wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor Sp8 (Q64HY5)
Organism: Gallus gallus (Chicken)
Function: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- TF_AP-2 domain-containing protein.
- GS homeobox 2.
Sequence:
MLAATCNKIGSPSPSPSALSDSASSFGKGFHPWKRSSSSSSASAGSCGAVGSGLPGFGVAGAARNGSSAAAAAAAAAAAALVSDSFSCGGSPGSSAFSLTSSGAAAASSPFANDYSVFQAPGSAGGGGGGGGGGGGAAGQEAAHQPVFISKVHASVEGLQGIYPRVGMAHPYESWFKPSHPGLAAGEVGSAGASSWWDVGAGWIDVQSPNGAAALPGSLHPAAGGLQSSLHSPLGGYNSDYSGLGHSAFGGGASSHLLSPAGQHLMDGFKPVLPGSYPDSAPSPLAGAGGSMLGGGPAAPLSASPRSSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHSCHIPGCGKVYGKTSHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACPVCNKRFMRSDHLSKHVKTHSGPGGAGGPGGGGPGPGPGGKKGSDTDSEHSAAGSPPCHSPELLPPPEPGHRNGLE
Protein: FI21225p1 (Uncoordinated 45, isoform A) (Uncoordinated 45, isoform B) (Q9VHW4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
- Heat shock protein 83
- Heat shock protein 83
- Dilute class unconventional myosin, isoform C
- Ubiquitin conjugation factor E4 B
- Myosin heavy chain, muscle
- Heat shock protein 75 kDa, mitochondrial
- FI06144p
- LD23779p
- Structural maintenance of chromosomes protein 5
Sequence:
MTNTINSEEVSDAGSYKDKGNEAFKASRWEEAVEHYGKAIKAGSKHKELAVFYKNRAAAYLKLGKYENAVEDCTESLKAAPGDPKALFRRAQAYEALEKFEEAYKDATALFKADPGNKTVQPMLQRLHVVVEERSARNAKTSTKVKQMMDLTFDLATPIDKRRAAANNLVVLAKEQTGAELLYKDHCIAKVASLTKVEKDQDIYVNMVHLVAALCENSVERTKGVLTELGVPWFMRVLDQKHENCVSTAQFCLQTILNALSGLKNKPDSKPEKELCTRNNREIDTLLTCLVYSITDRTISGAARDGVIELITRNVHYTALEWAERLVEIRGLCRLLDVCSELEDYKYESAMDITGSSSTIASVCLARIYENMYYDEAKARFTDQIDEYIKDKLLAPDMESKVRVTVAITALLNGPLDVGNQVVAREGILQMILAMATTDDELQQRVSCECLIAASSKKDKAKALCEQGVDILKRLYHSKNDGIRVRALVGLCKLGSYGGQDAAIRPFGDGAALKLAEACRRFLIKPGKDKDIRRWAADGLAYLTLDAECKEKLIEDKASIHALMDLARGGNQSCLYGVVTTFVNLCNAYEKQEMLPEMIELAKFAKQHIPEEHELDDVDFINKRITVLANEGITTALCALAKTESHNSQELIARVLNAVCGLKELRGKVVQEGGVKALLRMALEGTEKGKRHATQALARIGITINPEVSFSGQRSLDVIRPLLNLLQQDCTALENFESLMALTNLASMNESVRQRIIKEQGVSKIEYYLMEDHLYLTRAAAQCLCNLVMSEDVIKMFEGNNDRVKFLALLCEDEDEETATACAGALAIITSVSVKCCEKILAIASWLDILHTLIANPSPAVQHRGIVIILNMINAGEEIAKKLFETDIMELLSGLGQLPDDTRAKAREVATQCLAAAERYRIIERSDNAEIPDVFAENSKISEIIDD
Protein: Cytochrome c oxidase assembly protein COX14 (Q96I36)
Organism: Homo sapiens (Human)
Function: Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. Requires for coordination of the early steps of cytochrome c oxidase assembly with the synthesis of MT-CO1.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:22243966, ECO:0000269|PubMed:22356826, ECO:0000269|PubMed:27184847}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome c oxidase assembly factor 3 homolog, mitochondrial
- Surfeit locus protein 1
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase assembly factor 1 homolog
- Putative protein MSS51 homolog, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase copper chaperone
- HIG1 domain family member 2A, mitochondrial
- Cytochrome c oxidase assembly factor 6 homolog
- Cytochrome b-c1 complex subunit 9
Sequence:
MPTGKQLADIGYKTFSTSMMLLTVYGGYLCSVRVYHYFQWRRAQRQAAEEQKTSGIM
Protein: Evasin P1100 (A0A0K8R556)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL10, CXCL11 and CXCL13.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAFNVITFLQFSVFVVILFNINLHSASAGSKGSSASQSSDNSVVAKFCDTNCTINEGGKWTECKGGCFCVHVGNETVGRCMKLDGDYDYPSPKPEE
Protein: 5-hydroxytryptamine receptor 1 (5-HT receptor) (5HT-dro) (Serotonin receptor 1) (P20905)
Organism: Drosophila melanogaster (Fruit fly)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling activates adenylate cyclase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:2174167}; Multi-pass membrane protein {ECO:0000269|PubMed:2174167}.
