wanglab/gogpt-training-data huggingface dataset:
Protein: PDGF/VEGF receptor (Q95P10)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MAMLPRLILLPLLLILRISWSDAVPLQQFSPDPDDSIENCGGENGAPLMTPCKSAIILDAQTSTTLKCEDDEPMSWWTSQSQYVHVKSFDNTEDPARPFGTSLHLIEVTADYVAAYYCVKTSKFSQIAKEEQSDEAMIELVNQGYASSIYVYVNDPDTKLVDSHNVVTARQYTDVVIPCKPAMPDTEVLLETSNGEMHSSKSVGRYDPQRGFTIEIRSIVDGGDYYCRPNPPFPHNEEEMTSIEVRFIGNGHIDKDGKPLPKPVIRSSVEHHVFTDTNFTLDCEQSAYVESVYGMEWFTPSRDENRIFASQSRTDPKTRNSTHQTGRSTLTVLNAQPSDTGLYKCVTTDNSNQNVQRATYRIKVLKQNESYLNVGEPSGHYNVQEYANRTIQMTANFEGFPTPSFSWFKPDGTEVRQSENNFKILSTELSTMLQVLNAQLQDSGTYVLRGSNSFGVVQREYNVSVMDAPALKMSDAYVQVGSVARLECTVRSYPPAIVTFFFRPCSLEPQWPTCSVLNQNFSLPSEQEKYQFQTRPRPGKLSVERIYEVSFLPTEPGILTCIAQNIIDGKERRTLTKAHVLLGNISENMTIYGFDKDHKIAKEDNVNFTCEALAYHFDGNLKWFINGEDLKESDSVHIETSHTKYSYKSTVHITTISDRDRGTYECRAYHNDKDAAYSSREIDLYVHDPSAPQWTNGGQEGHSKIKRKLSQTLELECASTAVPVAIVRWFKDDKEVTESKLRHIIEKESKLLITHLYPGDEGVYKCVVENRLDRIERSFTVVISDLPGISMAWVWFGVILFLILIGLCVFLAVRYQKEHKRHLALKAAGLANFEEGAVGHINPDLTLDEQAELLPYNREFEFPRENLKLGKQLGAGAFGVVLKGEAKGIRREEPTTTVAVKMVKATADNEVVRALVSELKIMVHLGQHLNVVNLLGAVTKNIAKRELMVIVEYCRFGNIQNFLLRNRKCFINQINPDTDHIDPSIMTQRMSDNYELHRDTNGGGLKYANVGFPIHSYINEPHNNNTQPPTHRRNSDNDPRSGTRAGRTGSGTATYSYDRQMDTCATVMTTVPEDDQIMSNNSVQPAWRSNYKTDSTEAMTVTTVDLISWAFQVARGMDYLSSKKVLHGDLAARNILLCEDNVVKICDFGLARSMYRGDNYKKSENGKLPIKWLALESLSDHVFSTYSDVWSYGIVLWEMFSLAKVPYPGIDPNQELFNKLNDGYRMEKPKFANQELYEIMLECWRKNPESRPLFAELEKRFANMLGEDVASHYLDLNNPYMQSNIEYMKKQSTDYLALMGSPDELAPAAPRYVNGHIVPDIRIEELPDDYMEMSRDSDPDACTAIFSPTRLEGESSDFPDFSSETTFNFPGARQSPTLSNNLNSGSSKPLRKKNGMPTVDVADQAPEEIPMLHRSSTGSDGSPEQGRRFNQALKQQYVTPTPSPRHHVETKLNGEPSENYVNMKPPRKNIPGKTTTGGGGAAAGASTEAFSNPSYQPLSTVNEKEQRRY
Protein: Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 (PAPS synthase 2) (PAPSS 2) (Sulfurylase kinase 2) (SK 2) (SK2) [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (3'-phosphoadenosine-5'-phosphosulfate synthase) (APS kinase) (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenylylsulfate 3'-phosphotransferase)] (O88428)
Organism: Mus musculus (Mouse)
Function: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate/PAPS, the activated sulfate donor used by sulfotransferases. In mammals, PAPS is the sole source of sulfate while APS appears to only be an intermediate in the sulfate-activation pathway. May have an important role in skeletogenesis during postnatal growth.
