wanglab/gogpt-training-data huggingface dataset:
Protein: Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau) (P10637)
Organism: Mus musculus (Mouse)
Function: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10636}. Cell membrane {ECO:0000250|UniProtKB:P10636}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10636}; Cytoplasmic side {ECO:0000250|UniProtKB:P10636}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P10636}. Cell projection, axon {ECO:0000250|UniProtKB:P10636}. Cell projection, dendrite {ECO:0000250|UniProtKB:P10636}. Secreted {ECO:0000250|UniProtKB:P10636}. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000250|UniProtKB:P10636}.
Interaction partners:
Sequence:
MADPRQEFDTMEDHAGDYTLLQDQEGDMDHGLKESPPQPPADDGAEEPGSETSDAKSTPTAEDVTAPLVDERAPDKQAAAQPHTEIPEGITAEEAGIGDTPNQEDQAAGHVTQGRREGQAPDLGTSDWTRQQVSSMSGAPLLPQGLREATCQPSGTRPEDIEKSHPASELLRRGPPQKEGWGQDRLGSEEEVDEDLTVDESSQDSPPSQASLTPGRAAPQAGSGSVCGETASVPGLPTEGSVPLPADFFSKVSAETQASQPEGPGTGPMEEGHEAAPEFTFHVEIKASTPKEQDLEGATVVGVPGEEQKAQTQGPSVGKGTKEASLQEPPGKQPAAGLPGRPVSRVPQLKARVASKDRTGNDEKKAKTSTPSCAKAPSHRPCLSPTRPTLGSSDPLIKPSSPAVSPEPATSPKHVSSVTPRNGSPGTKQMKLKGADGKTGAKIATPRGAASPAQKGTSNATRIPAKTTPSPKTPPGSGEPPKSGERSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSASKSRLQTAPVPMPDLKNVRSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
Protein: Probable LRR receptor-like serine/threonine-protein kinase At1g05700 (EC 2.7.11.1) (C0LGD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Cotton fiber protein
- DEAD-box ATP-dependent RNA helicase 36
- Uncharacterized protein
- Cellulase
- Glycine-rich protein like
- Cation/H
- WAT1-related protein At1g09380
- PEARLI 4 protein family protein)
- Probable WRKY transcription factor 66
- Peptide methionine sulfoxide reductase B9
Sequence:
MEEFRFLYLIYSAAFALCLVVSVLAQDQSGFISIDCGIPSGSSYKDDTTGINYVSDSSFVETGVSKSIPFTAQRQLQNLRSFPEGSRNCYTLIPIQGKGKKYLIRASFMYGNYDGENGSPEFDLFLGGNIWDTVLLSNGSSIVSKEVVYLSQSENIFVCLGNKGKGTPFISTLELRFLGNDNTTYDSPNGALFFSRRWDLRSLMGSPVRYDDDVYDRIWIPRNFGYCREINTSLPVTSDNNSYSLSSLVMSTAMTPINTTRPITMTLENSDPNVRYFVYMHFAEVEDLSLKPNQTREFDISINGVTVAAGFSPKYLQTNTFFLNPESQSKIAFSLVRTPKSTLPPIVNALEIYVANSFSQSLTNQEDGDAVTSLKTSYKVKKNWHGDPCLPNDYIWEGLNCSYDSLTPPRITSLNLSSSGLTGHISSSFSNLTMIQELDLSNNGLTGDIPEFLSKLKFLRVLNLENNTLTGSVPSELLERSNTGSFSLRLGENPGLCTEISCRKSNSKKLVIPLVASFAALFILLLLSGVFWRIRNRRNKSVNSAPQTSPMAKSENKLLFTFADVIKMTNNFGQVLGKGGFGTVYHGFYDNLQVAVKLLSETSAQGFKEFRSEVEVLVRVHHVNLTALIGYFHEGDQMGLIYEFMANGNMADHLAGKYQHTLSWRQRLQIALDAAQGLEYLHCGCKPPIVHRDVKTSNILLNEKNRAKLADFGLSRSFHTESRSHVSTLVAGTPGYLDPLCFETNGLNEKSDIYSFGVVLLEMITGKTVIKESQTKRVHVSDWVISILRSTNDVNNVIDSKMAKDFDVNSVWKVVELALSSVSQNVSDRPNMPHIVRGLNECLQREESNKNY
Protein: Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (ENR) (EC 1.3.1.9) (Cold shock-induced protein 15) (CSI15) (NADH-dependent enoyl-ACP reductase) (Vegetative protein 241) (VEG241) (P54616)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism.
Interaction partners:
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Beta-ketoacyl-[acyl-carrier-protein] synthase III 1
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- Phosphate acyltransferase
- Beta-ketoacyl-[acyl-carrier-protein] synthase III 2
- Enoyl-[acyl-carrier-protein] reductase FabL
- Acyl carrier protein
- Putative oxidoreductase YtkK
Sequence:
MNFSLEGRNIVVMGVANKRSIAWGIARSLHEAGARLIFTYAGERLEKSVHELAGTLDRNDSIILPCDVTNDAEIETCFASIKEQVGVIHGIAHCIAFANKEELVGEYLNTNRDGFLLAHNISSYSLTAVVKAARPMMTEGGSIVTLTYLGGELVMPNYNVMGVAKASLDASVKYLAADLGKENIRVNSISAGPIRTLSAKGISDFNSILKDIEERAPLRRTTTPEEVGDTAAFLFSDMSRGITGENLHVDSGFHITAR
Protein: 3-hydroxyphenylacetate 6-hydroxylase (EC 1.14.13.63) (Q078T0)
Organism: Emericella nidulans (Aspergillus nidulans)
Function: Catalyzes the hydroxylation of 3-hydroxyphenylacetate and 3,4-dihydroxyphenylacetate to 2,5-dihydroxyphenylacetate (homogentisate) and 2,4,5-trihydroxyphenylacetate, respectively. Both of these compounds are used as substrate by homogentisate dioxygenase in the homogentisate pathway. The homogentisate pathway is used to catabolize phenylacetate and use it as a carbon source. Can also catalyze the hydroxylation of phenylacetate to 2-hydroxyphenylacetate at low efficiency to compensate for loss of phacA.
