wanglab/gogpt-training-data huggingface dataset:
Protein: T-complex protein 1 subunit beta (CCT-beta) (B5X2M8)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit zeta-like
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit delta
- Bardet-Biedl syndrome 10 protein
Sequence:
MASLSMAPVNIFRQGADEEKAETARLSSFIGAIAIGDLVKSTLGPKGMDKILIGGGREGTVTVTNDGATILKAIGVDNPAAKVLVDMSKTQDDEVGDGTTSVTVLAAELLREAELLIAKKIHPQIIISGWRKATQAARQALKDAAVDHGNDQVKFQEDLLNISRTTLSSKLLTHHKDHFAKLAVEAVLRLKSSGNLEAIHVIKKLGGSLIDSYLDEGFLLDKKIGVNQPKRLENVNILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEMAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFAAAGVMAIEHADFSGVERLALVTGGEITSTFDHPELVKLGHCKLIEEVMIGEDTLIHFSGVAMGEACTVVLRGATQQILDEAERSLHDALCVLAQTVKETRTVYGGGCSEMLMAKVVTDLALRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHQEGKTTMGLNMNQGTIGDMSEMGVTESFQVKRQVLLSAAEAAEMILRVDNIIKAAPRKRVPDHHPC
Protein: Heterogeneous nuclear ribonucleoprotein A0 (B5X0T7)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MTNQLCKLFVGGLNVETTDDGLRQHFEQYGQLTDCVVVQNQQLQRSRCFGFVTYSSAEEADAAMAARPHVVDGTNVELKRAVAREDAGRPEALAKVKKIFIGGLKDDIEDEHLNDYFSQFGAIEKAEVISDKETFKKRGFGFVYFEDNDSADKAVVLKFHTINGHKVEVKKALTKQEMQSAGGRGGRGGRGMRGSQNGYDGGRGGGYGSYGGGYGGNDGGYGGGYGNGGGYGNQGGYGGGYGDQMGGSYGGNGYNDFGGDYGQQSSGYGAMKGGSYSGRSAAPYSRGGAGGYGRGGYGGY
Protein: Lipoprotein signal peptidase (EC 3.4.23.36) (Prolipoprotein signal peptidase) (Signal peptidase II) (SPase II) (P9WK99)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00161}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00161}.
Interaction partners:
- CN hydrolase domain-containing protein
- CN hydrolase domain-containing protein
- Uncharacterized RNA pseudouridine synthase Rv1540
- Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
- L-asparaginase
- Signal peptidase I
- Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase
Sequence:
MPDEPTGSADPLTSTEEAGGAGEPNAPAPPRRLRMLLSVAVVVLTLDIVTKVVAVQLLPPGQPVSIIGDTVTWTLVRNSGAAFSMATGYTWVLTLIATGVVVGIFWMGRRLVSPWWALGLGMILGGAMGNLVDRFFRAPGPLRGHVVDFLSVGWWPVFNVADPSVVGGAILLVILSIFGFDFDTVGRRHADGDTVGRRKADG
Protein: Vacuolar protein sorting-associated protein 26A (H<beta>58 protein) (H beta 58) (Vesicle protein sorting 26A) (mVPS26) (P40336)
Organism: Mus musculus (Mouse)
Function: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3.The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC complex seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (By similarity). Required for retrograde transport of lysosomal enzyme receptor IGF2R. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Required for the endosomal localization of WASHC2 (indicative for the WASH complex). Required for the endosomal localization of TBC1D5. Mediates retromer cargo recognition of SORL1 and is involved in trafficking of SORL1 implicated in sorting and processing of APP (By similarity). Involved in retromer-independent lysosomal sorting of F2R. Involved in recycling of ADRB2 (By similarity). Acts redundantly with VSP26B in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1. Enhances the affinity of SNX27 for PDZ-binding motifs in cargo proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15078902}. Endosome membrane {ECO:0000269|PubMed:15078902}; Peripheral membrane protein {ECO:0000269|PubMed:15078902}. Early endosome {ECO:0000269|PubMed:18088321, ECO:0000269|PubMed:21920005}. Note=Predominantly found in early not late endosomes. {ECO:0000269|PubMed:21920005}.
