wanglab/gogpt-training-data huggingface dataset:
Protein: Dolichyldiphosphatase (EC 3.6.1.43) (Dolichyl pyrophosphate phosphatase) (P53223)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-essential protein which is required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11504728}; Multi-pass membrane protein {ECO:0000269|PubMed:11504728}.
Interaction partners:
- Dolichol kinase
- Dolichyl-phosphate beta-glucosyltransferase
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dolichol-phosphate mannosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1
- Dehydrodolichyl diphosphate synthase complex subunit RER2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4
Sequence:
MNSTAAAINPNPNVIPFDDTYILYDSHDFLSFLSAYFSLMPILVLAFYLSWFIITRELEACIVAFGQLMNEIFNNVIKNIIKQPRPVSFGASFQNDTIRSGYGMPSAHSQFMGFCFTYNSLKIYTSWKNLNFLEKCIFSGALALLSFCVCFSRVYLHYHNLDQVIVGFSVGALTGSLYFFIVGIIRELGLINWFLKLRIVRLFYMTDSYNLAPLTLKENYEAYWKRINQRSFNDKSKRD
Protein: Uncharacterized oxidoreductase C663.09c (EC 1.-.-.-) (Q7Z9I2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MATTNKVYFIAGGNRGIGLSLVKELSSREGTTVFASARKPEAATELQEWSKSHPNVKTVELDVTSQQSANEAAQSVAKAVDGIDVLWLNSGICQSYYTVMEAPEEVWNAHYQTNVLGPIHVFKAFYPLLTKKKTRQVIFTSSECGSMGDFRATGFSAYGQSKAAINFTMKELSVELADEHFTFISIHPGVVKTDMNADAIKKFTETSPEMLTYLKKVTIIPEESVSSMLKVVDNLKPENNGSFYRYDGTIIPF
Protein: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit I) (NDH subunit I) (NADH-plastoquinone oxidoreductase subunit I) (P0C385)
Organism: Oryza sativa subsp. indica (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01351}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01351}.
Interaction partners:
- NAD
- NAD
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NAD
- NAD
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase iron-sulfur protein 6
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NAD
Sequence:
MFPMVTGFMSYGQQTIRAARYIGQSFIITLSHTNRLPITIHYPYEKSITSERFRGRIHFEFDKCIACEVCVRVCPIDLPLVDWRFEKDIKRKQLLNYSIDFGVCIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALSRLPISIMGDYTIQTIRNSTQSKIDEEKSWNSRTITDY
Protein: Enoyl reductase (ER) domain-containing protein (G8BBN0)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Pyruvate decarboxylase
- Aldehyde dehydrogenase domain-containing protein
- Aldehyde dehydrogenase domain-containing protein
- Pyruvate decarboxylase
- Enoyl reductase
- Aldehyde dehydrogenase domain-containing protein
- Aldehyde dehydrogenase
- S-
- catechol O-methyltransferase
- MADS-box domain-containing protein
Sequence:
MSIPSSQYGFVFNKQSGLNLRNDLPVHKPKAGQLLLKVDAVGLCHSDLHVIYEGLDCGDNYVMGHEIAGTVAAVGDDVINYKVGDRVACVGPNGCGGCKYCRGAIDNVCKNAFGDWFGLGYDGGYQQYLLVTRPRNLSRIPDNVSADVAAASTDAVLTPYHAIKMAQVSPTSNILLIGAGGLGGNAIQVAKAFGAKVTVLDKKKEARDQAKKLGADAVYETLPESISPGSFSACFDFVSVQATFDVCQKYVEPKGVIMPVGLGAPNLSFNLGDLALREIRILGSFWGTTNDLDDVLKLVSEGKVKPVVRSAKLKELPEYIEKLRNNAYEGRVVFNP