Interaction partners:
- 3'
- Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase
- FAD synthase
- Sulfite oxidase, mitochondrial
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- Elongation factor 1-alpha 2
- Elongation factor 1-alpha 1
- Eukaryotic peptide chain release factor GTP-binding subunit ERF3A
- Eukaryotic peptide chain release factor GTP-binding subunit ERF3B
- HBS1-like protein
Sequence:
MSANFKMNHKRDQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITSFISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKTNLSSVSDCVQQVVELLQEQNIVPHTTIKGIHELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDGVVPRDGVINMSIPIVLPVSADDKARLEGCSKFALMYEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDGLDQYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLEWRMKQHAAVLEERVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVAAYNKIKKAMDFYDPARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLEKTN
Protein: Cdc42 effector protein 4 (Binder of Rho GTPases 4) (Q9JM96)
Organism: Mus musculus (Mouse)
Function: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.
Subcellular location: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Rho-related GTP-binding protein RhoQ
- Cell division control protein 42 homolog
- Septin-4
- Septin-7
- Septin-9
- Septin-8
- Neuronal-specific septin-3
- BAR/IMD domain-containing adapter protein 2-like 1
Sequence:
MPILKQLVSSSVNSKRRSRADLTAEMISAPLGDFRHTMHVGRAGDAFGDTSFLTSKAREADDESLDEQASASKLSLLSRKFRGSKRSQSVTRGDREQRDMLGSLRDSALFVKNAMSLPQLNEKEAAEKDSSKLPKSLSSSPVKKADARDGGPKSPHRNGATGPHSPDPLLDEQAFGDLMDLPIMPKVSYGLKHAESILSFHIDLGPSMLGDVLSIMDKDQWGSEEEEEAGGYRDKEGPSSIVQAPPVLEVVPPLGRQESKASWDQASMLPPHAVEDDGWAVVAPSPSSARSVGSHTTRDSSSLSSYTSGVLEERSPAFRGPDRVAAAPPRQPDKEFCFMDEEEEDEIRV
Protein: Phosphoserine phosphatase SerB2 (PSP) (PSPase) (EC 3.1.3.3) (O-phosphoserine phosphohydrolase) (Protein-serine/threonine phosphatase) (EC 3.1.3.16) (O53289)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the dephosphorylation of O-phospho-L-serine into L-serine, a step in the L-serine biosynthetic pathway. Exhibits high specificity for L-phosphoserine compared to substrates like L-phosphothreonine (5% relative activity) and L-phosphotyrosine (1.7% relative activity).
Subcellular location: Secreted {ECO:0000269|PubMed:26984196}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:26984196}. Note=Is secreted into the cytosol of infected macrophages and is found in bronchoalveolar lavage samples of tuberculosis patients. Co-localizes with host tubulin. {ECO:0000269|PubMed:26984196}.
Interaction partners:
- Phosphoserine aminotransferase
- L-serine dehydratase
- Serine hydroxymethyltransferase 1
- Serine hydroxymethyltransferase 2
- Probable cystathionine beta-synthase Rv1077
- Tryptophan synthase beta chain
- L-threonine dehydratase biosynthetic IlvA
- Tryptophan synthase alpha chain
- Serine acetyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
Sequence:
MPAKVSVLITVTGMDQPGVTSALFEVLAQHGVELLNVEQVVIRGRLTLGVLVSCPLDVADGTALRDDVAAAIHGVGLDVAIERSDDLPIIRQPSTHTIFVLGRPITAGAFSAVARGVAALGVNIDFIRGISDYPVTGLELRVSVPPGCVGPLQIALTKVAAEEHVDVAVEDYGLAWRTKRLIVFDVDSTLVQGEVIEMLAARAGAQGQVAAITEAAMRGELDFAESLQRRVATLAGLPATVIDDVAEQLELMPGARTTIRTLRRLGFRCGVVSGGFRRIIEPLARELMLDFVASNELEIVDGILTGRVVGPIVDRPGKAKALRDFASQYGVPMEQTVAVGDGANDIDMLGAAGLGIAFNAKPALREVADASLSHPYLDTVLFLLGVTRGEIEAADAGDCGVRRVEIPAD
Protein: E3 ubiquitin-protein ligase RNF183 (EC 2.3.2.27) (Q8QZS5)
Organism: Mus musculus (Mouse)
Function: Acts as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Triggers apoptosis in response to prolonged ER stress by mediating the polyubiquitination and subsequent proteasomal degradation of BCL2L1 (By similarity). May collaborate with FATE1 to restrain BIK protein levels thus regulating apoptotic signaling (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29300766}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q96D59}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96D59}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:29300766}. Lysosome membrane {ECO:0000269|PubMed:29300766}.