Interaction partners:
Sequence:
MALSGQDWRRHQSHRQHRNHRTQGNHQKLISTATLTLFVLFLSSWIAYAAGKATVPAPLVEGETESATSQDFNSSSAFLGAIASASSTGSGSGSGSGSGSGSGSGSYGLASMNSSPIAIVSYQGITSSNLGDSNTTLVPLSDTPLLLEEFAAGEFVLPPLTSIFVSIVLLIVILGTVVGNVLVCIAVCMVRKLRRPCNYLLVSLALSDLCVALLVMPMALLYEVLEKWNFGPLLCDIWVSFDVLCCTASILNLCAISVDRYLAITKPLEYGVKRTPRRMMLCVGIVWLAAACISLPPLLILGNEHEDEEGQPICTVCQNFAYQIYATLGSFYIPLSVMLFVYYQIFRAARRIVLEEKRAQTHLQQALNGTGSPSAPQAPPLGHTELASSGNGQRHSSVGNTSLTYSTCGGLSSGGGALAGHGSGGGVSGSTGLLGSPHHKKLRFQLAKEKKASTTLGIIMSAFTVCWLPFFILALIRPFETMHVPASLSSLFLWLGYANSLLNPIIYATLNRDFRKPFQEILYFRCSSLNTMMRENYYQDQYGEPPSQRVMLGDERHGARESFL
Protein: Peptidyl-lysine N-acetyltransferase PatZ (EC 2.3.1.-) (Protein lysine acetyltransferase) (P76594)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the acetyl-CoA-dependent acetylation of lysine residues of a large number of target proteins. Acetylates RNase R in exponential phase cells and RNase II. Required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits. Also acetylates acetyl-coenzyme A synthetase (Acs) and the chromosomal replication initiator protein DnaA, and inhibits their activity. Overexpression leads to the acetylation of a large number of additional proteins and inhibits motility.
Interaction partners:
- NAD-dependent protein deacylase
- Peptidyl-lysine N-acetyltransferase YjaB
- Peptidyl-lysine N-acetyltransferase YiaC
- Acetyl-coenzyme A synthetase
- tRNA-uridine aminocarboxypropyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
- HTH-type transcriptional regulator UlaR
- [Ribosomal protein bS18]-alanine N-acetyltransferase
- Aminoalkylphosphonate N-acetyltransferase
- PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM
Sequence:
MSQRGLEALLRPKSIAVIGASMKPNRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVLAWPDIASLPFTPDLAVLCTNASRNLALLEELGEKGCKTCIILSAPASQHEDLRACALRHNMRLLGPNSLGLLAPWQGLNASFSPVPIKRGKLAFISQSAAVSNTILDWAQQRKMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILVIKSGRSPAAQRLLNTTAGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDALWSRNGKLATLSEETCQKLRDALPEHVAISNPLDLRDDASSEHYIKTLDILLHSQDFDALMVIHSPSAAAPATESAQVLIEAVKHHPRSKYVSLLTNWCGEHSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYRRNQKQLRETPALPSNLTSNTAEAHLLLQQAIAEGATSLDTHEVQPILQAYGMNTLPTWIASDSTEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTANEVQQAANAIFDRVKMAWPQARVHGLLVQSMANRAGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEDQAVVALPPLNMNLARYLVIQGIKSKKIRARSALRPLDVAGLSQLLVQVSNLIVDCPEIQRLDIHPLLASGSEFTALDVTLDISPFEGDNESRLAVRPYPHQLEEWVELKNGERCLFRPILPEDEPQLQQFISRVTKEDLYYRYFSEINEFTHEDLANMTQIDYDREMAFVAVRRIDQTEEILGVTRAISDPDNIDAEFAVLVRSDLKGLGLGRRLMEKLITYTRDHGLQRLNGITMPNNRGMVALARKLGFNVDIQLEEGIVGLTLNLAQREES
