wanglab/gogpt-training-data huggingface dataset:
Protein: tRNA (cytosine(38)-C(5))-methyltransferase 2 (AtDNMT2) (EC 2.1.1.204) (DNA (cytosine-5)-methyltransferase-like protein 2) (Dnmt2) (F4JWT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp) (By similarity). Represses gene expression at transcription level, probably by regulating histone deacetylation and epigenetic regulatory network.
Subcellular location: Nucleus {ECO:0000269|PubMed:20331964}.
Interaction partners:
- 25S rRNA
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Putative tRNA
- DNA
- tRNA
- 26S rRNA
- DNA
- tRNA
- Transcriptional activator DEMETER
- rRNA
Sequence:
MAEQELQRINEKKPWQVLEFYSGIGGMRYSLMASGIVSEVVEAFEINDSANDVYQHNFKHRPYQGNIQSLTAADLDKYNADAWLLSPPCQPYTRQGLQKHSGDARAFSFLRILELIPHTTKPPQMLFVENVVGFETSDTHMEMIGTLTKLDYVTQEFILSPLQFGVPYSRPRYFCLAKRKPLPFKSQHSNNKLLWSPDPLYGRDDQVEFGKCQAEEGLDKLLEFCKPVEKFLELAAHVDGEPSSVDDSENGSKDCCGQEGDSVPDSVHQYLVPVSLIERWGNAMDIVYPDSKRCCCFTKSYYRYVKGTGSLLATVQPKIKGKESCLKEQRLRYFTPREVANFHSFPEDFEFPKHISLRQRYAMLGNSLSVAVVAPLLRYLFDS
Protein: Membrane metallo-endopeptidase-like 1 (EC 3.4.24.11) (Membrane metallo-endopeptidase-like 2) (NEP2(m)) (Neprilysin II) (NEPII) (Neprilysin-2) (NEP2) (NL2) [Cleaved into: Membrane metallo-endopeptidase-like 1, soluble form (Neprilysin-2 secreted) (NEP2(s))] (Q495T6)
Organism: Homo sapiens (Human)
Function: Metalloprotease involved in sperm function, possibly by modulating the processes of fertilization and early embryonic development. Degrades a broad variety of small peptides with a preference for peptides shorter than 3 kDa containing neutral bulky aliphatic or aromatic amino acid residues. Shares the same substrate specificity with MME and cleaves peptides at the same amide bond (By similarity).
Subcellular location: Membrane; Single-pass type II membrane protein. Secreted. Note=A secreted form produced by proteolytic cleavage also exists. {ECO:0000250}.
Interaction partners:
- Insulin-degrading enzyme
- Amyloid-beta precursor protein
- Angiotensin-converting enzyme
- Beta-secretase 1
- Mineralocorticoid receptor
- Renin
- Presenilin-1
- Nicastrin
- Angiotensinogen
- Presenilin-2
Sequence:
MGKSEGPVGMVESAGRAGQKRPGFLEGGLLLLLLLVTAALVALGVLYADRRGKQLPRLASRLCFLQEERTFVKRKPRGIPEAQEVSEVCTTPGCVIAAARILQNMDPTTEPCDDFYQFACGGWLRRHVIPETNSRYSIFDVLRDELEVILKAVLENSTAKDRPAVEKARTLYRSCMNQSVIEKRGSQPLLDILEVVGGWPVAMDRWNETVGLEWELERQLALMNSQFNRRVLIDLFIWNDDQNSSRHIIYIDQPTLGMPSREYYFNGGSNRKVREAYLQFMVSVATLLREDANLPRDSCLVQEDMVQVLELETQLAKATVPQEERHDVIALYHRMGLEELQSQFGLKGFNWTLFIQTVLSSVKIKLLPDEEVVVYGIPYLQNLENIIDTYSARTIQNYLVWRLVLDRIGSLSQRFKDTRVNYRKALFGTMVEEVRWRECVGYVNSNMENAVGSLYVREAFPGDSKSMVRELIDKVRTVFVETLDELGWMDEESKKKAQEKAMSIREQIGHPDYILEEMNRRLDEEYSNLNFSEDLYFENSLQNLKVGAQRSLRKLREKVDPNLWIIGAAVVNAFYSPNRNQIVFPAGILQPPFFSKEQPQALNFGGIGMVIGHEITHGFDDNGRNFDKNGNMMDWWSNFSTQHFREQSECMIYQYGNYSWDLADEQNVNGFNTLGENIADNGGVRQAYKAYLKWMAEGGKDQQLPGLDLTHEQLFFINYAQVWCGSYRPEFAIQSIKTDVHSPLKYRVLGSLQNLAAFADTFHCARGTPMHPKERCRVW