Interaction partners:
- Fetal and adult testis-expressed transcript protein homolog
Sequence:
MSEPQGQELRAECPVCWNPFNNTFHTPKVLDCCHSFCVECLAHLSLVTPARRRLLCPLCRQPTVLASGQPVTDLPTDTAMLTLLRLEPHHVILEGHQLCLKDQPKSRYFLRQPRVYTLDLGAEPGSQTGLPQDTAPDTRPVPIPSHYSLRECVRNPHFRIFAYLMAVILSVTLLLIFSIFWTKQFFWGMG
Protein: Salivary glue protein Sgs-5 (P07701)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Salivary glue protein Sgs-7
- Ecdysone-induced gene 71Ee
- Salivary glue protein Sgs-4
- Salivary glue protein Sgs-3
- Salivary glue protein Sgs-8
- Salivary gland secretion 1
- Sgs5bis
- Uncharacterized protein, isoform A
- Uncharacterized protein, isoform B
Sequence:
MFNIKLLLLLLAVSWFHHGQAVQETKIEEKPVSEPEIESEIKNSTSVPSKCNIYYRNYQWALQDCVCRCFQNECLMQIESDQRKKEGRSPFVPVTEELCRSFICKKCSVGFPVVAEFPIPAPCGCNRKPGSIATERFYSLCHLLKFSAENSKPFLTYSYCWPF
Protein: At3g02940 (MYB transcription factor) (Myb domain protein 107) (Putative MYB family transcription factor) (Putative transcription factor) (Q9LDI5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cytochrome P450 86B1
- Glycerol-3-phosphate acyltransferase 5
- Cytochrome P450 86A1
- Omega-hydroxypalmitate O-feruloyl transferase
- ABC transporter G family member 2
- CASP-like protein 1B2
- 3-ketoacyl-CoA synthase 2
- Probable 3-ketoacyl-CoA synthase 21
- 3-ketoacyl-CoA synthase 20
Sequence:
MGRSPCCDESGLKKGPWTPEEDQKLINHIRKHGHGSWRALPKQAGLNRCGKSCRLRWTNYLRPDIKRGNFTAEEEQTIINLHSLLGNKWSSIAGHLPGRTDNEIKNYWNTHIRKKLIQMGIDPVTHRPRTDHLNVLAALPQLLAAANFNNLLNLNQNIQLDATSVAKAQLLHSMIQVLSNNNTSSSFDIHHTTNNLFGQSSFLENLPNIENPYDQTQGLSHIDDQPLDSFSSPIRVVAYQHDQNFIPPLISTSPDESKETQMMVKNKEIMKYNDHTSNPSSTSTFTQDHQPWCDIIDDEASDSYWKEIIEQTCSEPWPFRE
Protein: Protein phosphatase Mn(2+)-dependent 1K (Branched-chain alpha-ketoacid dehydrogenase phosphatase) (BCKDH) (BDP) (EC 3.1.3.16) (Protein phosphatase 2C family member) (Protein phosphatase 2C isoform kappa) (PP2C-kappa) ([3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase) (EC 3.1.3.52) (Q8BXN7)
Organism: Mus musculus (Mouse)
Function: Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8N3J5}. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000250|UniProtKB:A6K136}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Branched-chain alpha-ketoacid dehydrogenase kinase
Sequence:
MLSAAFITLLRSGGNQVKKRVLLSSILLQDHRQATPACYFSTSEARCSRFDPDGSGQPATWDNFGIWDNRIDEPILLPPSIKYGKPIPKISLENVGCASLIGKRKENEDRFGFAQLTEEVLYFAVYDGHGGPAAADFCHTHMEKCVMDLLPREKDLETVLTLAFLEIDKAFASYAHLSADASLLTSGTTATVALLRDGVELVVASVGDSRALLCRKGKPMKLTTDHTPERKDEKERIKKFGGFVAWNSLGQPHVNGRLAMTRSIGDLDLKASGVIAEPETTRIKLYHADDSFLVLTTDGINFMVNSQEICDFVNQCHDPKEAAHSVTEQAIQYGTEDNSTAVVVPFGAWGKYKNSEITFSFSRSFASSGRWA
Protein: Anti-sigma F factor antagonist (Stage II sporulation protein AA) (O32726)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition.