Protein: Spectrin beta chain (Q6XDA0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTSATEFENVGNQPPYSRINARWDAPDDELDNDSSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRISDLYKDLRDGRMLIKLLEVLSGEMLPRPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGRETRSAKDALLLWCQMKTAGYPQVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFDVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQTISVLNSRKFANSLSGVQQQLQAFSTYRTVEKPPKFQEKGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYQRELALRSELIRQEKLEQLARRFDRKAAMRETWLNENQRLVTQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVKALEDLAQELEKENYHDQKRISARKNNILRLWSYLQELLRSRRQRLEATLALQKLFQDMLHSIDWMDEIKAHILSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKTITAATLQFTEGKGYQPCDPQVIQDRVSHLEQCFSELSNMAAGRKAQLEQSKRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLKQIFQEAEDMVAQKQFGHPQIETRVKEVSAQWDHLKELAAFRKKDLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKEFLEELEESRGVMEHLENQAQGFPEEFRDSPDVTNRLQALRKLYQQVMAQAELRGHKLQEALDLYTVFGESDACELWMTEKGKWLDQMDIPNTLEDLEVVQHRFDILDQEMKTLMAQIDGVNLAANNLVESGHPRSGEVKQYQDRLNKRWQAFQAVVSEQREAVDSALRVNNYCVDCEETSKWIVDKTKVVESTKDLGQDLAGVIAIQRKLSGLERDVLAIRDRVSALERESQYLMESHPDQKEDIGQRQADVEKMWKGLQDALQGQELSLGEASKLQAFLQDLDDFKAWLSMAQKAVASEDMPESLPEAEQLLQQHAAIKEEIDAHKDDYHRVKASGEKVIEGQTDPDYQLLGQRLEGLDTDWDALWRMWESRGNTLTQCLGFQEFQKDAKQAEAILSNQEYTLAHLEPPDSLAAAEAGIRKFEDFLVSMENNRDKVLSPVDSGNMLVSEGNLYSNKIKEKVQLIEDRHMKNNEKAQEVTALLKDNLELQNFLQNCKELTLWINDKLLTSPDISYDEARNLHNKWMKHQAFMAELASHQGWLENIVAEGRQLMAEKPQFTDVVSERLEALHKLWDELQTTTKAKTEQLSAARSSDLRLQTHADLSKWISAMEDQLRSDDLGKDLTTVNRMLVKLKRVEEQVNLRKEELEELFAEAPPLGAEAGDTDMSIEKRFLDLLEPLGRRKKQLELSKAKLQISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHAPRVEDVLHRGQELVKAAEIDCQDIEERLGHLQSSWDTLREAAAGRLQRLREAHEAQQYYLDAGEAEAWISEQELYVFSDEPPKDEEGAIVMLKRHLRQQRTVEEYGRNIKQLAGRAQSLLSAGHPEGEQIIRLQGQVDKQYAGLKDMAEERRRKLENMYHLFQLKREADDLEQWITEKEMVASSQEMGQDFDHVTMLRDKFRDFARETGAIGQERVDNVNSIIERLIDAGHSEAATIAEWKDGLNDMWADLLELIDTRMQLLAASYDLHRYFYTGTEILGLIDEKHRELPEDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEKADAIQSKEQEVSAAWQALLDACAGRRAQLVDTADKFRFFSMVRDLLSWMESIIRQIETQERPRDVSSVELLLKYHQGIKAEINTRAKNFSTCLELGESLLQRQHQASDEIREKLQQVISRRQEMNDKWEARSDRLHMLLEVCQFSRDASVAEAWLIAQEPYLASRDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEKPTTLELKERQTPDRPTEEPGPQEEEGETAGEAPQVHHAATERTSPVSFMSRLSSSWESLLPEPAHPF
Protein: Splicing factor 3B subunit 6 (Pre-mRNA branch site protein p14) (SF3b 14 kDa subunit) (SF3B14a) (Spliceosome-associated protein, 14-kDa) (Splicing factor 3b, subunit 6, 14kDa) (Q9Y3B4)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Directly contacts the pre-mRNA branch site adenosine for the first catalytic step of splicing. Enters the spliceosome and associates with the pre-mRNA branch site as part of the 17S U2 or, in the case of the minor spliceosome, as part of the 18S U11/U12 snRNP complex, and thus may facilitate the interaction of these snRNP with the branch sites of U2 and U12 respectively.
Subcellular location: Nucleus {ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300}.