Interaction partners:
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-2
- Sorting nexin-27
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-1
- Sorting nexin-3
- Sorting nexin-5
- TBC1 domain family member 5
- Sorting nexin-6
- Vacuolar protein sorting-associated protein 26B
Sequence:
MSFLGGFFGPICEIDVALNDGETRKMAEMKTEDGKVEKHYLFYDGESVSGKVNLAFKQPGKRLEHQGIRIEFVGQIELFNDKSNTHEFVNLVKELALPGELTQSRSYDFEFMQVEKPYESYIGANVRLRYFLKVTIVRRLTDLVKEYDLIVHQLATYPDVNNSIKMEVGIEDCLHIEFEYNKSKYHLKDVIVGKIYFLLVRIKIQHMELQLIKKEITGIGPSTTTETETIAKYEIMDGAPVKGESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIILWRKAPEKLRKQRTNFHQRFESPDSQASAEQPEM
Protein: SLAM family member 6 (Activating NK receptor) (NK-T-B-antigen) (NTB-A) (CD antigen CD352) (Q96DU3)
Organism: Homo sapiens (Human)
Function: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. 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. Triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors. Positive signaling in NK cells implicates phosphorylation of VAV1. NK cell activation seems to depend on SH2D1B and not on SH2D1A. In conjunction with SLAMF1 controls the transition between positive selection and the subsequent expansion and differentiation of the thymocytic natural killer T (NKT) cell lineage (By similarity). Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Promotes recruitment of RORC to the IL-17 promoter. In conjunction with SLAMF1 and CD84/SLAMF5 may be a negative regulator of the humoral immune response. In the absence of SH2D1A/SAP can transmit negative signals to CD4(+) T-cells and NKT cells. Negatively regulates germinal center formation by inhibiting T-cell:B-cell adhesion; the function probably implicates increased association with PTPN6/SHP-1 via ITSMs in absence of SH2D1A/SAP. However, reported to be involved in maintaining B-cell tolerance in germinal centers and in preventing autoimmunity (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- SH2 domain-containing protein 1A
- Signaling lymphocytic activation molecule
- SH2 domain-containing protein 1B
- CD48 antigen
- Natural killer cell receptor 2B4
- Killer cell lectin-like receptor subfamily F member 1
- Natural cytotoxicity triggering receptor 3
- CD226 antigen
- T-cell surface antigen CD2
- NKG2-D type II integral membrane protein
Sequence:
MLWLFQSLLFVFCFGPGNVVSQSSLTPLMVNGILGESVTLPLEFPAGEKVNFITWLFNETSLAFIVPHETKSPEIHVTNPKQGKRLNFTQSYSLQLSNLKMEDTGSYRAQISTKTSAKLSSYTLRILRQLRNIQVTNHSQLFQNMTCELHLTCSVEDADDNVSFRWEALGNTLSSQPNLTVSWDPRISSEQDYTCIAENAVSNLSFSVSAQKLCEDVKIQYTDTKMILFMVSGICIVFGFIILLLLVLRKRRDSLSLSTQRTQGPAESARNLEYVSVSPTNNTVYASVTHSNRETEIWTPRENDTITIYSTINHSKESKPTFSRATALDNVV
Protein: Nascent polypeptide-associated complex subunit beta-1 (NAC-beta-1) (BTF3 homolog EGD1) (Beta-1-NAC) (GAL4 DNA-binding enhancer protein 1) (Q02642)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum EGD1 may act as a transcription factor that exert a negative effect on the expression of several genes that are transcribed by RNA polymerase II. Can enhance DNA binding of the GAL4 protein activator.
Subcellular location: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic, may also transiently localize to the nucleus.