Protein: Motile sperm domain containing 2 (R4GMN1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAENHAQNKAKLISETRRRFEAEYVTDKSDKYDARDVERLQQDDNWVESYLSWRHNIVDETLKMLDESFQWRKEISVNDLNESSIPRWLLEIGVIYLHGYDKEGNKLFWIRVKYHVKDQKTILDKKKLIAFWLERYAKRENGKPVTVMFDLSETGINSIDMDFVRFIINCFKVYYPKYLSKIVIFDMPWLMNAAFKIVKTWLGPEAVSLLKFTSKNEVQDYVSVEYLPPHMGGTDPFKYSYPPLVDDDFQTPLCENGPITSEDETSSKEDIESDGKETLETISNEEQTPLLKKINPTESTSKAEENEKVDSKVKAFKKPLSVFKGPLLHISPAEELYFGSTESGEKKTLIVLTNVTKNIVAFKVRTTAPEKYRVKPSNSSCDPGASVDIVVSPHGGLTVSAQDRFLIMAAEMEQSSGTGPAELTQFWKEVPRNKVMEHRLRCHTVESSKPNTLTLKDNAFNMSDKTSEDICLQFATSSCEMDCSPP
Protein: Cytokine-like protein 1 (Protein C17) (Q9NRR1)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000269|PubMed:10857752}.
Interaction partners:
Sequence:
MRTPGPLPVLLLLLAGAPAARPTPPTCYSRMRALSQEITRDFNLLQVSEPSEPCVRYLPRLYLDIHNYCVLDKLRDFVASPPCWKVAQVDSLKDKARKLYTIMNSFCRRDLVFLLDDCNALEYPIPVTTVLPDRQR
Protein: Natural cytotoxicity triggering receptor 1 (Activating receptor 1) (mAR-1) (Lymphocyte antigen 94) (Natural killer cell p46-related protein) (NK-p46) (NKp46) (mNKp46) (CD antigen CD335) (Q8C567)
Organism: Mus musculus (Mouse)
Function: Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit gamma
- T-cell surface glycoprotein CD3 zeta chain
- NKG2-D type II integral membrane protein
- TYRO protein tyrosine kinase-binding protein
- Properdin
- MHC class I-like protein MILL2
- Low affinity immunoglobulin gamma Fc region receptor III
- UL16 binding protein 1
- Killer cell lectin-like receptor subfamily C, member 1
- Killer cell lectin-like receptor subfamily B member 1C
Sequence:
MLPTLTALLCLGLCLSQRINTEKETLPKPIIWAKPSIMVTNGNSVNIWCQGAQSASEYQLYFEGSFFALERPKPSRSMNKVRFFISQMTSHTAGIYTCFYQSGELWSKSSNPLKLVVTGLYDTPNLWVYPRPEVTLGENVTFFCQLKTATSKFFLLKERGSNHIQNKYGNIQAEFPMGPVTRAHRGTYRCFGSYNDYAWSFPSEPVTLLITGGVENSSLAPTDPTSSLDYWEFDLSTNESGLQKDSAFWDHTTQNLIRIGLACIILITLVWLLTEDWLSKRKDHEEANRLTNWECRRRWRMQHYFEEEQRNAISMMELKATPGAL
Protein: RBR-type E3 ubiquitin transferase (EC 2.3.2.31) (H7C3G0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XYRPTWDLALDPLVSCKLCLGEYPVEQMTTIAQCQCIFCTLCLKQYVELLIKEGLETAISCPDAACPKQGHLQENEIECMVAAEIMQRYKKLQFEREVLFDPCRTWCPASTCQAVCQLQDVGLQTPQPVQCKACRMEFCSTCKASWHPGQGCPETMPITFLPGETSAAFKMEEDDAPIKRCPKCKVYIERDEGCAQMMCKNCKHAFCWYCLESLDDDFLLIHYDKGPCRNKLGHSRASVIWHRTQGDAILEKCILHNTESECHL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q5I6E9)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Interaction partners:
Sequence:
MERIPEVRESTRQFPIGAKVAHTFSTSKKEVGIRGFRDFDLAIPIQTWKGKTSYQEEEDLMVDAGTIKRSDDSLEDSGSTSFHGASHPPEPVDTDLMRPVYVPIGQNKADGKCLVKNVSLKGPFLDDLSIRMPNVKPSPSLLSPAESLVEEPNDLGVISSPFTVPRPSQNTETSLPPDSEEKECIWDASLPPSGNVSPLSSIDSTGVVRSMSIVNSCTSTYRSDVLMSDGMLSVDRNYESTKGSIRGDSLESGKTSLSRASDSSGLSDDSNWSNITGSANKPHKGNDPRWKAILAIRARDGILGMSHFKLLKRLGCGDIGSVYLSELSGTRCYFAMKVMDKASLASRKKLTRAQTEREILQLLDHPFLPTLYTHFETDRFSCLVMEYCPGGDLHTLRQRQPGKHFSEYAARFYAAEVLLALEYLHMLGVVYRDLKPENVLVRDDGHIMLSDFDLSLRCAVSPTLIRISSDDPSKRGAAFCVQPACIEPTTVCMQPACFLPRLFPQKSKKKTPKPRADSGFQANSMPELVAEPTSARSMSFVGTHEYLAPEIIKGEGHGSAVDWWTFGIFLHELLYGKTPFKGSGNRATLFNVVGQQLKFPDSPATSYASRDLIRGLLVKEPQNRLGVKRGATEIKQHPFFEGVNWALIRCSTPPEVPRPVEPDYPAKYGQVNPVGVGNTSKRVVGADAKSGGKYLDFEFF
Protein: SPARC-related modular calcium-binding protein 1 (Secreted modular calcium-binding protein 1) (SMOC-1) (Q9H4F8)
Organism: Homo sapiens (Human)
Function: Plays essential roles in both eye and limb development. Probable regulator of osteoblast differentiation.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:12130637, ECO:0000269|PubMed:20359165}. Note=In or around the basement membrane.
Interaction partners:
- SPARC
- Follistatin
Sequence:
MLPARCARLLTPHLLLVLVQLSPARGHRTTGPRFLISDRDPQCNLHCSRTQPKPICASDGRSYESMCEYQRAKCRDPTLGVVHRGRCKDAGQSKCRLERAQALEQAKKPQEAVFVPECGEDGSFTQVQCHTYTGYCWCVTPDGKPISGSSVQNKTPVCSGSVTDKPLSQGNSGRKDDGSKPTPTMETQPVFDGDEITAPTLWIKHLVIKDSKLNNTNIRNSEKVYSCDQERQSALEEAQQNPREGIVIPECAPGGLYKPVQCHQSTGYCWCVLVDTGRPLPGTSTRYVMPSCESDARAKTTEADDPFKDRELPGCPEGKKMEFITSLLDALTTDMVQAINSAAPTGGGRFSEPDPSHTLEERVVHWYFSQLDSNSSNDINKREMKPFKRYVKKKAKPKKCARRFTDYCDLNKDKVISLPELKGCLGVSKEGRLV
Protein: PAC1 receptor short isoform (Pituitary adenylate cyclase-activating polypeptide type I receptor isoform 3 precursor) (Q5C8V0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MYRQAARETFLILFLIISLMWPIHSEISNCVIKREEERCLERIALHDPKDDQKFECPWEWDNLTCWQAASVGDVVEVNCPELFEFMSPEEGLGKISRNCTEFGWSEPYPHYVDACMTDENTTKPDMYYASVKALYTVGYSTSLVSLTTAMVILCRFRKLHCTRNFIHMNLFVSFILRAISVFIKDGVLYAEEDSDHCFVHTVGCKAVMVFFHYCVMSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTICVTIWAVLRLHFDDSGCWDMNDNTALWWVIKGPVVASIMINFVLFIGIIIILVQKLQSPDIGGNESSIYLRLARSTLLLIPLFGIHYTVFAFSPEDFSKRERLVFELGLGSFQGFVVAVLYCFLNGEAQSEIKRKWRSWTVNRYFAVDLKQQRHPSLASSGVNGGTQLSILSKSSSQIRMSSPLAETVNLNLPT
Protein: RE47911p (Spitting image) (Q8SYP8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MEILRTKLEACLLILNRNNAAAANWLNDLCAVLLEFATLAHSSFCSQGQSECSELVCLCLSQIMICIRQVENTMKLECGTTVSVSHQYFLDRIRWCLKRLMHLYSEESSSEAVAPERSFLKLVDGALDCLAQFTSHSEENTDTSNCPKTPKEVLPLSQKLRANIDLILGQSLGFANVALSQDKRALSALCQKVIRECNAFQEECKESFSANYLSTLKLRAMTMEQAIYQLEDFINDALLRLVFTCFLDFEKFSVDKIRALLRNSPDNDDLADEFIADFDVNIDRATQIGIFAISFAPNLKMKTIMRSCLASFESLDTTLIPSLQAHGSDLHSDILEQHFNEEVAKFKAALQEIIDSRALVGCCLEILTSGISATEKLFDKQRLEDLVQISLLLVEHFQLEVNRKGLSETQDRLGEEYYQQFIRVLRECKAILMCASQVEPQRILKRFKILRTILRKLHGSLGAGKQEEELPIPLAPLLADDTKGVNEDETHFTGYKTARSGSILYDTERRNRVTRRTDNKLPTNTLDIKSDKAKPHGNVLRRESLRTVMFKRQNIAESRKLYTSMSNQSTDLQITDILDQLTGMSNGYFEC
