKLLGTSPDTFPGSQPVSFSKKHLQALKEKNYFVCEKSDGIRCLLYMTEHPRYENRPSVYLFDRKMNFYHVEKIFYPVENDKSGKKYHVDTLLDGELVLDIYPGGKKQLRYLVFDCLACDGIVYMSRLLDKRLGIFAKSIQKPLDEYTKTHMRETAIFPFLTSLKKMELGHGILKLFNEVIPRLRHGNDGLIFTCTETPYVSGTDQSLLKWKPKEMNTIDFMLKLEFAQPEEGDIDYSAMPEFQLGVWEGRNMYSFFAFMYVDEKEWEKLKSFNVPLSERIVECYLDDENRWRFLRFRDDKRDANHISTVKSVLQSIEDGVSKEDLLKEMPIIREAYYNRKKPSVTKRKLDETSNDDAPAIKKVAKESEKEI
Protein: Reduction in Cnn dots 1, isoform G (EC 3.-.-.-) (A0A0B4KFM5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKESGSVSKNQPQTSEARGSIITYSPSKFLTSVGTGRTTYSTHTHTTTATSAATTATKTNNLPMGGSSAAYYVVKAGSLGSAASMSGCIKVSSPPKGPPMAKSPALVVTSPCTPTESSSTISAPSESSFSEKMEHSYMRDTPVRSDVHNGLTPARNILVRHPPQCPSCHTYPPQHEELSEIQQAHVPPYDEVVAKEAMNECARIAKYVKNNNSDEQDWVARVNKFNWTPMQEMVFEKVCSILDQDQLARLANDKRQHEPIHRRISSDKSASRFRKLLASVAWESRITQWIHALLMEHLSPSYMASYLEILQTLKTKLPTLVDKMLFGRPLNNSQELLAPVMKKRWEPNIMPKSRQLTHNAIMVVLPNMPTTGTVSDRMQKWYQALSTITQVVQISLPNTNNRIGNQNLDHVAETIVSITRVKINELRTENPSRGIILVGFNAGAALALQVALSESVACVVCMGFAYNTIRGPRGTPDDRMLDIKAPILFVIGQNSARTSQEEMEGLRERMQSESSLVVVGSADDALRVPKSKRRIEGVTQSMVDYMVVEEIFEFVNRTLSNPPGPRMPTCLMHQQGYQRLPKQSPHILADGNANKAVQQMRKRKMDGGLDDSMGQPSKTKFVPHIGRPRTRPLPNVGGSARSVSQKGAPHPDQPKLSGEEPNQSIEFILDDAQDYGDAQTTAGGSASLPKVITPGVLGKQLPPVNLAAGTKIKMIPSSQFVQIKSLPSQSKLINYTLNKPSVGTSSTANIGSVVKTLPCSSVSGQQIITLKTPSGQTQQFATAATSTGAAGSSTSTGTGQKKYTVFKNANGMTMLHLTKSVPTTGSSSGSANMDLSNIIDMPIVFADNEGNIPEHQQADKDIKPAPIRSANKSPLIISQKIIKEANKPSGMVTSGSITAVSKPGNIVLNKGLQQLLNSSPGGTLATQNKVVYLNRSTIKPMGNVAPGTHRVPIRIVSTPNTGGAVTTTASSSPIMVDPATGSKVAKTVNVQTIKPTGSVLAQGTIRQAGNVGTKSYLQMINTAPGASKTVAGDGKGSVRNIYFKSATGLKQLPVQMLGNRIPGGAVISSTASASSGSPGLRRVVNIGPVSKVTATSTTSSSIAATLTHNKM
Protein: Vesicular glutamate transporter 1 (VGluT1) (Brain-specific Na(+)-dependent inorganic phosphate cotransporter) (Solute carrier family 17 member 7) (Q9P2U7)
Organism: Homo sapiens (Human)
Function: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter which transports preferentially L-glutamate but also phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells (By similarity). The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane (By similarity). In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification (By similarity). Moreover, may function as a K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular glutamate uptake (By similarity). The vesicular K(+)/H(+) antiport activity is electroneutral (By similarity). At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Is necessary for synaptic signaling of visual-evoked responses from photoreceptors (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q3TXX4}. Cell membrane {ECO:0000305|PubMed:10820226}; Multi-pass membrane protein {ECO:0000305}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q3TXX4}.