Interaction partners:
- Nascent polypeptide-associated complex subunit alpha
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL31A
- Nascent polypeptide-associated complex subunit beta-2
- Protein TMA108
- Large ribosomal subunit protein eL31B
- Protein SSO1
- Large ribosomal subunit protein uL16
- Nucleoporin NIC96
- Large ribosomal subunit protein uL3
Sequence:
MPIDQEKLAKLQKLSANNKVGGTRRKLNKKAGSSAGANKDDTKLQSQLAKLHAVTIDNVAEANFFKDDGKVMHFNKVGVQVAAQHNTSVFYGLPQEKNLQDLFPGIISQLGPEAIQALSQLAAQMEKHEAKAPADAEKKDEAIPELVEGQTFDADVE
Protein: Alpha-amylase (EC 3.2.1.1) (Q5B7U2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- 1,4-alpha-glucan-branching enzyme
- Alpha-1,4 glucan phosphorylase
- Glucoamylase
- Glucoamylase
- Zn
- Alpha-glucosidase
- Probable alpha/beta-glucosidase agdC
- Alpha/beta-glucosidase agdC
- Alpha/beta-glucosidase agdC
Sequence:
MKLASTLAGLLLPLISTVSAADVDAWKSRNIYFALTDRVARGSDDTGGDACDDLSTYCGGTFKGLEGKLDYIKGMGFDAIWITPVVANHDGGYHGYWAKDLYSINENYGTADDLKSLVSAAHEKGIYIMADVVANHMGSPISDNQPESLSQESAYHSACTIDYSSQESIETCRIADDLPDVNTESEEIRTLFKEWITWLVKEYEFDGLRIDTVKHVEKDFWSDFSSAAGVYTIGEVFDGDPDYLAGYANTMDGLLNYAVYYPVNNFYQQAGSAQDIVDMHDKIDSSFPDPSALGTFIDNHDNARWLSNKDDKSLLKNALAYVILARGIPIVYYGTEQGYAGGNDPENREDLWRSNFDTDADLYKAISLLSAARSAAGGLGDNDHVHLHVAESAYAWSRAEGKLVVVTSNSGSGSENEICFDSKTPNGSWENIFGEGTISADDSGQICVSITNGEPAVLVAQS
Protein: PABC domain-containing protein (Q3TSA5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRPNPRWQQGGRPQGFQGMPSALRQSGPRPALRHLAPTGNAPASRGLPTTAQRVGSECPDRLAMDFGGAGAAQQGLTDSCQSGGVPTAVPNLAPRAAVAAAAPRAVAPYKYASSVRSPHPAIQPVQAPQPAVHVQGQEPLTASMLAAAPPQEQKQMLGERLFPLIQTMHSNLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHHAKKEAAQKVGTVAAATS
Protein: Retinoid isomerohydrolase (EC 3.1.1.64) (All-trans-retinyl-palmitate hydrolase) (Lutein isomerase) (Meso-zeaxanthin isomerase) (EC 5.3.3.22) (Retinal pigment epithelium-specific 65 kDa protein) (Retinol isomerase) (O70276)
Organism: Rattus norvegicus (Rat)
Function: Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore. Essential for the production of 11-cis retinal for both rod and cone photoreceptors. Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A9C3R9}. Cell membrane {ECO:0000250|UniProtKB:Q28175}; Lipid-anchor {ECO:0000250|UniProtKB:Q28175}. Microsome membrane {ECO:0000250|UniProtKB:Q28175}. Note=Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. Undergoes light-dependent intracellular transport to become more concentrated in the central region of the retina pigment epithelium cells (By similarity). {ECO:0000250|UniProtKB:Q16518, ECO:0000250|UniProtKB:Q28175}.