Protein: Uncharacterized protein (Q38CE1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAAVMKLEKFFVATLIVAVTRCFAEEVDTVAPGKAPPQDVVNTLCGAKHLLEAVNKKAGTLASEVEKHVTDAKASLDGTVKASKSTQTLYEKLQKDVMDAGLTAVVVERMKGIADAAVEVAASAEEAYEKVIRTNESVGTAAAEIETSSNHSANLIDKILMATAGVEDKETEEDFCSGVENKYGDGLKNASRPHCRLFDNCKLDDINGKAWQPTHMELVITYHGICYRLDAVELSMGIAKDAATKASQMKTRAEEGMASAYQESIVVAREIAGEAERKRLLAEKELAETREKAAADAKARKEAEEEMRRRAERERAEKEEAVARAERMEKKGKTVAEVVVKAEHDQKAKDGASDISSRRIGSLWSPLRDVWLILPAASLCLWTQ
Protein: DNA topoisomerase large subunit (EC 5.6.2.2) (DNA topoisomerase 64-kDa subunit) (Protein Gp39) (P09176)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Large subunit of the DNA topoisomerase that untwists superhelical DNA. Controls of topological states of double-stranded DNA by transient breakage and subsequent rejoining of DNA strands.
Interaction partners:
Sequence:
MIKNEIKILSDIEHIKKRSGMYIGSSANETHERFMFGKWESVQYVPGLVKLIDEIIDNSVDEGIRTKFKFANKINVTIKNNQVTVEDNGRGIPQAMVKTPTGEEIPGPVAAWTIPKAGGNFGDDKERVTGGMNGVGSSLTNIFSVMFVGETGDGQNNIVVRCSNGMENKSWEDIPGKWKGTRVTFIPDFMSFETNELSQVYLDITLDRLQTLAVVYPDIQFTFNGKKVQGNFKKYARQYDEHAIVQEQENCSIAVGRSPDGFRQLTYVNNIHTKNGGHHIDCAMDDICEDLIPQIKRKFKIDVTKARVKECLTIVMFVRDMKNMRLIRQTKERLTSPFGEIRSHIQLDAKKISRDILNNEAILMPIIEAALARKLAAEKAAETKAAKKASKAKVHKHIKANLCGKDADTTLFLTEGDSAIGYLIDVRDKELHGGYPLRGKVLNSWGMSYADMLKNKELFDICAITGLVLGEKAFEEKEDGEWFTFELNGDTIIVNENDEVQINGKWITVGELRKNL
Protein: Cytochrome b6-f complex subunit 8 (Cytochrome b6-f complex subunit PetN) (Cytochrome b6-f complex subunit VIII) (P0C396)
Organism: Oryza sativa subsp. indica (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MDIVSLAWAALMVVFTFSLSLVVWGRSGL
Protein: Phosphotransferase (EC 2.7.1.-) (G5EB08)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Glucokinase regulator family protein, putative
Sequence:
MASVDPAHSRLHTVEEHVIIHDDPIDDDEEHEEDDAEMDPSVRACLEHQRKVDEFLSPLCLDEAVLYKLARRLSSVYRKLALESDQQFLPTPVSKLPSGLETGRYLAIDVGGSNLRVAFIELLGDTADPDMARTSASERPLKKAQTQRVKRTLEKAWPIQEHLKMDKAEDLFAWIGDCIAEVVAESLSSDATKNAVPEELEMGITFSFPMMQESLAEATLMPMGKGFAITSDLNLRNILLSGYERHTRRPDDEDQPSTKRRKLYALPKLKISAITNDAVATLASLAYAVKSLPNSRVAMGLIVGTGCNATIPMKLSALHEDKVKHVRRSDPETSGIIVNTEWTIYGVLPPLKELNIITKWDAELDASSARPGFQPFEYMTGGRYIGELIRLIFTDYLINVAGVSTAALPATLTQGYALTTSYISDKVARARSDEELTDELAHSLPPPSDTWQWDATSAGVLRTVARTVQRRSAGLVAAAVVGLLACAGEIELRLDSPQGSPQDSHAASPERDSITTLSAQLKSEGSASNGFRGPIVPIISPTPADWQSGPEELVVACTGGIIQHYPNFKEMCQQTIDRLIMRTGPQKSGKSVFLREASDGGVIGAGVLAGMVGNR
Protein: Connector enhancer of kinase suppressor of ras 2 (Connector enhancer of KSR 2) (CNK homolog protein 2) (CNK2) (Q8WXI2)
Organism: Homo sapiens (Human)
Function: May function as an adapter protein or regulator of Ras signaling pathways.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein.