Interaction partners:
Sequence:
MSLAIDLEVKQDELIVRLSGELDHHTAENCMNKCRMCLEKRAIRHIVLNLGQLTFMDSSGLGVILGRYKQIKNVGGQMVVCAVSPAVKRLFDMSGLFKIIRVEADEQFALQALGVA
Protein: Regulator of G-protein signaling 5 (RGS5) (P49800)
Organism: Rattus norvegicus (Rat)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O15539}. Membrane {ECO:0000250|UniProtKB:O15539}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
Sequence:
MCKGLAALPHSCLERAKEIKIKLGILLQKPDSAVDLVIPYNEKPEKPAKAHKPSLEEVLQWRQSLDKLLQSNYGFASFKSFLKSEFSEENLEFWVACENYKKIKSPIKMAEKAKQIYEEFIQTEAPKEVNIDHFTKDITMKNLVEPSPHSFDLAQKRIYALMEKDSLPRFVRSEFYKELIN
Protein: BZIP domain-containing protein (F6WQK5)
Organism: Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription factor protein
- Cytochrome c oxidase subunit 5A, mitochondrial
- DUF4706 domain-containing protein
Sequence:
MNNQNDTGTPSGSGNQDTNVNFGDPGQTAEPLIKFKYPQRPQTVPAVQNFGGKAPPPSKAIVKGELEGDQDDYVKRRQRNNIAVKKSREKSREKSQITSERIDQLKEENCVLENKVEVLNQELKVLKQVFMDHAKGFSGSGIDLPDLEQLEKLLGHKLTDKPGTSQMHDNKTNGPSCSGSKS
Protein: 2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase (KD(P)G aldolase) (EC 4.1.2.14) (EC 4.1.2.51) (Q704D1)
Organism: Thermoproteus tenax
Function: Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is not able to use 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal) as substrate.
Interaction partners:
Sequence:
MSHPLIPFRANFLRAPRVLSMEIVAPVITTFRGGRLDPELFANHVKNITSKGVDVVFVAGTTGLGPALSLQEKMELTDAATSAARRVIVQVASLNADEAIALAKYAESRGAEAVASLPPYYFPRLSERQIAKYFRDLCSAVSIPVFLYNYPAAVGRDVDARAAKELGCIRGVKDTNESLAHTLAYKRYLPQARVYNGSDSLVFASFAVRLDGVVASSANYLPELLAGIRDAVAAGDIERARSLQFLLDEIVESARHIGYAAAVYELVEIFQGYEAGEPRGPVYPLDPEEKAWLRAAVAKAKSQLRL
Protein: MORC family CW-type zinc finger protein 1 (Cancer/testis antigen 33) (CT33) (Q86VD1)
Organism: Homo sapiens (Human)
Function: Required for spermatogenesis (By similarity). Essential for de novo DNA methylation and silencing of transposable elements in the male embryonic germ cells (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9WVL5}.