Interaction partners:
- Vesicular inhibitory amino acid transporter
- Vesicular acetylcholine transporter
- Disks large homolog 4
- Synaptic vesicular amine transporter
- Synaptotagmin-1
- Vesicle-associated membrane protein 2
- Chromaffin granule amine transporter
- Vesicular glutamate transporter 2
- Vesicular glutamate transporter 3
- Ras-related protein Rab-3A
Sequence:
MEFRQEEFRKLAGRALGKLHRLLEKRQEGAETLELSADGRPVTTQTRDPPVVDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVSMVNNSTTHRGGHVVVQKAQFSWDPETVGLIHGSFFWGYIVTQIPGGFICQKFAANRVFGFAIVATSTLNMLIPSAARVHYGCVIFVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTAFCGSYAGAVVAMPLAGVLVQYSGWSSVFYVYGSFGIFWYLFWLLVSYESPALHPSISEEERKYIEDAIGESAKLMNPLTKFSTPWRRFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFEISKVGLVSALPHLVMTIIVPIGGQIADFLRSRRIMSTTNVRKLMNCGGFGMEATLLLVVGYSHSKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPIIVGAMTKHKTREEWQYVFLIASLVHYGGVIFYGVFASGEKQPWAEPEEMSEEKCGFVGHDQLAGSDDSEMEDEAEPPGAPPAPPPSYGATHSTFQPPRPPPPVRDY
Protein: Beta-alanyl-bioamine nonribosomal peptide synthetase ebony (EC 6.3.2.-) (N-beta-alanyldopamine synthase) (NBAD-synthase) (Protein ebony) (Q9VDC6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Nonribosomal peptide synthase which is required for the regulation of histamine and dopamine levels in various tissues through their condensation with beta-alanine. In epithelial glial cells, plays an essential role in the inactivation of histamine, the main neurotransmitter in the optical nerve system, by catalyzing the conversion of histamine into carcinine. In the cuticle, catalyzes the condensation of beta-alanine with dopamine to form beta-alanyl-dopamine (NBAD), a metabolite involved in the pigmentation and sclerotization of the insect cuticle. Also, regulates the cuticular hydrocarbon composition in females. Acts downstream of the body clock to regulate circadian behavioral rhythms. Can also condense beta-alanine with biogenic amines tyramine, octopamine, and serotonin in vitro.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11934851, ECO:0000269|PubMed:12205712, ECO:0000269|PubMed:19715698}. Note=In glial cells, localizes to thin sheets of cytoplasm enwrapping the cartridge elements of photoreceptor R1-R6 terminals, extending between their profiles, but not into their capitate projections. {ECO:0000269|PubMed:12205712}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- Aromatic-L-amino-acid decarboxylase
- Straw, isoform E
- FI23334p1
- Protein-cysteine N-palmitoyltransferase Rasp
- Arylalkylamine N-acetyltransferase 1
- Tyrosine 3-monooxygenase
- LP03067p
- Carcinine transporter
- Uncharacterized protein, isoform B
Sequence:
MGSLPQLSIVKGLQQDFVPRALHRIFEEQQLRHADKVALIYQPSTTGQGMAPSQSSYRQMNERANRAARLLVAETHGRFLQPNSDGDFIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAGRFQGTPTLSTTELYAKSLQLAGSNLLSEEMLRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFKTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGVHRLYNFYGSTEVLGDVTYFACESKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRDPERFLENPLAVEKKYARLYRTGDYGSLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTEMQMEARLKDKLADYMTPQVVILEHVPLLVNGKVDRQALLKTYETANNNEGDSSIVLDFDYSQVPEDLKLTARDLFETVGGVIGRSTRATLAPHSNFYELGGNSLNSIFTVTLLREKGYNIGISEFIAAKNLGEIIEKMAANHDAVQLEEESLNACPHLKMEAVPLRLEHRQEVIDIIVASFYNKADLEQWLKPGVLRTDYSDILNDIWNVLVERDLSFVVYDTNTDRIIGTALNFDARNEPEVDIKSKLLIVFEFLEFCEGPIRDNYLPKGLNQILHSFMMGTAEKLNPRENIACMHFMEHEVLRVAREKQFAGIFTTNTSPLTQQLADVYHYKTLLNFQVNEYVHSDGSRPFGDAPDEQRAIVHWKEVGK
Protein: Mitogen-activated protein kinase 8 (AtMPK8) (MAP kinase 8) (EC 2.7.11.24) (Q9LM33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: MKK3-MPK8 and CAMs-MPK8 modules negatively regulates ROS accumulation through controlling expression of the RBOHD gene during wounding.