Interaction partners:
- Kinase suppressor of Ras 1
- RAF proto-oncogene serine/threonine-protein kinase
- Ras-related protein Ral-A
- Serine/threonine-protein kinase B-raf
- Rho GTPase-activating protein 39
- GTPase HRas
- Leucine-rich repeat-containing protein 7
Sequence:
MALIMEPVSKWSPSQVVDWMKGLDDCLQQYIKNFEREKISGDQLLRITHQELEDLGVSRIGHQELILEAVDLLCALNYGLETENLKTLSHKLNASAKNLQNFITGRRRSGHYDGRTSRKLPNDFLTSVVDLIGAAKSLLAWLDRSPFAAVTDYSVTRNNVIQLCLELTTIVQQDCTVYETENKILHVCKTLSGVCDHIISLSSDPLVSQSAHLEVIQLANIKPSEGLGMYIKSTYDGLHVITGTTENSPADRCKKIHAGDEVIQVNHQTVVGWQLKNLVNALREDPSGVILTLKKRPQSMLTSAPALLKNMRWKPLALQPLIPRSPTSSVATPSSTISTPTKRDSSALQDLYIPPPPAEPYIPRDEKGNLPCEDLRGHMVGKPVHKGSESPNSFLDQEYRKRFNIVEEDTVLYCYEYEKGRSSSQGRRESTPTYGKLRPISMPVEYNWVGDYEDPNKMKRDSRRENSLLRYMSNEKIAQEEYMFQRNSKKDTGKKSKKKGDKSNSPTHYSLLPSLQMDALRQDIMGTPVPETTLYHTFQQSSLQHKSKKKNKGPIAGKSKRRISCKDLGRGDCEGWLWKKKDAKSYFSQKWKKYWFVLKDASLYWYINEEDEKAEGFISLPEFKIDRASECRKKYAFKACHPKIKSFYFAAEHLDDMNRWLNRINMLTAGYAERERIKQEQDYWSESDKEEADTPSTPKQDSPPPPYDTYPRPPSMSCASPYVEAKHSRLSSTETSQSQSSHEEFRQEVTGSSAVSPIRKTASQRRSWQDLIETPLTSSGLHYLQTLPLEDSVFSDSAAISPEHRRQSTLPTQKCHLQDHYGPYPLAESERMQVLNGNGGKPRSFTLPRDSGFNHCCLNAPVSACDPQDDVQPPEVEEEEEEEEEEGEAAGENIGEKSESREEKLGDSLQDLYRALEQASLSPLGEHRISTKMEYKLSFIKRCNDPVMNEKLHRLRILKSTLKAREGEVAIIDKVLDNPDLTSKEFQQWKQMYLDLFLDICQNTTSNDPLSISSEVDVITSSLAHTHSYIETHV
Protein: E1B 55 kDa protein (E1B-55K) (E1B protein, large T-antigen) (E1B-495R) (P03244)
Organism: Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Function: Plays a major role to prevent cellular inhibition of viral genome replication. Assembles an SCF-like E3 ubiquitin ligase complex based on the cellular proteins ELOB, ELOC, CUL5 and RBX1, in cooperation with viral E4orf6. This viral RING-type ligase ubiquitinates cellular substrates and targets them to proteasomal degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3, DAXX and BLM. Degradation of host TP53/p53 activity is essential for preventing E1A-induced TP53 accumulation that would otherwise lead to cell apoptosis and growth arrest. E1B-55K also inactivates TP53 transcription-factor activity by binding its transactivation domain. E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies thereby contributing to maximal inhibition of TP53 function.