Interaction partners:
- ATPase MORC2
- Meiosis inhibitor protein 1
- Meiotic recombination protein SPO11
Sequence:
MDDRYPALQRAQLRLDFIHANSTTHSFLFGALAELLDNARDAGAERLDVFSVDNEKLQGGFMLCFLDDGCGMSPEEASDIIYFGRSKKRLSTLKFIGQYGNGLKSGSMRIGKDFILFTKKEETMTCVFFSQTFCEEESLSEVVVPMPSWLIRTRESVTDDPQKFAMELSIIYKYSPFKTEAELMQQFDVIYGKCGTLLVIYNLKLLLNGEPELDVKTDKEDILMAGALEDFPARWSFRAYTSVLYFNPWMRIFIQAKRVKTKHLCYCLYRPRKYLYVTSSFKGAFKDEVKKAEEAVKIAESILKEAQIKVNQCDRTSLSSAKDVLQRALEDVEAKQKNLKEKQRELKTARTLSLFYGVNVENRSQAGMFIYSNNRLIKMHEKVGSQLKLKSLLGAGVVGIVNIPLEVMEPSHNKQEFLNVQEYNHLLKVMGQYLVQYCKDTGINNRNLTLFCNEFGYQNDIDVEKPLNSFQYQRRQAMGIPFIIQCDLCLKWRVLPSSTNYQEKEFFDIWICANNPNRLENSCHQVECLPSIPLGTMSTISPSKNEKEKQLRESVIKYQNRLAEQQPQPQFIPVDEITVTSTCLTSAHKENTKTQKIRLLGDDLKHESLSSFELSASRRGQKRNIEETDSDVEYISETKIMKKSMEEKMNSQQQRIPVALPENVKLAERSQRSQIANITTVWRAQPTEGCLKNAQAASWEMKRKQSLNFVEECKVLTEDENTSDSDIILVSDKSNTDVSLKQEKKEIPLLNQEKQELCNDVLAMKRSSSLPSWKSLLNVPMEDVNLSSGHIARVSVSGSCKVASSPASSQSTPVKETVRKLKSKLREILLYFFPEHQLPSELEEPALSCELEQCPEQMNKKLKMCFNQIQNTYMVQYEKKIKRKLQSIIYDSNTRGIHNEISLGQCENKRKISEDKLKNLRIKLALLLQKLQLGGPEGDLEQTDTYLEALLKEDNLLFQNNLNKVTIDARHRLPLEKNEKTSEN
Protein: Organic solute transporter alpha-like protein 1 (Solute carrier family 51 subunit alpha homolog C) (O17204)
Organism: Caenorhabditis elegans
Function: Probable transporter.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MEIVKTIIPHNRSYIEPPIPSATEWLANMSVMHVSCLTIACVFVAITFLSSFFHLFFVLKYVSNERIRNDMYALIFMFPITTFASLVGMFIPRAAIFLYAVSLVYFMFTLFIMVTLLFNIFGGRQEMSAYLLQRNIRVNFTVPPLCFFKFLPTVESTDQNLRRIEWLVFQTPIIRTLLELVSVVVSMEQEGRRESVWFVFSQLMALLSMCIAFYGCYVMVPLGREKHAPYRFDFLFRTCDIAQCIYTIQKFVFEFAAAVGLITSDRYLPAAAKALWWASFMCTWEMMLLSALCSYCLRPAKCKFFDLYPGNDMPALSARDGSNSRVPSFSRRLSIEYEPRIAGVMLEPPSRSSLSITPRDKIEDPTTVSYFADNFDSLSQIQGQ
Protein: NADH dehydrogenase [ubiquinone] 1 subunit C2 (A0A8I5ZXV6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004298}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004298}; Matrix side {ECO:0000256|ARBA:ARBA00004298}.