Protein: Biotin synthase (EC 2.8.1.6) (Biotin synthetase) (P12996)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Interaction partners:
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- ATP-dependent dethiobiotin synthetase BioD 1
- 8-amino-7-oxononanoate synthase
- Malonyl-[acyl-carrier protein] O-methyltransferase
- ATP-dependent dethiobiotin synthetase BioD 2
- Bifunctional ligase/repressor BirA
- Biotin sulfoxide reductase
- tRNA-2-methylthio-N
- Lipoyl synthase
- L-lysine 2,3-aminomutase
Sequence:
MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGVKAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNPQQTAVLAGDNEQQQRLEQALMTPDTDEYYNAAAL
Protein: Protein inturned (Inturned planar cell polarity effector homolog) (Xint) (Q2I0E5)
Organism: Xenopus laevis (African clawed frog)
Function: Plays a role in the definition of cell polarity via the planar cell polarity (PCP) cascade. Required for ciliogenesis by controlling the organization of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules. Proposed to function as core component of a functional module called CPLANE (ciliogenesis and planar polarity effectors) involved in recruitment of peripheral IFT-A proteins to basal bodies. Controls the localization of both rhoa and disheveled in multi-ciliated cells. Has an indirect effect on hedgehog signaling.
Subcellular location: Cell surface {ECO:0000269|PubMed:16493421}. Cell membrane {ECO:0000269|PubMed:16493421}. Cytoplasm {ECO:0000250|UniProtKB:Q059U7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27158779}. Note=Enriched at the apical surface in ciliated cells. Localizes to the cell membrane in non-ciliated cells. {ECO:0000269|PubMed:16493421}.
Interaction partners:
Sequence:
MEHSRGDSVEAGEEEEGRGGWDSRSAGTFSSSCTDCSSYCSSDLEPEWLDRVQKNGELFYLELSEGEEEILLPLSPLEPVGVNHVRFSDNEAEILPEDRKNVRKNSEPRFRKLAKMLKKKNNKKGSAELNRQACPTSILKQNSRQKPGIIVHYQYRDTCLYVNPDHLPEDEHKKTSNLLQALIGIVHQSSRNSKRSERQGRQESNQRLSNQEKLVVHGFIPGSPAIRCGQVLIGDTLVAVNDVEVHVENIERVLSCIPGPMQLKLTFETPVLYSGMGLKNQNNQAQTSINDLASLVWGDEHTNSQQDLQHMPHIVMYLTLRLDSETSKEEQEILYQYPVSDASHKLKSIRGLFLTLGDMLQNVTGAPIVSSSLILNGELVHVSYWKENDKLFLISVPAQRFPLLQLKNVTADLVRTLKFMYSTLDRAFCQAENISRLDHFFSLFFQRVLRVFLLSGITGYGPQFYDACSSLLVENLPGVRWLSLPEDIKIQIDTVLSDLEALDFAELSEDYYEMRRLYMIIGTCIFYKGYLLSNHLPKEDLVDVVLYCRQYCLLALASERIGQLIIWREVYPRYHLKHCGSPATEECSEPGGRYFLLIVGLKHFMLCTLLEAGGCTSKATGNPGPDYIYVDQVKATLLQLEMLDLNLEERLGSAPNPCLSCADWFLPSARDKLGNFTSSIVLNKLQTPKRTTSPVSKRRLFAEAASSLRTRRPSPTRSSGGSDSGTDGAGESVGVITHSSPDMARKFGRRESLGSGGSDGSGGSGTLLKINKKKYSLPNPFSSASLRKNLSERETDDIYNTIKLTSGPENTLFHYLYFETLQGVFISPTHKEVEQLGGSIHPQLIKNFHRCCLSIRSVFQQALNKKNSKHSDSKACVDVAGFDPIKEHGVLFECSPENWNDQKKSPPTMSYWVVGRLFMHPQPQELYVCFHDSVTEISVELAFKLSFGIPL