Subcellular location: Host nucleus {ECO:0000269|PubMed:10211970}. Host cytoplasm {ECO:0000269|PubMed:10211970}. Note=Colocalizes with host TP53 to host PML nuclear bodies. PML localization of E1B-55K is necessary for E1B-55K-dependent SUMOylation of TP53. {ECO:0000250|UniProtKB:P03243}.
Interaction partners:
Sequence:
MERRNPSERGVPAGFSGHASVESGGETQESPATVVFRPPGNNTDGGATAGGSQAAAAAGAEPMEPESRPGPSGMNVVQVAELFPELRRILTINEDGQGLKGVKRERGASEATEEARNLTFSLMTRHRPECVTFQQIKDNCANELDLLAQKYSIEQLTTYWLQPGDDFEEAIRVYAKVALRPDCKYKISKLVNIRNCCYISGNGAEVEIDTEDRVAFRCSMINMWPGVLGMDGVVIMNVRFTGPNFSGTVFLANTNLILHGVSFYGFNNTCVEAWTDVRVRGCAFYCCWKGVVCRPKSRASIKKCLFERCTLGILSEGNSRVRHNVASDCGCFMLVKSVAVIKHNMVCGNCEDRASQMLTCSDGNCHLLKTIHVASHSRKAWPVFEHNILTRCSLHLGNRRGVFLPYQCNLSHTKILLEPESMSKVNLNGVFDMTMKIWKVLRYDETRTRCRPCECGGKHIRNQPVMLDVTEELRPDHLVLACTRAEFGSSDEDTD
Protein: Protein-S-isoprenylcysteine O-methyltransferase (EC 2.1.1.100) (Isoprenylcysteine carboxylmethyltransferase) (Prenylated protein carboxyl methyltransferase) (PPMT) (Prenylcysteine carboxyl methyltransferase) (pcCMT) (Q558K8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Methylates the C-terminal cysteine residues of small GTPases and the heterotrimeric G protein gamma subunit in response to cAMP. The methylation is required for intercellular signaling and regulation of cAMP waves propagation. It also seems to induce the activity of car1, a G protein-coupled receptor which senses extracellular cAMP during the aggregation phase of development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60725}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- CAAX prenyl protease 1 homolog
- intramembrane prenyl-peptidase Rce1
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein farnesyltransferase subunit beta
- Geranylgeranyl transferase type-2 subunit alpha
Sequence:
MDQSEIVKLNKIKAKSAWLKKGAARSSAISCGLGIGIGFGIALFIFSQTLRGFGIYLAGLCTFHMWEYIWVTMYHPDKLSSKSFLLNHSPQFNMALLISFIEFWIEWYFFPSLKTFSLWWVGAICMVFGQIVRSVAMDTAGSNFTHLVQEEKRDDHVLVTNGIYQYMRHPSYFGWFVWSVSTQVILMNPISIIGFGWASWSFFSQRIENEEDYLIQFFGKSYKDYKKSVWSGIPGIH
Protein: Large ribosomal subunit protein uL11 (50S ribosomal protein L11) (P56210)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Interaction partners:
Sequence:
MKLQIPAGKANPAPPVGPALGQAGVNIMAFCKEFNARTADQAGLIIPVEITVFEDRSFTFITKTPPAAVLLKKAAGIESGSGEPNRNKVATIKRDKVREIAELKMPDLNAASIEAAMRMIEGTARSMGIVVED
Protein: glutamate dehydrogenase [NAD(P)(+)] (EC 1.4.1.3) (Q8T453)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYLMVDLRAAFVSIPRSIQWMSCRRSHGDLFLKDKEWMDLLKWKTGWKDKTVIVQGFGNVGSFAAKYVHEAGAKVIGIKEFDVSLVNKDGIDINDLFEYTEEKKTIKGYPKAQESKEDLLVAETDILMPCATQKVITTDNAKDIKAKLILEGANGPTTPSGEKILLDKGVLLVPDLYCNAGGVTVSYFEYLKNINHVSYGKMNSKSTSELIIELMNSINESLHECPDSQLPNICPNKKLKRIQQCTTEADIVDSALQTVMESAARGIKEMAHKFELCNDLRRAAYVWSSFKIFQAMESSGISQQ
Protein: RNA-directed RNA polymerase L (Protein L) (EC 2.7.7.48) (Large structural protein) (Replicase) (Transcriptase) (P52639)
Organism: Borna disease virus (strain V) (BDV)
Function: Displays RNA-directed RNA polymerase activity. The mRNA guanylyl transferase and mRNA (guanine-N(7)-)-methyltransferase activities are supposedly provided by cellular enzymes. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). Functions either as transcriptase or as replicase. The transcriptase synthesizes subsequently three subgenomic RNAs, assuring their capping and polyadenylation by a stuttering mechanism. In replicase mode, the polymerase replicates the whole viral genome without recognizing the transcriptional signals.