Interaction partners:
- Splicing factor 3B subunit 4
- Splicing factor 3B subunit 1
- Splicing factor 3A subunit 2
- Splicing factor 3B subunit 5
- Splicing factor 3B subunit 2
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 3
- Splicing factor U2AF 65 kDa subunit
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein G
Sequence:
MAMQAAKRANIRLPPEVNRILYIRNLPYKITAEEMYDIFGKYGPIRQIRVGNTPETRGTAYVVYEDIFDAKNACDHLSGFNVCNRYLVVLYYNANRAFQKMDTKKKEEQLKLLKEKYGINTDPPK
Protein: Regulator of spindle assembly protein 2 (G5EFV3)
Organism: Caenorhabditis elegans
Function: Recruits rsa-1 and, thereby, phosphatase let-92/paa-1 complex to the centrosomes. Recruits sys-1/beta-catenin to mitotic centrosomes during the first embryonic cell divisions.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17218259, ECO:0000269|PubMed:25819561}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A regulatory subunit rsa-1
- Spindle-defective protein 5
- TPX2 domain-containing protein
- Spindle-defective protein 2
- Aurora kinase
- Serine/threonine-protein phosphatase 2A catalytic subunit
- Microtubule End Binding Protein
- Transforming acid coiled-coil-containing protein 1
- Kinesin-like protein
Sequence:
MSKIPVFKGSFKSWLAKNDEKPAKSVLLEPKYRDHHEKIRNKENMEEGEKPVFVSMANPQPTREDYERYDEDRRLKDKARDLRIARRRNSATPEASPSSDQYFTPEPADDEFVTPSTSKKSQKPRSSDATPVSSKPPRYLPRTPLSEQYTSCLSRKMEENFSRMQELMISGHSPHEARQQTIQESSEQLEPRAKVTRSSSQPPPIDTLKPRVPRIESPLVKKTTETPIRRTSYVDTLVATHQIQLQYSDRVVVGVERQMTKLESIKNLAAANRSPIIAEEAKKRRNEAEAVRKLIEVETQNAKKRAVIQELKDRIDKLTQAQLAIHQLVSSQPFSGDPYNQRLLRSIDNWMALPFREFDIQTAREMLELARKMKITIDHFRNVATLHRNSKSLNRSLNTSRKSIAVKINPSSQLNQQSSSDAAPPPSMREASTQMTSRLAESAMTQTSPRRIGVEPLDLSQLLEKHNSSSQTTPPVVEPVLAEVSAEPQRPPVTLSMTAPVSTIAEFDSMLNSISLHNESLETVAEPFSRLKTDISFPSTVEETTPRSGRVSLDSESARRLSAGLSHYLEQVKKERESMEAQESESESMELEIPVVSEVSVTTESENLEEVVSEHSDSKSPETLVASDNGEDSSGGSEDPNATQFEHEIEEHKEPEKLGLIIDPEDEQDETKRFVNHDEFEQSLEEELEPRGNNDSADDSGFLLDNSPAPRLKSIFDNLPPAAASAAVTDTPRVPAEADETTFAGMDMEEYCQREFLKEISPIMVQKAIELQDELRGVDWLTAQDVWQPPSFKDVQMEFDDNFEYFDSFSILIWSAVVDLINKNYLKFGRKMTENEEIAFEAEALKMLQTEHGPESRKSEWCTDVKMSKKLEGMMPMELDYRYDVRRGLPDAEKQKYQWQQVQMTVIAARYANKNLINEANEVYATEKEKLGQMVLESEIDATVTDV
Protein: ATP-dependent RNA helicase fal1 (EC 3.6.4.13) (Q10055)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Uncharacterized RNA-binding protein C23A1.09
- Protein mago nashi homolog
- Pre-mRNA-splicing factor cwf22
- Suppressor of glycerol defect protein 1
- Uncharacterized protein C18B11.06
- Nonsense-mediated mRNA decay protein 3
- Probable ATP-dependent RNA helicase prh1
- Protein pxr1