Interaction partners:
Sequence:
MMNGRPGHEPLRFLPDEARRLPPPKLNDPRLVYIGFLGYCTGLMDNMMRMRPVMKAGLHRQLLYVTSFFFAGYFYLKRQNYLYAVRDHDMFGYIKLHPEDFPEKGISC
Protein: Probable eukaryotic initiation factor 4A (EC 3.6.4.13) (ATP-dependent RNA helicase eIF4A) (Q584C4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Nucleolar protein, putative
- Ribosome biogenesis protein BOP1 homolog
- RNA-binding protein, putative
- Pescadillo homolog
- Nop14-like protein
- Sas10 C-terminal domain-containing protein
- RNA helicase
- ATP-dependent RNA helicase
- Nucleolar complex protein 2
- RNA helicase
Sequence:
MKGVGTWESAMEVAEEQQQQQKKRGGGFQSFGLEKPLLDGILRLGYNVPTPIQRRAIPPMMQGNDIVAMARTGSGKTAAFLIPMLHLLKAHSKIVGVRGLILSPTRELSMQILRFGIQISKFLDLRFVALVGGNSLEQQFEMLASNPDIVVATPGRILHIMEEASLQLSMVKSIVLDEADRLFELGLQPQIVAIMQKIPESCQRSLFSATMPSVLAEFTNAGLHNPVVLRLDAEMKLSDKLKQSAFFVRNDEKIAALIVLLKKVIGIEASDKKSESAEKQALVFVESKFHVDYLEAIMEAYHISCSAVHGQMDQEGRRNAVRAFAKRETSVMIVTDVAARGLDLPLLDNVVNFSFAPTPKLFVHRVGRVARAGRSGAAYSILTFEDFPHYVDLMAFLNRPLQCRKEPGDLLFTADDGCYGRMPEDALQLELDFIRRLVQNDVELKGMTKVVENAHKKFARTKKKATHDGIQTARQSEYQFDSTPLHPIFVERLEKKEIAADEARVGLKRFKAKESLLEIVHGEKMMEIKKPVTVQSLWREQRQRGEDKEGSEKVDTGSDKKQGKHESENCVSMVARKNGAVKGSSTMGRKLSLAESLLLKAQERKKREREAVNGEENDDVDGITVFPARAAYHSNSSAGAIGGMECNSDKYRDREFFMEDVKRNTIEDVHYSVKDATFDIGADTAQEAQQRRQVYAWSKKKNRYVRMNVNDAKALLRGVKNEAGKAVNFKTKLKTYSKWTKKSNLRIQDAGEEEDLGPLRQARDAQRQNERGVGDEDDGFDETEEVDISNPNQGKKLRIGRKLRRLPKDGHVRTFEEMALMKRKAAKEKARLERKKQKGKRKR
Protein: Arginine biosynthesis bifunctional protein ArgJ, mitochondrial [Cleaved into: Arginine biosynthesis bifunctional protein ArgJ alpha chain; Arginine biosynthesis bifunctional protein ArgJ beta chain] [Includes: Glutamate N-acetyltransferase (GAT) (EC 2.3.1.35) (Ornithine acetyltransferase) (OATase) (Ornithine transacetylase); Amino-acid acetyltransferase (EC 2.3.1.1) (N-acetylglutamate synthase) (AGS)] (O94346)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03124, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein arg11
- Amino-acid acetyltransferase, mitochondrial
- Probable acetylornithine aminotransferase, mitochondrial
- Ornithine carbamoyltransferase, mitochondrial
- Putative alanine aminotransferase
- Peptidase M20 domain-containing protein C757.05c
- Argininosuccinate synthase
- NADP-specific glutamate dehydrogenase
- Probable NAD-specific glutamate dehydrogenase
- Arginase
Sequence:
MQTKIFARLAGIGRARFVGTMPDKTKFISKSGTYPQGFSLNGIASGVKANGKKDLAILFSSRPCNAAAVFTKNAFQAAPVQVSRQTLNGCGGKDIHCVVFNSGCANAVTGEGGLMDAQLITAEADNLTRPHWTSWTENSEEFPSSLVMSTGVIGQRLKLDKIQSGLEHAVEDLGSTHEYWMRAAEAICTTDTFPKLVSRELSIAGKVYRIAGFAKGAGMINPNLATLLGLFVTDAPISVDAVRSILRHAINNSFNSISIDGDTSTNDTIAFLANGAAGGSEITKSSPAYKEIRDAVTDIAQQLAKLVVRDGEGATKFVTVQVRGARSEKDAALVASTISNSALVKTAFFGEDANWGRILCAVGYSGAAVNPPATTVSFIPADGTEPLKLLVNGEPQNVDETRASEILSQDELTVDVDLGCGPYAKTNWTCDFSYDYVRINADYRS
Protein: Ras association domain-containing protein 5 (New ras effector 1) (Regulator for cell adhesion and polarization enriched in lymphoid tissues) (RAPL) (Q8WWW0)
Organism: Homo sapiens (Human)
Function: Potential tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing. May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS and KRAS induced apoptosis.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton. Note=Isoform 2 is mainly located in the perinuclear region of unstimulated primary T-cells. Upon stimulation translocates to the leading edge and colocalizes with ITGAL/LFA-1 in the peripheral zone of the immunological synapse. Isoform 2 is localized to growing microtubules in vascular endothelial cells and is dissociated from microtubules by activated RAP1A.