Interaction partners:
- Lecithin retinol acyltransferase
- Retinol dehydrogenase 5
- Retinol dehydrogenase 10
- Diacylglycerol O-acyltransferase 1
- Patatin like phospholipase domain containing 4
- Acyltransferase
- Retinaldehyde-binding protein 1
- Bestrophin
- Rhodopsin
- Bestrophin
Sequence:
MSIQIEHPAGGYKKLFETVEELSTPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYYRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEITDNALVNIYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAHPHIESDGTVYNIGNCFGKNFTVAYNIIKIPPLKADKEDPINKSEVVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLFKFLSSWSLWGANYMDCFESNESMGVWLHVADKKRRKYFNNKYRTSPFNLFHHINTYEDNGFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKRNAMKAPQPEVRRYVLPLTIDKADTGRNLVTLPHTTATAILCSDETIWLEPEVLFSGPRQAFEFPQINYQKCGGKPYTYAYGLGLNHFVPDKLCKLNVKTKEIWMWQEPDSYPSEPIFVSQPDALEEDDGVVLSVVVSPGAGQKPAYLLVLNAKDLSEIARAEVETNIPVTFHGLFKKP
Protein: Homer protein homolog 1b isoform 2 (Homer scaffold protein 1b) (A0A0R4INT7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MGEQPIYSTRAHVFQIDPSTKKNWMPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMSFTKTSQKFGQWADSRANTVYGLGFSSEHHLAKFADKFAEYKEAARIAKEKSLEKMELASSPSQESPADIHSPLTPPVTADLCRINGTGDDVTLSDVSPNSMLQSDLSPTTPTLAHSPTTNKHWEAELAALKSNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVSELESQSSQTNVIKSQKTELNQTIEELECTLRAKEEEMMRLKEEVENAKQLQAQKDELTKKLEDTDMRNKELEEQLSDLEQRLESSQVDQENLRKNLKTLLEILDGKIFELTELRDNLAKLIEDS
Protein: Synaptotagmin-14 (Synaptotagmin XIV) (SytXIV) (Q8NB59)
Organism: Homo sapiens (Human)
Function: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent.
Subcellular location: Membrane {ECO:0000269|PubMed:21835308}; Single-pass type III membrane protein {ECO:0000269|PubMed:21835308}. Note=Localized in perinuclear and submembranous regions.
Interaction partners:
Sequence:
MAIEGGERTCGVHELICIRKVSPEAVGFLSAVGVFIILMLLLFLYINKKFCFENVGGFPDLGSEYSTRKNSQDKIYNSYMDKDEHGSSSESEDEALGKYHEALSRTHNSRLPLADSRQRNYAWETRQKYSPLSAEYDGYSSEASIDEGNCIQRMRRTPPLDELQPPPYQDDSGSPHLSCTPSEIGDSKCEFSHCSNSPRCSYNKCPSEGSTGHEIESFHNKGYEEDVPSDSTAVLSPEDMSAQGSSSQLPKPFDPEPEAKYGTLDVTFDYDSQEQKLLVTVTAVTDIPTYNRTGGNSWQVHLVLLPIKKQRAKTSIQRGPCPVFTETFKFNHVESEMIGNYAVRFRLYGVHRMKKEKIVGEKIFYLTKLNLQGKMSLPVILEPSYNHSGCDSQMSVSEMSCSESTSSCQSLEHGSVPEILIGLLYNATTGRLSAEVIKGSHFKNLAANRPPNTYVKLTLLNSMGQEMSKCKTSIRRGQPNPVYKETFVFQVALFQLSDVTLILSVYNKRSMKRKEMIGWISLGLNSSGEEELNHWTEMKESKGQQVCRWHALLES
Protein: Pregnancy specific glycoprotein 19 (G3V9P5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Prolactin-5A1
- CD9 antigen
Sequence:
MEVSSVLLCSGCSPWQGFLLTASLLTCWLLPTTAQVTLKSSPPQVVEGENVLLSADNLPENIIAFAWYKGETDMNRGIALYSLRYTVSLTGPVHSGRETLYSDGSLWIKNVTQEDTGFYTFRIINNHGKIQSNTTLFLHVKSSLFVCGRPSNIDEPTIESVPVSVSEWGSVLLRVHNLPENLRTLFWYKGVLVLKKLEIARYRTTKNTYELGPVHSGRETVYSNGSLLLQNVTWKDTGFYTLRTLSTDLKVEITHIYLQVNTSLSSCCDPVTSVPLMIEPVPRHAVEGESVLLYVHNLPEALQTFSWYKGVYSLKEFKIAEYSIATKSVFPGPAHRGRATGYTNGSLLLQDLTARDTGLYTLVTLDSNSKIKSAPVQVTVHKPVTQPFLRVTVSTVTVQSSVVFTCLSDNTGVSIRWLFKNRNLQVTERMTLSPSNCQLRIHVVRREDAGQYRCEAFNPISSKTSRPVSLAVISE
Protein: Aldo/keto reductase slr0942 (AKR) (EC 1.1.1.184) (AKR3G1) (P74308)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Aldo/keto reductase with broad substrate spectrum. Catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols. Highest enzymatic efficiency is observed with 4-oxonon-2-enal (4-ONE) and 4-hydroxynon-2-enal (4-HNE), that are lipid peroxidation products, and 9,10-phenanthrenequinone (9,10-PQ), a photoproduct of phenanthrene that is one of the most prevalent polycyclic aromatic hydrocarbons in the environment. Is also active on sugar-derived reactive carbonyls such as methylglyoxal (MG), glyoxal and 3-deoxyglucosone (3-DG), and on other lipid-derived carbonyls such as acrolein. May be involved in the detoxification of the toxic lipid peroxidation products 4-ONE and 4-HNE besides many other exo- and endogenic reactive carbonyl compounds (RCs) that may lead to photoinhibition or other cell damages.
Interaction partners:
- S-
- Aldehyde reductase AdhA
- Aldehyde dehydrogenase
- Glycerol kinase
- Uncharacterized oxidoreductase slr1167
- Slr0315 protein
- Slr1503 protein
- Methionine synthase
- Hydroxyacylglutathione hydrolase
Sequence:
MQSFNRINSMKYFPLSNGEQIPALGLGTWKSSPQVVGQAVEQALDLGYRHLDCAAIYGNEAEIGATLANAFTKGVVKREELWITSKLWSNAHHPDAVLPALEKTLQDLGLDYLDLYLIHWPVVIQPDVGFPESGDQLLPFTPASLEGTWQALEKAVDLGLCHHIGVSNFSLKKLEMVLSMARIPPAVNQVELHPYLQQSDLLTFANSQNILLTAYSPLGSGDRPAAFQQAAEPKLLTDPVINGIAAEQGCSAAQVLLAWAIQRGTVTIPKSVNPERLEQNLRAADITLTDSEMAKIALLDRHYRYVSGDFWTMPGSPYTLQNLWDEI
Protein: Phosphatidylinositol 3-kinase regulatory subunit gamma (PI3-kinase regulatory subunit gamma) (PI3K regulatory subunit gamma) (PtdIns-3-kinase regulatory subunit gamma) (Phosphatidylinositol 3-kinase 55 kDa regulatory subunit gamma) (PI3-kinase subunit p55-gamma) (PtdIns-3-kinase regulatory subunit p55-gamma) (p55PIK) (Q64143)
Organism: Mus musculus (Mouse)
Function: Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- RAC-gamma serine/threonine-protein kinase
- Epidermal growth factor receptor
- Insulin receptor substrate 1