- Uncharacterized RNA-binding protein C106.12c
- ATP-dependent helicase upf1
Sequence:
MADEIMENVELTTSEDVNAVSSFEEMNLKEDLLRGIYAYGYETPSAVQSRAIIQICKGRDVIAQAQSGTGKTATFSIGILQSIDLSVRDTQALILSPTRELAVQIQNVVLALGDHMNVQCHACIGGTSVGNDIKKLDYGQHVVSGTPGRVTDMIRRRNLRTRNVKMLILDEADELLNQGFKEQIYDIYRYLPPGTQVVVVSATLPQDVLEMTNKFTTNPVRILVKRDELTLEGLKQYFIAVEKEEWKFDTLCDLYDTLTITQAVIFCNSRRKVDWLTEKMREANFTVTSMHGEMPQKERDAIMQDFRQGNSRVLICTDIWARGIDVQQVSLVINYDLPANRENYIHRIGRSGRFGRKGVAINFVTNEDVRILRDIEQYYSTVIDEMPMNIGDMV
Protein: 26S proteasome non-ATPase regulatory subunit 1 homolog B (26S proteasome regulatory subunit RPN2b) (AtRPN2b) (26S proteasome regulatory subunit S1 homolog B) (Q9MAT0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome non-ATPase regulatory subunit 3 homolog B
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- 26S proteasome non-ATPase regulatory subunit 7 homolog B
- 26S proteasome regulatory subunit 8 homolog A
- 26S proteasome regulatory subunit 6A homolog A
- 26S proteasome regulatory subunit 4 homolog B
- 26S proteasome non-ATPase regulatory subunit 7 homolog A
- 26S proteasome regulatory subunit 6A homolog B
Sequence:
MAAAMVSSAGGLLAMLNEPHPSLKLHALSYLIRLVDQFWPEISTSVPIIESLYEDEEFDQHQRQLAALLASKVFYYLGELNDSLSYALGAGSLFDVSEDSDYIHTLLSKAIDEYAILRSKAVESSEVVEIDPRLVAIVERMLDKCITDGKYQQAMGIAIECRRLDKLEEAIIKSENVQGTLSYCINVSHSFVNQREYRHEVLRLLVNVYQKLASPDYLSICQCLMFLDEPQGVASILEKLLRSENKDDALLAFQISFDLVQNEHQAFLMSVRDRLPAPKTRPVEAIQAVETSTAQNENTAGDVQMADETPSQTIVHETDPVDAVYAERLTKAKGILSGETSIQLTLQFLYSHNKSDLLILKTIKQSVEMRNSVCHSATIYANAIMHAGTTVDTFLRENLDWLSRATNWAKFSATAGLGVIHRGHLQQGRSLMAPYLPQGGAGGGGSPYSEGGALYALGLIHANHGEGIKQFLRDSLRSTSVEVIQHGACLGLGLAALGTADEDIYDDIKSVLYTDSAVAGEAAGISMGLLLVGTATDKASEMLAYAHETQHEKIIRGLALGIALTVYGREEGADTLIEQMTRDQDPIIRYGGMYALALAYSGTANNKAIRQLLHFAVSDVSDDVRRTAVLALGFVLYSDPEQTPRIVSLLSESYNPHVRYGAALAVGISCAGTGLSEAISLLEPLTSDVVDFVRQGALIAMAMVMVQISEASDSRVGAFRRQLEKIILDKHEDTMSKMGAILASGILDAGGRNVTIRLLSKTKHDKVTAVIGLTVFSQFWYWYPLIYFISLAFSPTAFIGLNYDLKVPKFEFMSHAKPSLFEYPKPTTVATANTAAKLPTAVLSTSAKAKAKAKKEAEQKAKAENSGNEAGKANAASDEKEAESMQVDSTATTVEKKVEPEATFEILVNPARVVPSQEKYIKLMEDSRYVPMKLAPSGFVLLRDLRPHEPEVLSLTDAPTSTASPAVGAEAAGQAQQAATTSAMAIDDEPQPPQAFEYASP
Protein: Short transient receptor potential channel 4b isoform X1 (Transient receptor potential cation channel, subfamily C, member 4b) (A0A0R4IM91)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Calmodulin
- Transient receptor potential cation channel, subfamily V, member 4.
- Transient receptor potential cation channel subfamily V member 1
- Transient receptor potential cation channel, subfamily A, member 1a.