Interaction partners:
- Calmodulin-7
- Calmodulin-1
- Calmodulin-6
- Mitogen-activated protein kinase kinase 3
- Calmodulin-2
- Calmodulin-like protein 10
- Calcium-binding protein CP1
- Calmodulin-4
- Serine/threonine-protein kinase OXI1
- Protein-tyrosine-phosphatase PTP1
Sequence:
MGGGGNLVDGVRRWLFQRPSSSSSSSSSNNNNNNHEQPIFNSSSFSSSSNPNHSANSGELIIEEDLDFSGLTLINVPKRNHLPMDPHKKGETEFFTEYGEANRYQIQEVVGKGSYGVVASAVDSHTGERVAIKKINDVFEHVSDATRILREIKLLRLLRHPDVVEIKHIMLPPSRREFRDIYVVFELMESDLHQVIKANDDLTPEHYQFFLYQLLRGLKYVHAANVFHRDLKPKNILANADCKLKICDFGLARVSFNDAPTAIFWTDYVATRWYRAPELCGSFFSKYTPAIDIWSVGCIFAEMLLGKPLFPGKNVVHQLDLMTDFLGTPPPESISRIRNEKARRYLSSMRKKQPVPFSHKFPKADPLALRLLERLLAFDPKDRASAEDALADPYFSGLSNSEREPTTQPISKLEFDFERKKLVKDDVRELIYREILEYHPQMLEEYLRGGDQLSFMYPSGVDRFKRQFAHLEENQGKPGAAGGGRSTALHRHHASLPRERVPAPNGETAEESSDVERRAAAAVASTLESEEADNGGGYSARNLMKSASISGSKCIGVQSKTDKEDTIAEEEDNETVAELTDKVASLHNS
Protein: BTH-induced ERF transcriptional factor 3 (Q5MFV1)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLLNPASREVAALDSIRHHLLEEEEETPATAPAPTRRPVYCRSSSFGSLVADQWSESLPFRPNDAEDMVVYGALRDAFSSGWLPDGSFAAVKPESQDSYDGSSIGSFLASSSSEAGTPGEVTSTEATVTPGIREGEGEAVAVASRGKHYRGVRQRPWGKFAAEIRDPAKNGARVWLGTFDSAEEAAVAYDRAAYRMRGSRALLNFPLRIGSEIAAAAAAAAAGNKRPYPDPASSGSSSPSSSSSSSSSSSSGSPKRRKRGEAAAASMAMALVPPPPPPAQAPVQLALPAQPWFAAGPIQQLVS
Protein: DnaJ homolog subfamily C member 11 (Q9NVH1)
Organism: Homo sapiens (Human)
Function: Required for mitochondrial inner membrane organization. Seems to function through its association with the MICOS complex and the mitochondrial outer membrane sorting assembly machinery (SAM) complex.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25997101}. Note=Isoforms show differential submitochondrial localization. A 57 kDa form (potentially isoform 3) shows either mitochondrial matrix or innermembrane (IM) localization, possibly anchored to the IM facing the matrix. A 35 kDa form behaved either as an inner membrane space (IMS) or an IM protein exposed to the IMS. {ECO:0000269|PubMed:25111180}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion outer membrane {ECO:0000269|PubMed:25111180}; Peripheral membrane protein {ECO:0000269|PubMed:25111180}.