- Phosphoinositide 3-kinase regulatory subunit 5
Sequence:
MYNTVWSMDRDDADWREVMMPYSTELIFYIEMDPPALPPKPPKPMTPAVTNGMKDSFISLQDAEWYWGDISREEVNDKLRDMPDGTFLVRDASTKMQGDYTLTLRKGGNNKLIKIYHRDGKYGFSEPLTFTSVVELINHYHHESLAQYNPKLDVKLTYPVSRFQQDQLVKEDNIDAVGKNLQEFHSQYQEKSKEYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCHTQEQHSKDYIERFRREGNEKEIERIMMNYDKLKSRLGEIHDSKLRLEQDLKKQALDNREIDKKMNSIKPDLIQLRKIRDQHLVWLNHRGVRQRRLNAWLGIKNEDSDESYFINEEDENLPHYDEKTWFVEDINRVQAEDLLYGKPDGAFLIRESSKKGCYACSVVADGEVKHCVIYSTARGYGFAEPYNLYSSLKELVLHYQQTSLVQHNDSLNVRLAYPVHAQMPTLCR
Protein: Formin-like protein 14 (AtFH14) (Q9C6S1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cytochrome C oxidase assembly factor
- Profilin-3
- Profilin-4
- Profilin-2
- Profilin-1
- Profilin-5
- Protein JASON
- FH protein interacting protein FIP2
- AT3g13990/MDC16_11)
- FRIGIDA-like protein 3
Sequence:
MSLLSRFFYKRPPDGLLEFADRVYVFDSCFCTEVLADSLYQIFLHEVINDLHEEFPESSFLAFNFREGEKKSVFAETLCEYDVTVLEYPRQYEGCPMLPLSLIQHFLRVCESWLARGNRQDVILLHCERGGWPLLAFILASFLIFRKVHSGERRTLEIVHREAPKGLLQLLSPLNPFPSQLRYLQYVARRNINSEWPPPERALSLDCVIIRGIPNFDSQHGCRPIIRIFGRNYSSKSGLSTEMVYSMSDKKKPLRHYRQAECDVIKIDIQCWVQGDVVLECVHMDLDPEREVMMFRVMFNTAFIRSNILMLNSDNLDILWEAKDHYPKGFRAEVLFGEVENASPQKVPTPIVNGDETGGLPIEAFSRVQELFSGVDLAENGDDAALWLLKQLAAINDAKEFTRFRHKGSFYFNSPDSEEETNTSSAADSSDEGFEAIQRPRIHIPFDNDDTDDITLSVAHESSEEPHEFSHHHHHEIPAKDSVDNPLNLPSDPPSSGDHVTLLPPPPPPPPPPLFTSTTSFSPSQPPPPPPPPPLFMSTTSFSPSQPPPPPPPPPLFTSTTSFSPSQPPPPPPLPSFSNRDPLTTLHQPINKTPPPPPPPPPPLPSRSIPPPLAQPPPPRPPPPPPPPPSSRSIPSPSAPPPPPPPPPSFGSTGNKRQAQPPPPPPPPPPTRIPAAKCAPPPPPPPPTSHSGSIRVGPPSTPPPPPPPPPKANISNAPKPPAPPPLPPSSTRLGAPPPPPPPPLSKTPAPPPPPLSKTPVPPPPPGLGRGTSSGPPPLGAKGSNAPPPPPPAGRGRASLGLGRGRGVSVPTAAPKKTALKPLHWSKVTRAAKGSLWADTQKQENQPRAPEIDISELESLFSAVSDTTAKKSTGRRGSSISKPEKVQLVDLRRANNCEIMLTKIKIPLPDMLSAVLALDSLALDIDQVENLIKFCPTKEEMELLRNYTGDKEMLGKCEQFFMELMKVPRIEAKLRVFGFKITFASQVEELKSCLNTINAATKEVKESAKLRQIMQTILTLGNALNQGTARGSAVGFKLDSLLKLSDTRARNNKMTLMHYLCKLVGEKMPELLDFANDLVHLEAASKIELKTLAEEMQAATKGLEKVEQELMASENDGAISLGFRKVLKEFLDMADEEVKTLASLYSEVGRNADSLSHYFGEDPARCPFEQVTKILTLFMKTFIKSREENEKQAEAEKKKLEKEAIKEKSATKKDGVDNDNDLIQQIHRHRT
Protein: GABAA receptor betaZ2 subunit (Q9DDD9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MESIGKTPHIFLLCPLIVAVACAQSIRDPSNMPVVKDTVDRLMKGYDIRLRPDFGGAPVAVRMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYSEIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGGDGAVSGVERIELPQFSIVGYKLISKNVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFLALLEYAFVNYIFFGRGPQRQKKAAEKAATANNEKLRPDPNKWLVGSVVQRDDALYARMKQREIDGYDSMWDPIFAEDAALGLGDQRLKMTPDDIRLTTVEMKNEMGPSDLSKGLGDPRSTMLAYDSSTLQYRRAAMARQNYGHSALERHATQKKSRLRRRASQLKVNIPDLSDVNSIDKWSRMIFPTLFSFFNIVYWLYYVH