Protein: At1g15730/F7H2_7 (Cobalamin biosynthesis CobW-like protein) (F7H2.7 protein) (Putative PRLI-interacting factor L) (Q9LMR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- General transcription and DNA repair factor IIH subunit TFB5
- Chaperone DnaJ-domain superfamily protein
- General transcription and DNA repair factor IIH subunit TFB1-3
- General transcription and DNA repair factor IIH subunit TFB5
- Probable protein phosphatase 2C 8
- Large ribosomal subunit protein bL28c
- General transcription and DNA repair factor IIH subunit TFB1-1
Sequence:
MATLLKLDIATTFLAFIVPRANTSLNHRFASARLSTATVSLRTKSSSFYSAALYSDSRRRFHSAVASDSSLAVVDDEDIFDVASEILPDNRIPATIITGFLGSGKTTLLNHILTGDHGKRIAVIENEFGEVDIDGSLVAAQTAGAEDIMMLNNGCLCCTVRGDLVRMISEMVQTKKGRFDHIVIETTGLANPAPIIQTFYAEDEIFNDVKLDGVVTLVDAKHARLHLDEVKPEGYVNEAVEQIAYADRIIVNKTDLVGEPELASVMQRIKTINSMAHMKRTKYGKVDLDYVLGIGGFDLERIESSVNEEEKEDREGHDDHHHGHDCHDHHNEHEHEHEHEHHHSHDHTHDPGVGSVSIVCEGDLDLEKANMWLGALLYQRSEDIYRMKGILSVQDMDERFVFQGVHEIFEGSPDRLWRKDETRTNKIVFIGKNLNREELEMGFRACLI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q6IPE9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSRTVLAPGNDRNSDTAENLLLDAEANIKIADFGFSNEFTLGSKLDTFCGSPPYAAPELFQGKKYDGPEVDIWSLGVILYTLVSGSLPFDGHNLKR
Protein: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (A0A2R8YCS7)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
Sequence:
MQRADSEQPSKRPRCDDSPRTPSNTPSAEADWSPGLELHPDYKTWGPEQVCSFLRRGGFEEPVLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRLVQIHVDTMKVINDPIHGHIELHPLLVRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVHALGEKQPELQISERDVLCVQIAGLCHDLGHGPFSHMFDGRFIPLARPEVKWTHEQGSVMMFEHLINSNGIKPVMEQYGLIPEEDICFIKEQIVGPLESPVEDSLWPYKGRPENKSFLYEIVSNKRNGIDVDKWDYFARDCHHLGIQNNFDYKRFIKFARVCEVDNELRICARDKEVGNLYDMFHTRNSLHRRAYQHKVGNIIDTMITDAFLKADDYIEITGAGGKKYRISTAIDDMEAYTKLTDNIFLEILYSTDPKLKDAREILKQIEYRNLFKYVGETQPTGQIKIKREDYESLPKEVASAKPKVLLDVKLKAEDFIVDVINMDYGMQEKNPIDHVSFYCKTAPNRAIRITKNQVSQLLPEKFAEQLIRVYCKKVDRKSLYAARQYFVQWCADRNFTKPQSPTRASH
Protein: Uncharacterized protein (Q38B84)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGSMVIGGDRKSISSVEPLTALQSSNATPNKVNQRPTPSQREQKQETSKSPLVMRANAAADVHQWPDFSGFRERNDIFNTSSLPRSPNQKQMDTHAENNSKAELTSPASEGSGRVMERSMTAAVSARTFSDDRVLDDESDIDIVIHMPTHYQPGPPAQIQEKEVVSSSSPSCNTGVALSTNEVPCRDIINSAENEKVSFTGACQQKEIAHLNEFVAVVKEAVVKAVVEIPASPKPQRRPRLTRALLNRTREVTFKPYTIEEWLGGVQLLGDQPAAVKICSVENVILTATIATMKVEDQFTGSNGCTDARLEESTN
Protein: ATP-dependent DNA helicase (EC 5.6.2.4) (X1WCM8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU364117}.