Interaction partners:
- MICOS complex subunit MIC60
- Sorting and assembly machinery component 50 homolog
- MICOS complex subunit MIC19
- MICOS complex subunit MIC27
- MICOS complex subunit MIC26
- Stress-70 protein, mitochondrial
- Metaxin-1
- MICOS complex subunit MIC10
- Metaxin-2
- MICOS complex subunit MIC13
Sequence:
MATALSEEELDNEDYYSLLNVRREASSEELKAAYRRLCMLYHPDKHRDPELKSQAERLFNLVHQAYEVLSDPQTRAIYDIYGKRGLEMEGWEVVERRRTPAEIREEFERLQREREERRLQQRTNPKGTISVGVDATDLFDRYDEEYEDVSGSSFPQIEINKMHISQSIEAPLTATDTAILSGSLSTQNGNGGGSINFALRRVTSAKGWGELEFGAGDLQGPLFGLKLFRNLTPRCFVTTNCALQFSSRGIRPGLTTVLARNLDKNTVGYLQWRWGIQSAMNTSIVRDTKTSHFTVALQLGIPHSFALISYQHKFQDDDQTRVKGSLKAGFFGTVVEYGAERKISRHSVLGAAVSVGVPQGVSLKVKLNRASQTYFFPIHLTDQLLPSAMFYATVGPLVVYFAMHRLIIKPYLRAQKEKELEKQRESAATDVLQKKQEAESAVRLMQESVRRIIEAEESRMGLIIVNAWYGKFVNDKSRKSEKVKVIDVTVPLQCLVKDSKLILTEASKAGLPGFYDPCVGEEKNLKVLYQFRGVLHQVMVLDSEALRIPKQSHRIDTDG
Protein: Na(+)-translocating NADH-quinone reductase subunit E (Na(+)-NQR subunit E) (Na(+)-translocating NQR subunit E) (EC 7.2.1.1) (NQR complex subunit E) (NQR-1 subunit E) (Q56589)
Organism: Vibrio alginolyticus
Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00429, ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00429}.
Interaction partners:
- Na
- Na
- Na
- Na
- Na
- NADH:ubiquinone reductase
- FAD:protein FMN transferase
- Electron transport complex subunit RsxD
- Electron transport complex subunit RsxG
- Quinone oxidoreductase
Sequence:
MEHYISLLVKSIFIENMALSFFLGMCTFLAVSKKVKTSFGLGVAVVVVLTIAVPVNNLVYNLVLRENALVEGVDLSFLNFITFIGVIAALVQILEMVLDRFFPPLYNALGIFLPLITVNCAIFGGVSFMVQRDYNFAESIVYGFGSGVGWMLAIVALAGIREKMKYSDVPPGLRGLGITFITVGLMALGFMSFSGVQL
Protein: CD48 antigen (B-lymphocyte activation marker BLAST-1) (BCM1 surface antigen) (Leukocyte antigen MEM-102) (SLAM family member 2) (SLAMF2) (Signaling lymphocytic activation molecule 2) (TCT.1) (CD antigen CD48) (P09326)
Organism: Homo sapiens (Human)
Function: Glycosylphosphatidylinositol (GPI)-anchored cell surface glycoprotein that interacts via its N-terminal immunoglobulin domain with cell surface receptors including 2B4/CD244 or CD2 to regulate immune cell function and activation. Participates in T-cell signaling transduction by associating with CD2 and efficiently bringing the Src family protein kinase LCK and LAT to the TCR/CD3 complex. In turn, promotes LCK phosphorylation and subsequent activation. Induces the phosphorylation of the cytoplasmic immunoreceptortyrosine switch motifs (ITSMs) of CD244 initiating a series of signaling events that leads to the generation of the immunological synapse and the directed release of cytolytic granules containing perforin and granzymes by T-lymphocytes and NK-cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1999351, ECO:0000269|PubMed:9041467}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1999351}. Membrane raft {ECO:0000269|PubMed:12007789}. Secreted {ECO:0000269|PubMed:9418191}.