- Stromal interaction molecule 1 isoform X1
- Transient receptor potential cation channel, subfamily M, member 7.
- Mucolipin 2.
- Transient receptor potential cation channel subfamily V member 6 isoform X1
- SEC14 domain and spectrin repeat-containing protein 1
- Transient receptor potential cation channel, subfamily C, member 1
Sequence:
MSQLYFRRTDNSSYRDRIPLRIVRAESELSTQEKSYLSAVEKGDYASVKLALEEAEIYFKININCIDPLGRTALLIAIENENLEIIELLLSFNVYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQVPPILLDKQFSDFTPDITPIILAAHTNNYEIIKMLVQKGVSVPQPHEVRCNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVENEFKAEYEELSHQCKHFAKDLLDQTRSSRELELILNFRDDMNLLQDEANNELARLKLAIKYRQKEFVAQPNCQQLLASRWYDEFPGWRRRHWAGKLITCVFIGLMFPLLSLCYLVAPKSRYGLFIRKPFIKFICHTASYLTFLFLLLLASQHIVSNNPDRQGPKPTTVEWMILPWVLGFIWTEIKQMWDGGFQDYIHDWWNLMDFVMNSLYLATISLKIVAYVKYSGCKPRDTWEMWHPTLVAEAVFAIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYENSEGMTCKGIRCERQNNAFSTLFETLQSLFWSIFGLISLYVTNVKADHKFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQHIADHADIEWKFARTKLWMSYFEEGGTLPPPFNIIPSPKSICYLITWIKVHVFKRRSKRKETFGTLGRRAAENVRLNHQYQEVLRNLVKRYVAAMIRDAKTEEGLTEENFKELKQDISSFRYEVIGMMKGNRKSTRANKSDTSASDVSHPEGSLQYSSALKQNSKLHLYDVTTALQQQNSEEAKASLGCLANGSAVVLTEPILKDKARSDFPKDFTDFGLFPKKQNPNKIYSLAEEATESDPDILDWGKEDKPLAGKVEQDVNESKCLMEEDERVLEEQEMEHIASSHEH
Protein: Lipopolysaccharide induced TNF factor (I3L3U8)
Organism: Homo sapiens (Human)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004125}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004414}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004630}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004630}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004630}.
Interaction partners:
Sequence:
MSVPGPYQAATGPSSAPSAPPSYEETVAVNSYYPTPPAPMPGPTTGLVTGPDGKGMNPPSYYTQPAPIPNNNPITVQTVYVQHPITFLDRPIQMCCPSCNKMIVSQLSYNAGALTWLSCGSLCLLGCIAGCCFIPFCVDALQDVDHYCPNCRA
Protein: O-phosphoserine--tRNA(Cys) ligase (O-phosphoserine--tRNA ligase) (EC 6.1.1.27) (Non-canonical O-phosphoseryl-tRNA(Cys) synthetase) (O-phosphoseryl-tRNA(Cys) synthetase) (SepRS) (O30126)
Organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Function: Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).