Subcellular location: Virion {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:12134049}.
Interaction partners:
Sequence:
MSFHASLLREEETPRPVAGINRTDQSLKNPLLGTEVSFCLKSSSLPHHVRALGQIKARNLASCDYYLLFRQVVLPPEVYPIGVLIRAAEAILTVIVSAWKLDHMTKTLYSSVRYALTNPRVRAQLELHIAYQRIVGQVSYSREADIGPKRLGNMSLQFIQSLVIATIDTTSCLMTYNHFLAAADTAKSRCHLLIASVVQGALWEQGSFLDHIINMIDIIDSINLPHDDYFTIIKSIFPYSQGLVMGRHNVSVSSDFASVFAIPELCPQLDSLLKKLLQLDPVLLLMVSSVQKSWYFPEIRMVDGSREQLHKMRVELETPQALLSYGHTLLSIFRAEFIKGYVSKNAKWPPVHLLPGCDKSIKNARELGRWSPAFDRRWQLFEKVVILRIADLDMDPDFNDIVSDKAIISSRRDWVFEYNAAAFWKKYGERLERPPARSGPSRLVNALIDGRLDNIPALLEPFYRGAVEFEDRLTVLVPKEKELKVKGRFFSKQTLAIRIYQVVAEAALKNEVMPYLKTHSMTMSSTALTHLLNRLSHTITKGDSFVINLDYSSWCNGFRPELQAPICRQLDQMFNCGYFFRTGCTLPCFTTFIIQDRFNPPYSLSGEPVEDGVTCAVGTKTMGEGMRQKLWTILTSCWEIIALREINVTFNILGQGDNQTIIIHKSASQNNQLLAERALGALYKHARLAGHNLKVEECWVSDCLYEYGKKLFFRGVPVPGCLKQLSRVTDSTGELFPNLYSKLACLTSSCLSAAMADTSPWVALATGVCLYLIELYVELPPAIIQDESLLTTLCLVGPSIGGLPTPATLPSVFFRGMSDPLPFQLALLQTLIKTTGVTCSLVNRVVKLRIAPYPDWLSLVTDPTSLNIAQVYRPERQIRRWIEEAIATSSHSSRIATFFQQPLTEMAQLLARDLSTMMPLRPRDMSALFALSNVAYGLSIIDLFQKSSTVVSASQAVHIEDVALESVRYKESIIQGLLDTTEGYNMQPYLEGCTYLAAKQLRRLTWGRDLVGVTMPFVAEQFHPHSSVGAKAELYLDAIIYCPQETLRSHHLTTRGDQPLYLGSNTAVKVQRGEITGLAKSRAANLVKDTLVLHQWYKVRKVTDPHLNTLMARFLLEKGYTSDARPSIQGGTLTHRLPSRGDSRQGLTGYVNILSTWLRFSSDYLHSFSKSSDDYTIHFQHVFTYGCLYADSVIRSGGVISTPYLLSASCKTCFEKIDSEEFVLACEPQYRGAEWLISKPVTVPEQITDAEVEFDPCVSASYCLGILIGKSFLVDIRASGHDIMEQRTWANLERFSVSDMQKLPWSIVIRSLWRFLIGARLLQFEKAGLIRMLYAATGPTFSFLMKVFQDSALLMDCAPLDRLSPRINFHSRGDLVAKLVLLPFINPGIVEIEVSGINSKYHAVSEANMDLYIAAAKSVGVKPTQFVEETNDFTARGHHHGCYSLSWSKSRNQSQVLKMVVRKLKLCVLYIYPTVDPAVALDLCHLPALTIILVLGGDPAYYERLLEMDLCGAVSSRVDIPHSLAARTHRGFAVGPDAGPGVIRLDRLESVCYAHPCLEELEFNAYLDSELVDISDMCCLPLATPCKALFRPIYRSLQSFRLALMDNYSFVMDLIMIRGLDIRPHLEEFDELLVVGQHILGQPVLVEVVYYVGVVRKRPVLARHPWSADLKRITVGGRAPCPSAARLRDEDCQGSLLVGLPAGLTQLLIID