Interaction partners:
- Natural killer cell receptor 2B4
- T-cell surface antigen CD2
- Tyrosine-protein kinase Lck
- T-lymphocyte surface antigen Ly-9
- SLAM family member 6
- SH2 domain-containing protein 1A
- SLAM family member 5
- Lymphocyte function-associated antigen 3
- CAMPATH-1 antigen
- SLAM family member 7
Sequence:
MCSRGWDSCLALELLLLPLSLLVTSIQGHLVHMTVVSGSNVTLNISESLPENYKQLTWFYTFDQKIVEWDSRKSKYFESKFKGRVRLDPQSGALYISKVQKEDNSTYIMRVLKKTGNEQEWKIKLQVLDPVPKPVIKIEKIEDMDDNCYLKLSCVIPGESVNYTWYGDKRPFPKELQNSVLETTLMPHNYSRCYTCQVSNSVSSKNGTVCLSPPCTLARSFGVEWIASWLVVTVPTILGLLLT
Protein: Kel1p (Q5AB80)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Protein phosphatase regulator
- CAP-Gly domain-containing protein
- Cell division control protein 42 homolog
- Bud6p
Sequence:
MALFKLGGKLKKKDHQSDPDTTVSSSSSTNSANRKSTSRFSSILHSSAAPMPSISNQPAHTSRPPPHANLSVTTPWNRFKLFDSPFPRYRHAAASIASEKNELFLMGGLKDGSVFGDTWKIVPQINHEGDIINYVAENIEVVNNNNPPARVGHAAVLCGNAFIVYGGDTVDTDTNGFPDNNFYLFNINNHKYTIPNHILNKPNGRYGHTIGVISLNNTSSRLYLFGGQLENDVFNDLYYFELNSFKSPKATWQLVEPLNDVKPPPLTNHSMSVYKNKVYVFGGVYNNEKVSNDLWVFDAINDTWTQVTTTGDIPPPVNEHSSCVADDRMYVYGGNDFQGIIYSSLYVLDLQTLEWSSLQSSAEKSGPGPRCGHSMTLLPKFNKILIMGGDKNDYVDSDPHNFETYESFNGEEVGTMVYELDLNIIDHFLAASAPVNAPTIIPPVASYEELPKPKKPAASARNDLQGYDRHARSFSGGPEDFATPQASARGSPSPERTQGGGDNFVEVDLPSTTISQVDDDPPYDTTSLNQPQEVTNGHVDDEPFRRRSLDPKFDDHSGAPEVAPVAVPVTEPVSAPVTAPVAEPVVAPAVAPDASGKVKKIISELTNELVQLKATTKEQMQKATEKIEQLERQNSLLHQSQQRDAESYTKQIEEKDVLINELKSSLDPSAWDPEQPQTATNISELNRYKLERLELNNKLLYLEQENVKLKDQFAEFEPFMDHQIGELDKFQKVIKVQEEQIDKLSNQVKDQEALHKQIYDWKSKFESLSLEFENYRAIHNDDDISDGEVELQDDDRSILSSAKSRKDISSQLGNLVSLWNQKHASSSSRDLSAPPVINPESHPVVAKLQSQVDELLKIGKQNETTFSQEIEALRKELQEKTTSLKTVEENYRESIQSVNNTSKALKLNQEELSNQRILMERLIKENNELKLYKKASSKKLGSRDGTPVVNEYQQGEDSPGVDELNNDDDDDEDVISTAHYNMKIKDLEADLYILKQERDQLKDNVTSLQKQLYLAQNQ
Protein: Ras-related protein Rab-14 (EC 3.6.5.2) (P61106)
Organism: Homo sapiens (Human)
Function: Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity). Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion.
Subcellular location: Recycling endosome {ECO:0000269|PubMed:22595670}. Early endosome membrane {ECO:0000269|PubMed:16962593, ECO:0000269|PubMed:20534812}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:16962593}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16962593}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle {ECO:0000269|PubMed:26032412}. Note=Recruited to recycling endosomes by DENND6A (PubMed:22595670). Recruited to phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211). Colocalizes with RAB11FIP1 on punctate vesicles (PubMed:26032412). {ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:22595670, ECO:0000269|PubMed:26032412}.