Interaction partners:
- Helicase ATP-binding domain-containing protein.
- FA complementation group M.
- F-box DNA helicase 1.
- DNA topoisomerase
- RecQ-mediated genome instability protein 1
- DNA helicase
- DNA replication helicase/nuclease 2.
- ATR serine/threonine kinase
- DNA repair protein RAD52 homolog
- Structure-specific endonuclease subunit MUS81
Sequence:
MSVVHRALKTHFGFEKFRSRQQEEAVNALLQGDRDVFVCMPTGAGKSLCYQLPALMASGVTLVISPLIALIQDQVEHLKALNVPARSINSKLPLAERRQILADLESETPRLKLLYITPEMVASPSFQPVLSSLSSRGLLGYLAVDEAHCVSQWGHDFRPDYLKLGDLRSRLQGIRCIALTATAPKRVKEDIERSLRLRSPLVFSTPVFRKNLKYDVIFRDLLPEPYVHLLAFAKEALGGNTAEKGCGIVYCRTRESCEEVAHKLTKLGIAAKPYHAGLKSGDRSENQADWMADKVPIIVATISFGMGVDKANVRFVVHWNLAKSLASYYQESGRAGRDGLPSSCRIYYSPKDRDQLNFLIRKEISRKQEKRGSEKEQDKAPILDFEAMVAFCEQEGCRHATISTFFGNEKPNCAGACDFCRDPKLVRAQLARAAALSTRTNPTHSAEPRGPFGFDPELYAGGRKGYGFERHDEEYGSEEDDSEKRKKQFGDLFKKQMSLRKGSDAPKETFVPPDADCVLKDASSQRIPRLTVKSREHCLSLLQECLSSHSGDAEFLHRSEALDQAVDIEHEIFKSSKSANIYKAAVLKRVSEMKKSTSVSVTEEKPCESAEEKPTCSSSAQHLDGFTSASQIYSLKRKRVGAGFRGSSSLFQPAGDLLKSSDQTPGDSTCEEESGKTQKDNNNTSSIKAKSGSSSSLNSPSKKLSRKQQKLAEAARDTRLISLYFGKKQAQRESSPEPEETEDACEDRSASANGVHTLSSSSVDAERAAQESLCEVTAHAEDYGENQQSDGQRKSPKQAHEDRSEVRAPSPPVKRRRVLKDTKRVTFDPVVQETQVEALNGDGAGISRKPVTLKEAADIVVRCLDPFYKQGKFATKDLFKSFARFLSHLLTEGKTPNRGQVKLEAKRLIKRFFSRTVRCESESDWMLLKTQDR
Protein: Protein MAK10 homolog (O17003)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- N-terminal methionine N
- N-alpha-acetyltransferase daf-31
- Sm domain-containing protein
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
- Probable small nuclear ribonucleoprotein-associated protein B
- Histidine ammonia-lyase
- Zinc transporter ttm-1
- PID domain-containing protein
- Probable small nuclear ribonucleoprotein E
- N-terminal acetyltransferase B complex subunit NAA25 homolog
Sequence:
MPGAMESPNESEDVSKTFFKLCDGLRLGELVTTEHFRLSDVMSAIELGEPKMDVGVGSKHIKTLKEAISGGLYADDYPFQLAIMDSTLAMVVAWLEGSALGSTVWTNVLLSNVTFVKHPVFHPFASGVNLFIRNAHALINSVGNLEELPEDFNPQMLFSHQRWAPRRVVVQLMREQVTLLGTTGRKWRESAFSKQAYDICCAVASRLEMFIMLLEIIGLLVAPEIEDPNFDHKVHLGDFYVHEKEYEGAEENSDEKSEESTSDPTPSSEAKSETTEKKEQKSNDEATDETDQNDDENVGDDEDEDDMKQFKPNFGFASILAERLCKVTKAYAETVKLGRRAPDNIDGDGDYLWLGAYEPKTCIRMIPACFPRKIKVPSRQEAADWWVKCAERIYHLCIVTPKTSKDLNYLFYFARTFGQNACVFTRSLLQICMFPVDNHLCGDENRSIADAVEYSLSNCFCPQILDRVSPVYKDQTAQSLYVLFLNHMSKLAITVYGSFGCNLSRQRDRLEMAIEDLGQIHSYAGRLEERTDEVLLSGKMVTAKEQNYSYHSVATFVFHNLLAIINHYFELGFRMDLYVPYEFPYIYWFIGSVQAHWMRTTLERSQEIQLNVYQANPLRETKNKKLWEERCKLGEELKRRVAAHQFSVLNQIAISMISDGVVRLTVVLIRKGIIKMPKGGDDAEKLRFERRFEPFDSLGPPVRVDYERFKSDSGIDQMYEDKIETLIDQAQKSFNEAREHLEKIDNSVEQNREMMQLIHVAKSNIIACRVLKLDLTDRNVVWSFSEEIPMFPCLKISKK