Interaction partners:
- O-phospho-L-seryl-tRNA:Cys-tRNA synthase 1
- Phenylalanine--tRNA ligase beta subunit
- O-phospho-L-seryl-tRNA:Cys-tRNA synthase 2
- Serine--tRNA ligase
- Cysteine--tRNA ligase
- Aspartate--tRNA
- Glutamate--tRNA ligase
- Threonine--tRNA ligase
- Leucine--tRNA ligase
- Tyrosine--tRNA ligase
Sequence:
MKFDPQKYRELAEKDFEAAWKAGKEILAERSPNELYPRVGFSFGKEHPLFATIQRLREAYLSIGFSEVVNPLIVEDVHVKKQFGREALAVLDRCFYLATLPKPNVGISAEKIRQIEAITKREVDSKPLQEIFHRYKKGEIDGDDLSYLIAEVLDVDDITAVKILDEVFPEFKELKPISSTLTLRSHMTTGWFITLSHIADKLPLPIKLFSIDRCFRREQGEDATRLYTYFSASCVLVDEELSVDDGKAVAEALLRQFGFENFRFRKDEKRSKYYIPDTQTEVFAFHPKLVGSSTKYSDGWIEIATFGIYSPTALAEYDIPYPVMNLGLGVERLAMILYGYDDVRKMVYPQIHGEIKLSDLDIAREIKVKEVPQTAVGLKIAQSIVETAEKHASEPSPCSFLAFEGEMMGRNVRVYVVEEEENTKLCGPAYANEVVVYKGDIYGIPKTKKWRSFFEEGVPTGIRYIDGFAYYAARKVEEAAMREQEEVKVKARIVENLSDINLYIHENVRRYILWKKGKIDVRGPLFVTVKAEIE
Protein: ADP-ribosylation factor 1 (EC 3.6.5.2) (P84079)
Organism: Rattus norvegicus (Rat)
Function: Small GTPase involved in protein trafficking between different compartments (By similarity). Modulates vesicle budding and uncoating within the Golgi complex (By similarity). In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane (By similarity). The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles (By similarity). The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasticity of excitatory synapses and spine shrinkage during long-term depression (LTD).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23889934}; Lipid-anchor {ECO:0000250|UniProtKB:P84080}; Cytoplasmic side {ECO:0000305}. Synapse, synaptosome {ECO:0000269|PubMed:23889934}. Postsynaptic density {ECO:0000269|PubMed:23889934}. Note=In the GDP-bound form, associates transiently with the membranes via its myristoylated N-terminus where guanine nucleotide-exchange factor (GEF)-mediated nucleotide exchange occurs (By similarity). Following nucleotide exchange, the GTP-bound form undergoes a conformational change, leading to the exposure of a myristoylated N-terminal amphipathic helix that provides stable membrane anchorage (By similarity). {ECO:0000250|UniProtKB:P84080}.
Interaction partners:
- Cytohesin-2
- Cytohesin-1
- Cytohesin-3
- Phospholipase D1
- Phospholipase D2
- Cytohesin 4
- Coatomer subunit beta
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- Nck-associated protein 1
- Cytoplasmic FMR1-interacting protein
Sequence:
MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
Protein: Cytochrome P450 2C39 (EC 1.14.14.1) (CYPIIC39) (P56656)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase that primarily catalyzes the epoxidation of 11,12 and 14,15 double bonds of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) forming 11,12- and 14,15-epoxyeicosatrienoic acids (11,12- and 14,15-EET) regioisomers. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2E1
- Epoxide hydrolase 1
- Cytochrome P450 2U1
- Polyunsaturated fatty acid lipoxygenase ALOX8
- Arachidonate 12-lipoxygenase, 12R-type
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Polyunsaturated fatty acid 5-lipoxygenase
- Cytochrome P450 7A1
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
Sequence:
MDLVTFLVLTLSSLILLSLWRQSCGRGSLPPGPTPFPIIGNFLQIDIKNVSQSLTNFSKAYGPVFTLYLGSRPTVVLHGYEAVKEALIDHGEEFSDRGSIPMVEKINNGLGIVFSNGNRWKEIRRFTLTTLRNLGMGKRNIEDRVQEEAQCLVEELRKTKGSPCDPTFILSCAPCNVICSIIFQDRFDYKDKDFLMLMEKLNENVKILSSPWLQVCNNFPLLIDYCPGSHHKVLKNVKYIRSYLLEKIKEHQESLDVTNPRDFIDYYLIKQKQANHIQQAEFSLENLACTINNLFAAGTETTSTTLRYALLLLMKYPDVTAKVQEEIDHVIGRHRSPCMQDRNHMPYTDAMIHEVQRFINLVPNNIPRAVTCDIKFRNYLIPKGTTVVTSLTSVLHDSKEFPNPELFDPGHFLDANGNFKKSDHFMPFSAGKRVCAGEGLARMELFLFLTTILQNFKLKSLVHPKDIDMIPFVNGLIALPPHYQVCIIPR