Interaction partners:
- Solute carrier family 2, facilitated glucose transporter member 4
- TBC1 domain family member 4
- TBC1 domain family member 1
- Rab GDP dissociation inhibitor alpha
- RUN and FYVE domain-containing protein 1
- Kinesin-like protein KIF16B
- Leucyl-cystinyl aminopeptidase
- Exocyst complex component 6
- Ras-related protein Rab-10
- Rab GDP dissociation inhibitor beta
Sequence:
MATAPYNYSYIFKYIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEFGTRIIEVSGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYDITRRSTYNHLSSWLTDARNLTNPNTVIILIGNKADLEAQRDVTYEEAKQFAEENGLLFLEASAKTGENVEDAFLEAAKKIYQNIQDGSLDLNAAESGVQHKPSAPQGGRLTSEPQPQREGCGC
Protein: acetyl-CoA carboxylase (EC 6.4.1.2) (D3ZBE2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MVLLLFLTCLVFSCLTISWLKIWGKMTDSKPLSNSKVDASLLSSKEESFSASDQSEEHGDCSCPLTTPDQEELASHGGPVDASQQRNSVPSSHQKPPRNPLSSNDTCSSPELQTNRVAAPGSEVPEANGLPFPARPQTQRTGSPTREDKKQAHIKRQLMTSFILGSLDDNSSDEDPSASSFQTSSRKGSRASLGTLSQEAALNTADPESHTPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGNRVIETVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADQYVPVPGGPNNNNYANVELIIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKISSTIVAQTLQIPTLPWSGSGLTVEWTEDSQHQGKCISVPEDVYEQGCVRDVDEGLQAAEKVGFPLMIKASEGGGGKGIRRAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPVSFETPLSPPIARGHVIAARITSENPDEASGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQAEKPDIMLGVVCGALNVADAMFRTCMTEFLHSLERGQVLPADSLLNIVDVELIYGGIKYVLKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGSSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLMQYTVEDGQHVEVGSSYAEMEVMKMIMTLNVQESGRVKYIKRPGAVLEAGCVVAKLELDDPSKVHAAQPFTGELPAQQTLPILGERLHQVFHSVLENLTNVMNGYCLPEPFFSMKLKDWVEKLMMTLRHPSLPLLELQEIMTSVAGRIPVPVEKAVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKVDREAFFMNTQSIVQLIQRYRSGTRGYMKAVVLDLLRRYLNVEHHFQQGKRHHPQLCVINLREQFKPDMTRVLDCIFSHSQVAKKNQLVTMLIDELCGPDPTLSEELTSILKELTQLSRSEHCKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRELPDGTCVVEFQFMLPSSHPNRMAMPINVSDPDLLRHSKELFMDSGFSPLCQRMGAMVAFRRFEEFTRNFDEVISCFANVPTDTPLFSKACTSLYSEEDSKSLQEEPIHILNVAIQCADHMEDERLVPVFRAFVQSKVFPSCLWGQRTGCLDLCVREFPKFFTFRARDEFAEDRIYRHLEPALAFQLELSRMRNFDLTAVPCANHKMHLYLGAAKVKEGLEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPLKIEESVRAMVMRYGSRLWKLRVLQAEVKINIRQTTSDCAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSFGNKQGSLHGMLINTPYVTKDLLQAKRFQAQSLGTTYVYDFPEMFRQALFKLWGSPEKYPKDILTYTELVLDSQGQLVEMNRLPGCNEVGMVVFKMRFKTPEYPEGRDTIVIGNDITFQIGSFGIGEDFLYLRASEMARTEGIPQIYLAANSGARMGLSEEIKQIFQVAWVDPEDPYKGFRYLYLTPQDYTQISSQNSVHCKHIEDEGESRYVIVDVIGKDSSLGVENLRGSGMIAGEASLAYEKNVTISMVTCRAIGIGAYLVRLGQRVIQVENSHIILTGAGALNKVLGREVYTSNNQLGGVQIMHTNGVSHVTVPDDFEGVCTILEWLSYIPKDNQSPVPIITPSDPIDREIEFTPTKAPYDPRWLLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRSVEVAVPADPANLDSEAKIIQQAGQVWFPDSAFKTAQVIRDFNQEHLPLMIFANWRGFSGGMKDMYEQMLKFGAYIVDSLRLFKQPVLIYIPPGAELRGGAWVVLDSSINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLVKTIRRIDPVCKKLLGQLGTAQLPDKDRKELESQLKAREDLLLPIYHQVAVQFADLHDTPGHMLEKGIISVRVPHRDTEDHIGVSLCLYLGEAWALERIDKCRLQFGSEDILSLLPSTMGSCRARLCAYLWDSNQVVVQWLEQHWSARDNLRSTIRENINYLKRDSVLKTIQSLVQEHPEATMDCVAYLSQHLTPAEQMQVVQLLSTTESPASH