Protein: PTS system fructose-specific EIIABC component (EIIABC-Fru) [Includes: PTS system fructose-specific EIIA component (EII-Fru) (Fructose-specific phosphotransferase enzyme IIA component); PTS system fructose-specific EIIB component (EC 2.7.1.202) (EIII-Fru) (Fructose-specific phosphotransferase enzyme IIB component); PTS system fructose-specific EIIC component (Fructose permease IIC component)] (P71012)
Organism: Bacillus subtilis (strain 168)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in fructose transport.
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00427}.
Interaction partners:
- 1-phosphofructokinase
- Mannitol-specific phosphotransferase enzyme IIA component
- Uncharacterized HTH-type transcriptional regulator FruR
- PTS system fructose-specific EIIA component
- Phosphocarrier protein HPr
- PTS system glucose-specific EIICBA component
- Fructose permease IIC component
- PTS system mannose-specific EIIBCA component
- Fructose permease IID component
- Uncharacterized sugar kinase YdjE
Sequence:
MKITELLTKHTIKLNIESKEKENVIDEMVTVLDKAGKLNDRQAYKEAILNRESQSSTGIGEGIAIPHAKTASVINPAIAFGRSKDGVDYESLDGQPAHLVFMIAATEGANNTHLEALSRLSTLLMREEIRKQLLEAESEDAIIDIINQHDKDDDEEEEEEEAAPAPAGKGKILAVTACPTGIAHTFMAADALKEKAKELGVEIKVETNGSSGIKHKLTAQEIEDAPAIIVAADKQVEMERFKGKRVLQVPVTAGIRRPQELIEKAMNQDAPIYQGSGGGSAASNDDEEAKGKSGSGIGNTFYKHLMSGVSNMLPFVVGGGILVAISFFWGIHSADPNDPSYNTFAAALNFIGGDNALKLIVAVLAGFIAMSIADRPGFAPGMVGGFMATQANAGFLGGLIAGFLAGYVVILLKKVFTFIPQSLDGLKPVLIYPLFGIFITGVLMQFVVNTPVAAFMNFLTNWLESLGTGNLVLMGIILGGMMAIDMGGPLNKAAFTFGIAMIDAGNYAPHAAIMAGGMVPPLGIALATTIFRNKFTQRDREAGITCYFMGAAFVTEGAIPFAAADPLRVIPAAVVGAAVAGGLTEFFRVTLPAPHGGVFVAFITNHPMLYLLSIVIGAVVMAIILGIVKKPVTEK
Protein: Secreted effector protein SseJ (EC 3.-.-.-) (Salmonella-translocated effector J) (STE J) (Q9FD10)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is required for endosomal tubulation and negatively regulates the formation of Salmonella-induced filaments (Sifs) in epithelial cells. Has both deacylase and esterification activities in vitro, but esterification is probably the dominant activity in host cells. Significantly contributes to cholesterol esterification, which reduces cellular cholesterol in cells and abrogates the ability of SifA to associate with cholesterol and LAMP-1 vesicles.
Subcellular location: Secreted. Host cytoplasm. Note=Secreted via type III secretion system 2 (SPI-2 T3SS), and delivered into the host cytoplasm. Localizes to the Salmonella-containing vacuole (SCV) at early time points following invasion and subsequently traffics away from the SCV along Salmonella-induced filaments (Sifs) in epithelial cells.
Interaction partners:
- Secreted effector protein SifB
- Deubiquitinase SseL
- Secreted effector protein SifA
- Secreted effector kinase SteC
- Secreted effector protein PipB
- Secreted effector protein PipB2
- Secreted effector protein sopD2
- Secretion system effector
- Secretion system effector
- Secreted effector protein SptP
Sequence:
MPLSVGQGYFTSSISSEKFNAIKESARLPELSLWEKIKAYFFTTHHAEALECIFNLYHHQELNLTPVQVRGAYIKLRALASQGCKEQFIIESQEHADKLIIKDDNGENILSIEVECHPEAFGLAKEINKSHPKPKNISLGDITRLVFFGDSLSDSLGRMFEKTHHILPSYGQYFGGRFTNGFTWTEFLSSPHFLGKEMLNFAEGGSTSASYSCFNCIGDFVSNTDRQVASYTPSHQDLAIFLLGANDYMTLHKDNVIMVVEQQIDDIEKIISGGVNNVLVMGIPDLSLTPYGKHSDEKRKLKDESIAHNALLKTNVEELKEKYPQHKICYYETADAFKVIMEAASNIGYDTENPYTHHGYVHVPGAKDPQLDICPQYVFNDLVHPTQEVHHCFAIMLESFIAHHYSTE
Protein: Very long chain fatty acid elongase 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Elongation of very long chain fatty acids protein 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7) (A1L3X0)
Organism: Homo sapiens (Human)
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:20937905}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03207}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase
- Very long chain fatty acid elongase 3
- Very long chain fatty acid elongase 1
Sequence:
MAFSDLTSRTVHLYDNWIKDADPRVEDWLLMSSPLPQTILLGFYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGIGYSFRCDIVDYSRSPTALRMARTCWLYYFSKFIELLDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYSYYGLSALGPAYQKYLWWKKYLTSLQLVQFVIVAIHISQFFFMEDCKYQFPVFACIIMSYSFMFLLLFLHFWYRAYTKGQRLPKTVKNGTCKNKDN
Protein: RH36157p (Q7JQK3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNVHKRPRLNMEFGSSTSNTNTSTSPSSVNISNANPTAGPGLMTITNHHTADLSEALVHSSFANGQQSLILTSDTGNPLMNSQGAQIFLTICGDENSDDSQEYYTIKQEPGCDLDIHSLLPSNLQLPNNLQLPTGCEIYLVKETGSLMGEPPTKAAIKLELDTLSEKPLLPSVTTSSSTQSAVITAQTVNPPIPGNINTTTSTTSTTTTTSVLYGSHGNGHGHGHAHAQARSQPESAGQTPSSKLEAYKKRDDKRRATHNEVERRRRDKINSWIFKLKEMLPSLSSSSSFSEASTSPSTSGSTSTNGSSHSKGNASSSSGRAPPNDSKSQILIKACEYIKSMQGEIDT
Protein: Cytochrome P450 2C1 (EC 1.14.14.1) (CYPIIC1) (Cytochrome P-450 IIC1) (Cytochrome P450 PBc1) (P00180)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
Sequence:
MDPVVVLGLCLSCLLLLSLWKQSYGGGKLPPGPTPFPILGNILQIGIQDISKSFTKLSEVYGPVFTVYLGMKPTVVIHGYDAVKEALVDLGEEFSGRIVFPLTAKINKGYGIVFSNGKRWKETRRFSLMTLRDFGMGKRSIEDRVQEEARCLVEELRKTNGSPCNPTFILGAAPCNVICSVIFQNRFDYTDQDFLSLMGKLNENFKILNSPWVQMCNNFPILIDYLPGSHNKILRNNIYIRNYVLEKIKEHQETLDINNPRDFIDCFLIKMEQEKDNQQSEFTIENLMTTLSDVFGAGTETTSTTLRYGLLLLMKHPEVIAKVQEEIERVIGRHRSPCMQDRSRMPYTDATVHEIQRYINLIPNNVPRATTCNVKFRSYLIPKGTAVITSLTSMLYNDKEFPNPDRFDPGHFLDASGKFRKSDYFMPFSTGKRVCVGEVLARMELFLFLTAILQNFTPKPLVDPKDIDTTPLVSGLGRVPPLYQLSFIPA
Protein: Ig gamma-3 chain C region (P03987)
Organism: Mus musculus (Mouse)
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
Interaction partners:
Sequence:
TTTAPSVYPLVPGCSDTSGSSVTLGCLVKGYFPEPVTVKWNYGALSSGVRTVSSVLQSGFYSLSSLVTVPSSTWPSQTVICNVAHPASKTELIKRIEPRIPKPSTPPGSSCPPGNILGGPSVFIFPPKPKDALMISLTPKVTCVVVDVSEDDPDVHVSWFVDNKEVHTAWTQPREAQYNSTFRVVSALPIQHQDWMRGKEFKCKVNNKALPAPIERTISKPKGRAQTPQVYTIPPPREQMSKKKVSLTCLVTNFFSEAISVEWERNGELEQDYKNTPPILDSDGTYFLYSKLTVDTDSWLQGEIFTCSVVHEALHNHHTQKNLSRSPELELNETCAEAQDGELDGLWTTITIFISLFLLSVCYSASVTLFKVKWIFSSVVQVKQTAIPDYRNMIGQGA
Protein: Glycosylphosphatidylinositol anchor biosynthesis protein 11 (PIGF homolog) (Q06636)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts in the GPI biosynthetic pathway between GlcNAc-PI synthesis and GPI transfer to protein. Required for the formation of complete GPI precursors CP1 and CP2.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- GPI ethanolamine phosphate transferase 3
- GPI mannosyltransferase 3
- GPI-anchor transamidase
- GPI ethanolamine phosphate transferase 2
- GPI transamidase component GPI16
- GPI transamidase component GPI17
- GPI transamidase component GAA1
- GPI transamidase component GAB1
- GPI mannosyltransferase 2
- GPI mannosyltransferase 4
Sequence:
MPAKKRTRKTVKKTVSFSDDTTLTTHQNREKKNVDHDRPPVYVRKTPLMTFPYHLVALLYYYVFVSSNFNTVKLLSFLIPTQVAYLVLQFNKCTVYGNKIIKINYSLTIICLGVTFLLSFPTMLLTILFGAPLMDLLWETWLLSLHFAFLAYPAVYSVFNCDFKVGLWKKYFIFIVVGGWISCVVIPLDWDRDWQNWPIPIVVGGYLGALVGYTIGAYI
Protein: Calcium/calmodulin-dependent protein kinase type 1D (EC 2.7.11.17) (CaM kinase I delta) (CaM-KI delta) (CaMKI delta) (CaM kinase ID) (CaMKI-like protein kinase) (CKLiK) (mCKLiK) (Q8BW96)
Organism: Mus musculus (Mouse)
Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons. In neutrophil cells, required for cytokine-induced proliferative responses and activation of the respiratory burst. Activates the transcription factor CREB1 in hippocampal neuron nuclei. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta (By similarity). Isoform 1 but not isoform 2 activates CREB1.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. Nuclear upon activation. {ECO:0000250}.
Interaction partners:
- Neuronal migration protein doublecortin
- Translation initiation factor eIF2 assembly protein
- Juxtaposed with another zinc finger protein 1
Sequence:
MARENGESSSSWKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALSKNIHESVSAQIRKNFAKSKWRQAFNATAVVRHMRRLQLGSSLDSSNASVSSNLSLASQKDCLAPSTLCSFLSSSSGVAGVGAERRPRPTTVTTGHTGSK
Protein: Scavenger receptor (Q58SM3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
TCDRDGRLRGEKPFCASRGCARPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVQLMTGSECGTNGFTTTTEPTAPTGSNEQPLVYDMMSCSGRCGTSMSASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELLTTTEDDISSVPPTVTSTSTSTTRKSTTTTTTTTTTTTTTSTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPKSTTSTTSTTPTTTTTINVFTTKKTTTMIPTSSTEKTTDTNTTMKTRKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLGIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNSMDDQPLCDSDNDDVEYFEEMGVDIRHRTDL