Protein: Probable inactive shikimate kinase like 2, chloroplastic (AtSKL2) (O82290)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Probable inactive shikimate kinase like 1, chloroplastic
- RBR-type E3 ubiquitin transferase
- Pentatricopeptide repeat-containing protein At1g05600
- Protein CHLOROPLAST J-LIKE DOMAIN 1
- acid phosphatase
- Probable protein phosphatase 2C 76
- Myosin-binding protein 1
- UBP1-associated proteins 1B
- Gluconokinase
- N-alpha-acetyltransferase MAK3
Sequence:
MAAFASGLAIIFNSPSLNPVTTQATFLSSNRIRSSPRVFSGFHSLRRRGFRRFSQNVIPDRFNSFSCNCLSAVSTSTIDYEFTDGGKEVELRLRLKTGEILSPKDISVDADGTSLAVKEKRNGLLITLLETNHLFEKIMPSETIWYIDEDQLVVNMKKVDGELKWPDIVESWESLTAGMMQLLKGASIYIVGDSTEINQKVSRELAVGLGYSPLDSKELLESFSKQTIDSWILAEGPDSVAEAESSVLESLSSHVRTVVSTLGGKHGAAGRADQWRHLYSGFTVWVSQTEATDEESAKEEARRSKQEREIGYSNADVVVKLQGWDPTHAKSVAQASLSALKQLIISDKGLPGKKSLYIRLGCRGDWPNIKPPGWDPSSDTGPHPQFT
Protein: Mitochondrial inner membrane protease ATP23 (EC 3.4.24.-) (P53722)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes the N-terminal 10 residues of mitochondrial ATPase CF(0) subunit 6 (ATP6) at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of ATP6 with the subunit 9 ring.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:17135288, ECO:0000269|PubMed:17135290}; Peripheral membrane protein {ECO:0000269|PubMed:17135288, ECO:0000269|PubMed:17135290}; Intermembrane side {ECO:0000269|PubMed:17135288, ECO:0000269|PubMed:17135290}. Note=Associates loosely with the inner membrane.
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40
- Mitochondrial ATPase complex subunit ATP10
- ATP synthase subunit a
- Mitochondrial import inner membrane translocase subunit TIM10
- Mitochondrial metalloendopeptidase OMA1
- Mitochondrial FAD-linked sulfhydryl oxidase ERV1
- Mitochondrial inner membrane protein OXA1
- Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1
- Inner membrane assembly complex subunit 22
- Inner membrane assembly complex subunit 17
Sequence:
MNSSGDNAGFEWWRRTMQYKTGIGLTPEEKTRYEDDSKARELKKECLKCYEYRDWMLKYSPTVRFMVQAITKLNKGSDSKFDDSKIICDYCPDWKGGGFHPELGILLCQNRLRDKWHLEDTLSHELIHYFDDLKWQIDWLNLKHHACSEIRASSLSGECRFWEEFKRRGFRTGFHVARGHQDCVRRRAIISVSGNPNCQSKEHAAKIVDEVWDSCFADTRPFDEIYR
Protein: mRNA decay activator protein ZFP36L2-B (CCCH zinc finger protein 3-B) (XC3H-3b) (Zinc finger protein 36, C3H1 type-like 2-B) (Q805B4)
Organism: Xenopus laevis (African clawed frog)
Function: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis. Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (By similarity). Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (By similarity). Binds to 3'-UTR ARE of numerous mRNAs. Induces also the degradation of ARE-containing mRNAs even in absence of poly(A) tail (By similarity). Required for tubulogenesis during pronephros development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P23949}. Cytoplasm {ECO:0000250|UniProtKB:P23949}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:P23949}.
Interaction partners:
Sequence:
MSTTLLSAFYDIDLLYKNEKALNNLALSTMLDKKAVGSPVSSTNSNLFPGFLRRHSATNLQALSGSTNLAKFCPNNNNNPLKDPAVSSTALLNRENKFRDRSFSENGERSQHLLHLQQQQQQQKAGAQVNSTRYKTELCRPFEENGACKYGEKCQFAHGFHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRQAPGAGERPKLHHSLSFSGFPNHSLDSPLLESPTSRTPPPQSSGSLYCQELLQLNNNNPCANNAFTFSGQELGLIAPLAIHTQNQSYCRQPCSSPPLSFQPLRRVSESPVFDAPPSPPDSLSDRDSYLSGSLSSGSLSGSDSPTLDSNRRLPIFSRLSISDD