Protein: Glutamate--tRNA ligase, chloroplastic/mitochondrial (EC 6.1.1.17) (AtERS) (Glutamyl-tRNA synthetase) (GluRS) (Protein OVULE ABORTION 3) (Q9FEA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16107332, ECO:0000269|PubMed:16251277, ECO:0000269|PubMed:17433818, ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000269|PubMed:16107332, ECO:0000269|PubMed:16251277, ECO:0000269|PubMed:17433818, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Glutamyl-tRNA reductase 2, chloroplastic
- Glutamyl-tRNA reductase 1, chloroplastic
- Probable glutamyl-tRNA reductase 3, chloroplastic
- Proline--tRNA ligase, chloroplastic/mitochondrial
- Leucine--tRNA ligase, chloroplastic/mitochondrial
- Large ribosomal subunit protein eL38z/eL38y
- Leucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, chloroplastic/mitochondrial
- Large ribosomal subunit protein eL42z/eL42y
- Isoleucine--tRNA ligase, cytoplasmic
Sequence:
MASLVYGTPWLRVRSLPELAPAFLRRRQSSLFYCSRRSFAVVACSTPVNNGGSVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLERSTRESEAAVLQDLSWLGLDWDEGPGVSGDFGPYRQSERNALYKQYAEKLLESGHVYRCFCSSEELVKMKENAKLKQLPPVYTGKWATASDAEIEQELEKGTPFTYRFRVPKEGSLKINDLIRGEVCWNLDTLGDFVVMRSNGQPVYNFCVTVDDATMAISHVIRAEEHLPNTLRQALIYKALKFPMPQFAHVSLILAPDRSKLSKRHGATSVGQYREMGYLPQGMVNYLALLGWGDGTENEFFTLEDLVEKFSIERVNKSGAIFDSTKLRWMNGQHLRALPNEKLTKLVGERWKSAGILTESEGSFVNEAVELLKDGIELVTDSDKVLLNLLSYPLHATLASPEAKPAVEDKLHEVAASLIAAYDSGEIPSALEEGQGAWQKWVKAFGKSLKRKGKSLFMPLRVLLTGKLHGPEMGTSIVLIYKAGSPGIVVPQAGFVSMEERFKILREIDWEALNKDESVPLESTATVST
Protein: Putative nickel-responsive regulator (O25896)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Transcriptional regulator.
Interaction partners:
- Probable nicotinate-nucleotide adenylyltransferase
- Biopolymer transport protein ExbB
Sequence:
MDTPNKDDSIIRFSVSLQQNLLDELDNRIIKNGYSSRSELVRDMIREKLVEDNWAEDNPNDESKIAVLVVIYDHHQRELNQRMIDIQHASGTHVLCTTHIHMDEHNCLETIILQGNSFEIQRLQLEIGGLRGVKFAKLTKASSFEYNE
Protein: Large ribosomal subunit protein uL11 (60S ribosomal protein L12) (Q9W1B9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 40S ribosomal protein S27
- Small ribosomal subunit protein uS14
- 60S ribosomal protein L27
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL38
Sequence:
MPPKFDPTEVKLVYLRCVGGEVGATSSLAPKIGPLGLSPKKIGDDIAKATSDWKGLKITVCLTIQNRQAAISVVPSAASLIIKALKEPPRDRKKQKNIKHSGNIGFEDILAIARVMRPRSMARELKGTCKEVLGTAQSVGCTVDGKHPHDVIDELNEGSIEVPAE