Interaction partners:
- Serine/threonine-protein kinase 4
- GTPase HRas
- Ras association domain-containing protein 1
- Ras-related protein Rap-1A
- GTPase KRas
- Ras-related protein Rap-1b
- Ras-related protein R-Ras
- Ras-related protein M-Ras
- Integrin alpha-L
- GTPase NRas
Sequence:
MAMASPAIGQRPYPLLLDPEPPRYLQSLSGPELPPPPPDRSSRLCVPAPLSTAPGAREGRSARRAARGNLEPPPRASRPARPLRPGLQQRLRRRPGAPRPRDVRSIFEQPQDPRVPAERGEGHCFAELVLPGGPGWCDLCGREVLRQALRCTNCKFTCHPECRSLIQLDCSQQEGLSRDRPSPESTLTVTFSQNVCKPVEETQRPPTLQEIKQKIDSYNTREKNCLGMKLSEDGTYTGFIKVHLKLRRPVTVPAGIRPQSIYDAIKEVNLAATTDKRTSFYLPLDAIKQLHISSTTTVSEVIQGLLKKFMVVDNPQKFALFKRIHKDGQVLFQKLSIADRPLYLRLLAGPDTEVLSFVLKENETGEVEWDAFSIPELQNFLTILEKEEQDKIQQVQKKYDKFRQKLEEALRESQGKPG
Protein: Stevor (O96111)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKMYYLKMLLFTFLINTLVARHYENFVNNHYNVSLIQNKTKRVTIKSRLLAQTQIHNPHYHNDPELKEIIDKMNEEAIKKYQQTHDPYKQLKEVVEKNGSQNRSGHVAEPMSTLEKELLETYVETFGEESNIMLKSGRYQNGDDVSDDSSSCDCTDINNAKLEKTKGRDKYLKHLKGRCTRGIYFCSAGSALLTLIALIAAKKAALSAVASYAGFKNCMSSIATFKLLDSSTLLSSFLSMKACVVGATDMAGTIATPAMAAFYPYGIAALVLLILAVVLIILYIWLYRRRKHSWKHECKKHLCK
Protein: Interferon regulatory factor 8 (A0A8I5Y754)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MCDRNGGRRLRQWLIEQIDSSMYPGLIWESEEKTLFRIPWKHAGKQDYNQEVDASIFKPSVDEYMGIAKRSPSPPEACRSQILPDWWAQQPNAGLPLVTGYTAYDAHHSALSQMVINFYYGGKLVGQATTTSLEGCRLSLSQPGLPKLYGPDGLEPVCFPAADTIPSERQRQVTRKLFGHLERGVLLHSNRKGVFVKRLCQGRVFCSGNAVVCKGRPNKLERDEVVQVFDTNMFLRDLQQFYATQSRLPDSRVVLCFGEEFPDTAPLRSKLILVQVEQLYARQMVEEAGKSCGAGSLMPALEEPQPDQAFRMFPDICTSHQRPFFRENQQITV
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) (eIF-3-delta) (eIF3 p42) (eIF3 p44) (O75821)
Organism: Homo sapiens (Human)
Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. This subunit can bind 18S rRNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Note=Colocalizes with AIFM1 in the nucleus and perinuclear region.
Interaction partners:
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit C
Sequence:
MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSPEPELLPGAPLPPPKEVINGNIKTVTEYKIDEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN