wanglab/gogpt-training-data huggingface dataset:
Protein: Olfactory receptor (Q9QZ18)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MEPSNRTAVSEFVLKGFSGYPALERLLFPLCSVMYLVTLLGNTAIVAVSMLDARLHTPMYFFLGNLSILDICYTSTFVPLMLVHLLSSRKTISFTGCAVQMCLSLSTGSTECLLLAVMAYDRYLAICQPLRYPVLMSHRLCLMLAGASWVLCLFKSVAETVIAMRLPFCGHHVIRHFTCEILAVLKLTCGDTSVSDAFLLVGAILLLPIPLTLICLSYMLILATILRVPSATGRSKAFSTCSAHLAVVLLFYSTIIFMYMKPKSKEARISDQVFTVLYAVVTPMLNPIIYSLRNKEVKEAARKAWGSRWACR
Protein: Probable two-component-system connector protein AriR (P75993)
Organism: Escherichia coli (strain K12)
Function: Probably a connector protein for RcsB/C regulation of biofilm and acid-resistance, providing additional signal input into the two-component signaling pathway. May serve to stimulate biofilm maturation, via the Rcs phosphorelay. Regulates expression of genes involved in acid-resistance and biofilm formation, including the RcsB/C two-component system. May be a non-specific DNA-binding protein that binds genes and/or intergenic regions via a geometric recognition. Also confers resistance to H(2)O(2). Overexpression at 28 and 16 degrees Celsius increases the production of colanic acid, an exopolysaccharide and matrix component, and reduces adhesive curli fimbriae expression. Both of these effects require RcsB; AriR probably acts upstream of the RcsB/C system to stimulate the activity and not transcription of RcsB/C. 5-fluorouracil reduction in biofilm formation requires this protein.
Interaction partners:
- Probable two-component-system connector protein YmgA
- Uncharacterized protein YmgC
- Probable two-component-system connector protein YcgZ
- HTH-type transcriptional repressor BluR
- Blue light- and temperature-regulated antirepressor BluF
Sequence:
MLEDTTIHNAITDKALASYFRSSGNLLEEESAVLGQAVTNLMLSGDNVNNKNIILSLIHSLETTSDILKADVIRKTLEIVLRYTADDM
Protein: Uncharacterized protein Rv2627c (P9WL67)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable diacyglycerol O-acyltransferase tgs1
- Probable membrane protein Rv1733c
- Universal stress protein Rv2623
- Putative NAD
- Probable nitrate/nitrite transporter NarK2
- Uncharacterized protein Rv2030c
- Hypoxic response protein 1
- Universal stress protein Rv3134c
- Universal stress protein Rv1996
- Putative zinc metalloprotease Rip3
Sequence:
MASSASDGTHERSAFRLSPPVLSGAMGPFMHTGLYVAQSWRDYLGQQPDKLPIARPTIALAAQAFRDEIVLLGLKARRPVSNHRVFERISQEVAAGLEFYGNRRWLEKPSGFFAQPPPLTEVAVRKVKDRRRSFYRIFFDSGFTPHPGEPGSQRWLSYTANNREYALLLRHPEPRPWLVCVHGTEMGRAPLDLAVFRAWKLHDELGLNIVMPVLPMHGPRGQGLPKGAVFPGEDVLDDVHGTAQAVWDIRRLLSWIRSQEEESLIGLNGLSLGGYIASLVASLEEGLACAILGVPVADLIELLGRHCGLRHKDPRRHTVKMAEPIGRMISPLSLTPLVPMPGRFIYAGIADRLVHPREQVTRLWEHWGKPEIVWYPGGHTGFFQSRPVRRFVQAALEQSGLLDAPRTQRDRSA
Protein: Immunoglobulin heavy variable 4-59 (Ig heavy chain V-II region NEWM) (P01825)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MKHLWFFLLLVAAPRWVLSQVQLQESGPGLVKPSETLSLTCTVSGGSISSYYWSWIRQPPGKGLEWIGYIYYSGSTNYNPSLKSRVTISVDTSKNQFSLKLSSVTAADTAVYYCAR
Protein: 26S proteasome subunit RPT4 (26S protease subunit SUG2) (Proteasomal cap subunit) (P53549)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
Interaction partners:
- Proteasome subunit alpha type-4
- 26S proteasome regulatory subunit RPN8
- 26S proteasome complex subunit SEM1
- 26S proteasome regulatory subunit RPN3
- Proteasome subunit beta type-4
- Ubiquitin carboxyl-terminal hydrolase 6
- 26S proteasome regulatory subunit RPN5
- 26S proteasome regulatory subunit RPN12
- 26S proteasome regulatory subunit RPN6
- Proteasome subunit beta type-6
Sequence:
MSEEQDPLLAGLGETSGDNHTQQSHEQQPEQPQETEEHHEEEPSRVDPEQEAHNKALNQFKRKLLEHRRYDDQLKQRRQNIRDLEKLYDKTENDIKALQSIGQLIGEVMKELSEEKYIVKASSGPRYIVGVRNSVDRSKLKKGVRVTLDITTLTIMRILPRETDPLVYNMTSFEQGEITFDGIGGLTEQIRELREVIELPLKNPEIFQRVGIKPPKGVLLYGPPGTGKTLLAKAVAATIGANFIFSPASGIVDKYIGESARIIREMFAYAKEHEPCIIFMDEVDAIGGRRFSEGTSADREIQRTLMELLTQMDGFDNLGQTKIIMATNRPDTLDPALLRPGRLDRKVEIPLPNEAGRLEIFKIHTAKVKKTGEFDFEAAVKMSDGFNGADIRNCATEAGFFAIRDDRDHINPDDLMKAVRKVAEVKKLEGTIEYQKL
Protein: glucuronosyltransferase (EC 2.4.1.17) (D3XD69)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- Mitochondrial pyruvate carrier
- Cytochrome P450, family 3, subfamily A, polypeptide 65
- Aldehyde oxidase 6
- Xanthine dehydrogenase/oxidase
- Aromatase
Sequence:
MPVPSSTHGHPKMGLVAFIWCIVLTFASAGEAVKSKEASWTGSLLVVPMDGSHWTGVKALAEEMGRRGHKVTVVIPEVSVLLGPGKHYVTRTFPVLYGKQQLDELQARNAQVMESKQLPLMEKISTRFSNMRKFVNLQRATAESLLLNQELVDFLRKQNFDAVLTSPAVPTGAILAYNLSLPAVYMLRGLPCGLDSVATACPNPPSYIPRFFTHSSDRMSFGQRVLNVLVSMLEPLLCRLIYWTTEDVASRFMQRDVSVTEVLSSGALWLLRYDFTLEFPKPLMPNMVLIGGINCAIRHPLTKEVEEFVNGSGEHGIVVFSLGSLVSSMPKEKADIFFKAFSMIPQRVLWRYTGEIPNNVPENVKLMKWLPQNDLLGHPKARAFITHGGTHGIYEGICHGVPMVMLPLFGDQADNVHRVATRGVGVILSIHDITVETLLDALNSVINNSSYKQKMQKLSAIHNDRPIQPLDLAVFWTEFVMRHKGADHLRPAAHELNWLQYHSLDVIGFMLLIVLIVTLAMLKCCSLCWRRCCRKTQKRKED
Protein: Peptide methionine sulfoxide reductase B2, chloroplastic (AtMSRB2) (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductasemethionine) (Q9C5C8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Specifically reduces the MetSO R-enantiomer. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. May play an essential function in association with MSRB1 in maintaining vegetative growth during environmental constraints, through the preservation of photosynthetic antennae. MSRB1 and MSRB2 account for most of the leaf peptide MSR capacity.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15923321}.
Interaction partners:
- Peptide methionine sulfoxide reductase A3
- Peptide methionine sulfoxide reductase A4, chloroplastic
- Uncharacterized protein
- Peptide methionine sulfoxide reductase A2
Sequence:
MAFNIITPGRVYSATSLTFVSTIKAAFVKPPLASPSRRNLLRFSSSPLSFPSLRRGFHGGRIVAMGSSAPESVNKPEEEWRAILSPEQFRILRQKGTEYPGTGEYNKVFDDGIYCCAGCGTPLYKSTTKFDSGCGWPAFFDGLPGAITRTPDPDGRRIEITCAACGGHLGHVFKGEGFPTPTDERHCVNSISLKFTPENPTL
Protein: WD repeat-containing protein 26 (H0Y9R3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XTKLATGSKDTTVIIWQVDPDTHLLKLLKTLEGHAYGVSYIAWSPDDNYLVACGPDDCSELWLWNVQTGELRTKMSQSHEDSLTSVAWNPDGKRFVTGGQRGQFYQCDLDGNLLDSWEGVRVQCLWCLSDGKTVLASDTHQRIRGYNFEDLTDRNIVQEDHPIMSFTISKNGRLALLNVATQGVHLWDLQDRVLVRKYQGVTQGFYTIHSCFGGHNEDFIASGSEDHKVYIWHKRSELPIAELTGHTRTVNCVSWNPQIPSMMASASDDGTVRIWGPAPFIDHQNIEEECSSMDS
Protein: Small conductance calcium-activated potassium channel protein (Protein SK) (dSK) (Q7KVW5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ETV5-related protein Ets96B
Sequence:
MSIQKLNDTTNSGYVSSEETDSLLVSSSNPSKGGGRTALLRQVKSNSTNGPTTGASTSSSGSVSGGGGGSGSGGGSASGSAAGASKPTLMRQDRTSTYLTSPQQSQHARMGSEESMRGGASGAAGHDEDVEQGLVRSSIVPDIEVHEEDQEQHSQQLNATTMATMTNNQQQQQPTISIMNLSLKPGDSHSHSSSPGSHPNLGTSSYQNLASSIPPSVPSRCRACRNCSRRASTTPTTLIDRSASRDSVKSAFQQGNLSGSMAICISNSALPQQQQLQQQYHLQQQQQQHYQLQQHHLHQQQLQQSQQQVPPVLITSSPTNGSRIIRQSSQPESSSTAICCGPHSACVGHAHSHSHTVPNVSLKQLRESSGDGIAGIAADSLRINGGMRPFKQLRKPASTLSIPGSMKTPSIANREQISSGCNEEAAEALVGIHSDYPRYEMYMEERALTGGNTSRKPSTNSAKHKPNVGYRLGKRKALFEKRKRISDYALVMGMFGIIVMVIENELSSAGVYTKASFYSTALKTLISVSTVILLGLIVAYHALEVQLFMIDNCADDWRIAMTWQRISQIGLELFICAIHPIPGEYYFQWTTKLANKNKTIGTEMVPYDVALSLPMFLRLYLICRVMLLHSKLFTDASSRSIGALNRINFNTRFVLKTLMTICPGTVLLVFMVSLWIIASWTLRQCERFHDEEHANLLNSMWLTAITFLCVGYGDIVPNTYCGRGITLTCGMVGAGCTALLVAVVSRKLELTRAEKHVHNFMMDTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQNTVYEIISDMSSRQDAIEERLTNLEDKMQSIQEHMESLPDLLSRCLTQHQERIEQRRNFLHPDTAAVAPIQAPTPQSMFNAAPMLFPHSS
Protein: Maintenance of telomere capping protein 4 (P38335)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:14562095}. Note=Punctate pattern.
Interaction partners:
- Defect at low temperature protein 1
- Maintenance of telomere capping protein 2
- Uncharacterized protein YBR259W
- Protein SLM6
- Putative proline--tRNA ligase YHR020W
- Probable proline--tRNA ligase, mitochondrial
- Maintenance of telomere capping protein 6
- Glutamate--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, mitochondrial
- Glutamine--tRNA ligase
Sequence:
MTHTNEHDHKAEQQQNGRGDTTTETVNPQKMKLVTKLLIDNKFGLMDDLNFSIPLTASSEGVPISAKTSELGTEYLKNQQENSVSPILPISRSTRIKADRVRIYLDYYYNILERCISIDSSQNHHEGVEGVYNPLQVIRNRKLKKKHHELPTREFYTTKHPIIAIKQFSKKPNKKMPWFVDINEKYMDLTWRTSHWEELVDPQGKLWFQSYSPSNESSGSSSSRRHHGHHIHPRRHLQHHSRVRTANSVHSNTQSLTPKRVMTNEEDNNNHNNNNMITKIATTPEAQISRNKKSDLNLSHIHLEVPITNTVTNTSSDQGSLIIEAKGSSYGGDRRGSSNTSGSGGKRNSKHYRSKSAGPPENEKSRMNGLEKIISKTSKGWSRSPKKNTPGLEKQVLLNPTISNGGTSRRSSNNGESISTNSSKSSMGITFGNTETYKTPVDNGKDAIIRQSLLSEVPVHTLRGKTSNRSLRAEGEQALESDKELPNGAGSIYEGAPREKTTSQGSEPVGLVSDSLQVDEQLQRYWHDTRYIMSTVAMMQHRRETHDIVKRREIARRNEIEITQDADTNIRKTADALTQYDNELNKVLKLGNDWTSKLLNDYSIRVETLISSSDRILSDINTTLTLKLKMFQENTERYVTVKVMRAQKMTKTIYRLLEFGIVLVLWTIWFLFSVLRSIRFTIFLVLKIIKALLW
Protein: Ferredoxin (P83522)
Organism: Hordeum vulgare (Barley)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:P00228}.
Interaction partners:
Sequence:
ATYKVKLVTPEGEVELEVPDDVYILDQAEEEGIDLPYSCRAGSCSSCAGKLVSGEIDQSDQSFLDDDQMEEGWVLTCAAYPKSDVVIETHKEEELTA
Protein: SERTA domain-containing protein 2 (Transcriptional regulator interacting with the PHD-bromodomain 2) (TRIP-Br2) (Q14140)
Organism: Homo sapiens (Human)
Function: Acts at E2F-responsive promoters as coregulator to integrate signals provided by PHD- and/or bromodomain-containing transcription factors. May act as coactivator as well as corepressor of E2F1-TFDP1 and E2F4-TFDP1 complexes on E2F consensus binding sites, which would activate or inhibit E2F-target genes expression. Modulates fat storage by down-regulating the expression of key genes involved in adipocyte lipolysis, thermogenesis and oxidative metabolism.
Subcellular location: Nucleus {ECO:0000269|PubMed:18316374}. Cytoplasm {ECO:0000269|PubMed:18316374}. Note=Exported out of the nucleus via its NES in a XPO1-dependent manner. Once in the cytoplasm, is degraded by the proteasome.
Interaction partners:
Sequence:
MLGKGGKRKFDEHEDGLEGKIVSPCDGPSKVSYTLQRQTIFNISLMKLYNHRPLTEPSLQKTVLINNMLRRIQEELKQEGSLRPMFTPSSQPTTEPSDSYREAPPAFSHLASPSSHPCDLGSTTPLEACLTPASLLEDDDDTFCTSQAMQPTAPTKLSPPALLPEKDSFSSALDEIEELCPTSTSTEAATAATDSVKGTSSEAGTQKLDGPQESRADDSKLMDSLPGNFEITTSTGFLTDLTLDDILFADIDTSMYDFDPCTSSSGTASKMAPVSADDLLKTLAPYSSQPVTPSQPFKMDLTELDHIMEVLVGS
Protein: Hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2 (Q5QP01)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGWSCLVTGAGGLLGQRIVRLLVEEKELKEIRALDKAFRPELREEFSKLQNRTKLTVLEGDILDEPFLKRACQDVSVVIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPTPYPYSKKLAEKAVLAANGWNLKNGDTLYTCALRPTYIYGEGGP
Protein: Disintegrin and metalloproteinase domain-containing protein 21 (ADAM 21) (EC 3.4.24.-) (Disintegrin and metalloproteinase domain-containing protein 31) (ADAM 31) (Q9JI76)
Organism: Mus musculus (Mouse)
Function: May be involved in sperm maturation and/or fertilization. May also be involved in epithelia functions associated with establishing and maintaining gradients of ions or nutrients.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 2
- A disintegrin and metallopeptidase domain 30
- Disintegrin and metalloproteinase domain-containing protein 25
Sequence:
MECFIMLGADARTLMRVTLLLLWLKALPSLIDLSQTGSTQYLSSPEVVIPLKVTSRARGAKNSEWLSYSLVFGGRRHVVHMRVKKLLVSTHIPVLTYTEEHTPLSDYPFVPSDCYYHGYVEGALESLVAFSACNGGLQGVLQMNGFSYEIEPIKHSSTFEHLVYTLNNNKTQFPPMLCSLTEKRLLYQPFGVEEAKKSAMKQNYGKLWPHMWFLELAVVVDYGFFTNAQQNLSKVRGDVVLVVNMVDSMYKPLDTYVTLVGIEIWNRGNVLPMENIHQVLEDFSHWKQISLSQVHHDAAHIFIRSSLISVLGIAYIAGICRPPLDCGVENFQGDAWSLFANTVAHELGHTFGMKHDEESCSCGKSGCVMSTFRVPAERFTNCSYSDFMKTTLNQGTCLYNHPRPGAGFLVKRCGNGMVESEEECDCGSVQECEQDPCCFLNCTLRPAAACSFGLCCKDCKFMLLGELCRPKINECDLPEWCNGTSHQCPEDGYVQDGVPCGAGAYCYQKQCNNHDQQCREIFGKGARSASHNCYKEINLQGNRFGHCGTDGTVFLKCRMSDVFCGKVHCENVEDIHHPQAPYVLQNIYANGITCWSTGHCLGMGVPDVGEVKDGTTCGVGKICLHKKCVSLSVLSNACLPETCNRKGVCNNKHHCHCDYGWSPPFCLHRGYGGSIDSGPTSQKRRVIITVLSITVPVLSILICLLIAGLYRIYCKIPSGPKETKASSPG
Protein: G-protein regulator 2 (Q03569)
Organism: Caenorhabditis elegans
Function: In the 1-cell embryo, probably together with gpr-1, controls nuclear rotation and spindle elongation during mitosis. Complex of gpr-1 and gpr-2, in association with lin-5, activates G-protein signaling to affect mitotic spindle force. Polarity determinants (par genes) may regulate lin-5/gpr-1/gpr-2/goa-1 locally to create the asymmetric forces that drive spindle movement.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:14534135}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12730122}. Note=Located to the spindle and cell cortex when in complex with lin-5 and gpr-1 (PubMed:12730122). During early embryogenesis, cortical localization changes with the cell cycle. In one-cell embryo, uniform cortical localization from prophase to metaphase and posterior enrichment during anaphase. In the 2-cell embryo, uniform cortical localization in AB blastomere and posterior cortical enrichment in P1 blastomere during interphase. In P1, uniform cortical localization from prophase to early anaphase and then posterior cortical enrichment during late anaphase and telophase (PubMed:12730122, PubMed:14534135). Cortical localization and asymmetrical distribution is regulated by the csnk-1-mediated regulation of pkk-1 (PubMed:18694560). Enriched at the contact site between EMS and P2 from prophase to prometaphase (PubMed:14534135). {ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:14534135, ECO:0000269|PubMed:18694560}.
Interaction partners:
- Guanine nucleotide-binding protein alpha-16 subunit
- Guanine nucleotide-binding protein G
- Spindle apparatus protein lin-5
- G-protein regulator 1
- HoloCentric chromosome binding Protein
Sequence:
MDVSYYDGPKDEVIEAMLKSAVTAMKLGQYEDGKGRLEDTMEFGTSNFQLLGTIYMYYGRVCRHLNHDAKALEFFEHELNMFKLIFNYPEACDSTRRIVQQALKMEKFSKARRFAEDLIDYTSNKKNGEKYIGQARILFASVCLEGCERDVESNQDEKKKLLSICAEQIAAVKLFNENNTEGAVSETKIMLIEAKCLSLDEKYEESRRKYQECIDFAIKTDQFEAVHIAYYDKALYAETYLLFFIIRDLRSALFYATKFGKERDVVKYKSKLSEEMLRNGEFHEAYLYGLEALVSIRKLGLNEHIGDVLLTIAKCLIALGKRRQAAYFIILGSVLTINQSSFKLFYEQIDVAMNQERSETATDQDACLAIDSSPDPTSSNDMINKFVVKLEHATNVETWEMIVNGIIEDQKKPVAIEKKENEEPVDMMDLIFSMSSRMDDQRTELSAARFIPPRPVSSASKKTTKSHRILPGLRANWTKVQSMKFDGHTMNRILKRSKKSKSSLDSTNSIQGDDTRSDDVTMTSK
Protein: RAB11 family interacting protein 2 (A0A8I6A5U7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Recycling endosome {ECO:0000256|ARBA:ARBA00004172}.
Interaction partners:
Sequence:
MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLMQGNPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKSDGVFSDTSSAIVPSTHMPDANPEFSSGEMQMKSKPKKPFLLGPQRLSSAHSMSDLTGSHLSSEKLKSSTVGPTHLLSHQINSFGVVPESGSLKSPHRRTLSFDTSKLNQPGSIVDEGEHCFGRQSDPFTNVTASLPQKFATLPRKKNPFEESSEPWDSSTNLFSKPIEVRKESKREKREKVSLFERVTGKRDSRRSDKLNNGGSDSPCDLKSPSAFNENRQDYFEYESTNPFTAKFRASTIMPSSSFHMNPTSSDDLRKIPDSNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAASLCCRQVFLPLWTLP
Protein: Cytochrome P450 94B1 (EC 1.14.14.48) (Jasmonoyl-L-amino acid 12-hydroxylase) (Q9FMV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydroxylase involved in the oxidation of the plant hormone jasmonoyl-L-isoleucine (JA-Ile), a bioactive phytohormone of the jasmonate-mediated signaling pathway. Converts JA-Ile to 12-hydroxy-JA-Ile.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- IAA-amino acid hydrolase ILR1-like 6
- IAA-amino acid hydrolase ILR1-like 4
- Cytosolic sulfotransferase 15
- Probable long-chain-alcohol O-fatty-acyltransferase 6
- KIB1-4 beta-propeller domain-containing protein
- 60S ribosomal L18a-like protein
Sequence:
MEMLNAIILILFPIIGFVLIFSFPTKTLKAKTASPSNPTSYQLIGSILSFNKNRHRLLQWYTDLLRLSPSQTITVDLLFGRRTIITANPENVEHILKTNFYNFPKGKPFTDLLGDLLGGGIFNSDGELWSSQRKLASHEFTMRSLREFTFEILREEVQNRLIPVLSSAVDCGETVDFQEVLKRFAFDVVCKVSLGWDPDCLDLTRPVPELVKAFDVAAEISARRATEPVYAVWKVKRFLNVGSEKRLREAIKTVHLSVSEIIRAKKKSLDIGGDVSDKQDLLSRFLAAGHGEEAVRDSVISFIMAGRDTTSAAMTWLFWLLSQNDDVETKILDELRNKGSLGLGFEDLREMSYTKACLCEAMRLYPPVAWDSKHAANDDILPDGTPLKKGDKVTYFPYGMGRMEKVWGKDWDEFKPNRWFEEEPSYGTKPVLKSVSSFKFPVFQAGPRVCIGKEMAFTQMKYVVGSVLSRFKIIPVCNNRPVFVPLLTAHMAGGLKVKIKRREQCDSMYI
Protein: Ribosomal Protein, Small subunit (A8WIR1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLKVIVRFLTVMMKHGYIGEFEIVDDHRAGKIVVNLTGRLNKASVISPRLNIRLNDLEKYTNTLLPSRQFGYLILTTSAGIMDHEEARRKHLGGKILGFFF
Protein: FI24002p1 (Salt-inducible kinase 2 (EC 2.7.11.1)) (Q9W532)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- CREB-regulated transcription coactivator, isoform B
Sequence:
MSTCEAAAAGENGSQAKSEESQPPEDQKKKQPQHERNEKQLDKPPENLPQNGKTEAKGAEGACSHPPLDALRSSVLLDAGAASPSIDAIVACKDALLAQKLFASGGGSTPGPSPTSSAVGAGGISGKDLLKLKEPMRVGFYDIERTIGKGNFAVVKLARHRITKNEVAIKIIDKSQLDQTNLQKVYREVEIMKRLKHPHIIKLYQVMETKNMIYIVSEYASQGEIFDYIAKYGRMSESAARFKFWQIISAVEYCHKKGIVHRDLKAENLLLDLNMNIKIADFGFSNHFKPGELLATWCGSPPYAAPEVFEGKQYTGPEIDIWSLGVVLYVLVCGALPFDGSTLQSLRDRVLSGRFRIPFFMSSECEHLIRRMLVLEPTRRYTIDQIKRHRWMCPELLEHVLIAKYNLGAERQTSVEPSEDILRIMAEYVGIGSDKTRASLKKNTYDHVAAIYLLLQDRVSHKKEQSNGLGASALASSTSASRMIYSSRNDHQPTQQQSQQQSKTISTSSILAKDQCHKRLSRHQTVLMSERNAHAGATPTVPDPGPGYYAKYGPLQLPLPLTGHSHLTGYLNGGGVEVDASGIPLPMRYTPLPTAASPAPSNCSSTSSRVGRHSLSSSSPRSHRPVAISLSIDNNPSLANLRCREMMEAGGGPVGAVGVPLASKQLHQTISEFIIKQSTEDCRALLQQSTAVAEGKDDPPKAESSVGGVPPPASTTPTSSTAGPESGSAPCPGEINGKTIKTMSSSSSFDSKANLGQSFRYKMSAEASKLFQTLQESPLPVEQRTKRRVHVGSTNGSGGDSGQETNDAKSNGDSRSEKKVLAQGSSSTDEGCETDQGNDPGSASQESKGSNGGGSGNANGGPTSHSSSDLTRLVGTTTSGQSHKMRSYASSSSSSGVLAGSAGSYSKSLSQNLSRGSSKSNCSGPYDSLDFALPSGKGSLPSCMGSSSMLATPTPASASPAGISSEHSSERSLYGSHNSCIHMPGALPLGLGLPQSSASTPTPNPTPPPNGGGVTFLDKRSPIHFREGRRASDGLVAQGLLSSGSLLGTSRVYGSYRYEQAKRHGWLEIQQLQQLQQEAAVGHSHPHAHQHPHQHPHPHPQAYGLEELCQFPNGQFYALPGKHHPLLTLPHHHAHPAQHHHGHHSLFHSGHQATPLLLEAAAGGDMYGHGCYAPPPPPPGLYTHHQLGVGMAVPMSPMQKPPLQQQLLQHRLLQQKRQLFQKQYALEAQLAGRHHHHQQHSHHHHHHFGHSLGPPPPPAPAPEHHLADELYELALLDRPRSGTPRLQHSMTMPGAHAFSQMNLKTSYISQSDQVPGAAPNGAGSGGSAAGVSCSAPPSTAPGTPTVKCKPTTPHGHSLDSDYHTSTPVLSLFTPNWQSLVKPLSESPILEISEHLESV
Protein: Protein unc-50 homolog (Uncoordinated-like protein) (O55227)
Organism: Rattus norvegicus (Rat)
Function: Involved in the cell surface expression of neuronal nicotinic receptors. Binds RNA.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:10980252}; Multi-pass membrane protein {ECO:0000269|PubMed:10980252}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q53HI1}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- RIC3 acetylcholine receptor chaperone
- Protein disulfide-isomerase TMX3
Sequence:
MLPSTSLNSSMYGNGALNSRDAARHTAGAKRYKYLRRLFRFRQMDFEFAAWQMLYLFTSPQRVYRNFHYRKQTKDQWARDDPAFLVLLSIWLCVSTIGFGFVLDMGFFETIKLLLWVVFIDCVGVGLLISTLMWFISNKYLVKRQSRDYDVEWGYAFDVHLNAFYPLLVILHFIQLFFINHVILTDTFIGYLVGNTLWLIAVGYYIYVTFLGYSALPFLKNTVVLLYPFAPLIVLYGLSLALGWNFTHTLCSFYKYRVK
Protein: Signal recognition particle protein (EC 3.6.5.4) (Fifty-four homolog) (A0A0H2UQC2)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}. Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. {ECO:0000256|HAMAP-Rule:MF_00306}.
Interaction partners:
Sequence:
MAFESLTERLQNVFKNLRKKGKISESDVQEATKEIRLALLEADVALPVVKDFIKKVRERAVGHEVIDTLNPAQQIIKIVDEELTAVLGSDTAEIIKSPKIPTIIMMVGLQGAGKTTFAGKLANKLKKEENARPLMIAADIYRPAAIDQLKTLGQQIDVPVFALGTEVPAVEIVRQGLEQAQTNHNDYVLIDTAGRLQIDELLMNELRDVKALAQPNEILLVVDAMIGQEAANVAREFNAQLEVTGVILTKIDGDTRGGAALSVRHITGKPIKFTGTGEKITDIETFHPDRMSSRILGMGDMLTLIEKASQEYDEQKALEMAEKMRENTFDFNDFIDQLDQVQNMGPMEDLLKMIPGMANNPALQNMKVDERQIARKRAIVSSMTPEERENPDLLNPSRRRRIAAGSGNTFVEVNKFIKDFNQAKQLMQGVMSGDMNKMMKQMGINPNNLPKNMPNMGGMDMSALEGMMGQGGMPDLSALGGAGMPDMSQMFGGGLKGKIGEFAMKQSMKRMANKMKKAKKKRK
Protein: Ferredoxin--NADP reductase, chloroplastic (FNR) (EC 1.18.1.2) (Q9SLP6)
Organism: Zea mays (Maize)
Subcellular location: Plastid, chloroplast {ECO:0000256|PIRNR:PIRNR000361}.
Interaction partners:
- Ferredoxin-1, chloroplastic
- Sulfite reductase [ferredoxin], chloroplastic
- Tic62 protein
- Ferredoxin-2, chloroplastic
- assimilatory sulfite reductase
- Photosystem I reaction center subunit VI, chloroplastic
- Ferredoxin--nitrite reductase, chloroplastic
- Ferredoxin--nitrite reductase, chloroplastic
- Uncharacterized protein
- Protein kinase domain-containing protein
Sequence:
MATVMAAAVSSFPSSSAVVAKASPASPCAAPHFRPRAVRAAIRAQASAVEAPATAKAKKESKKQEEGVVTNLYKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGKIPYREGQSIGVIADGVDKNGKPHKVRLYSIASSAIGDFGDSKTVSLCVKRLIYTNDAGEIVKGVCSNFLCDLQPGDNVQITGPVGKEMLMPKDPNATIIMLATGTGIAPFRSFLWKMFFEKHDDYKFNGLGWLFLGVPTSSSLLYKEEFGKMKERAPENFRVDYAVSREQTNAAGERMYIQTRMAEYKEELWELLKKDNTYVYMCGLKGMEKGIDDIMVSLAEKDGIDWFDYKKQLKRGDQWNVEVY