Interaction partners:
Sequence:
MAIAEALLFVNNRAVEHPLQFLTAVAFAVPLLYVVINEFIRASARIPGFKGPRGLPLIGNLAQIRKDAAEQYRIWSKIYGPVYQIQLGNIPVLVVNSAAAAKVLFGQNAQALSSRPEFYTFHKIVSNTAGTTIGTSPYSESLKRRRKGAASALNRPSVESYVHHLDVESKAFVAELFKYGNGGKTPVDPMAMIQRLSLSLALTLNWGVRVASQEEELFDEITEVEDKISKFRSTTGNLQDYIPILRLNPFSSNSHKAKEMRDRRDKYLSSLNRDLDDRMEKGTHKPCIQANVILDKEAKLNSEELTSISLTMLSGGLDTVTTLVAWSISLLAQRPDIQDKAAKAIQEMYSEGQPLCDPADDQKCAYVAALVRECLRYYTVLRLALPRTSIRDITYDGKVIPKGTVFFLNAWACNMDPEVWSDPDEFRPERWFEQPDAPMFTYGMGYRMCAGSLLANRELYLVFIRTLNSFRIEPTEEKIEWHPLKGNSDPTSLVAIPKKYKVRFVPKNEVSLVEALS
Protein: Early placenta insulin-like peptide (EPIL) (Insulin-like peptide 4) (Placentin) [Cleaved into: Early placenta insulin-like peptide B chain; Early placenta insulin-like peptide A chain] (Q14641)
Organism: Homo sapiens (Human)
Function: May play an important role in trophoblast development and in the regulation of bone formation.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Insulin-like peptide INSL6
- Prorelaxin H1
- Prorelaxin H2
- Insulin-like 3
- Relaxin-3
Sequence:
MASLFRSYLPAIWLLLSQLLRESLAAELRGCGPRFGKHLLSYCPMPEKTFTTTPGGWLLESGRPKEMVSTSNNKDGQALGTTSEFIPNLSPELKKPLSEGQPSLKKIILSRKKRSGRHRFDPFCCEVICDDGTSVKLCT
Protein: Tubulin beta chain (B1PBV8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MREILHIQGGQCGNQIGAKFWEVVCAEHGIDATGRYQGDLDLQLERINVYYNEASCGRFVPRAVLMDLEPGTMDSIRSGPVGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSTVCDIPPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFKRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADDEEYEEEEEEPEYED
Protein: HCG1985507, isoform CRA_a (Rho GDP-dissociation inhibitor 3) (F1T0H7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLGLDACELGAQLLELLRLALCARVLLADKEGGPPAVDEVLDEAVPEYRAPGRKSLLEIRQLDPDDRSLAKYKRVLLGPLPPAVDPSLPNVQVTRLTLLSEQAPGPVVMDLTGDLAVLKDQVFVLKEGVDYRVKISFKVHREIVSGLKCLHHTYRRGLRVDKTVYMVGSYGPSAQEYEFVTPVEEAPRGALVRGPYLVVSLFTDDDRTHHLSWEWGLCICQDWKD
Protein: G-protein alpha 13a (Guanine nucleotide-binding protein (G protein), alpha 13a) (Guanine nucleotide-binding protein subunit alpha-13a) (Q5YKG3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Lysophosphatidic acid receptor 1
- Rho guanine nucleotide exchange factor
- Rho guanine nucleotide exchange factor
- Rho guanine nucleotide exchange factor
- Rho guanine nucleotide exchange factor
- Lysophosphatidic acid receptor 2b
- Lysophosphatidic acid receptor 2a
- Endothelin receptor type Ab
- Endothelin-1 receptor
- Alpha-1A adrenergic receptor
Sequence:
MADFLPSRTAIVCIPNCLLSSGEIDQIRKSKEIDKSLSREKTYVKKLVKILLLGAGESGKSTFLKQMRIIHGQDFDQRAKEEFRATIYSNVIKGVRVLVDAREKLHIPWGNPENQAHGETVMAFDTRSSLMAKGMMETKVFLNFLPAIRALWQDSGIQNAYDRRREFQLGESVKYFLDNVDKLGQLDYLPSQKDILLARKPTKGIHEYEFEIKNVPFKMVDVGGQRSERKRWFECFDSVTSILFLVSSSEYDQVLMEDRQTNRLTESLNIFETIVNNRVFANVSIILFLNKTDLLEDKVKTVNIKDYFSEFTGEPHNLQDVQKFLVECFRNKRREQQQKPLYHHFTTAINTENIRLVFRDVKDTILHDNLKQLMLQ
Protein: Glutamate synthase [NADPH] small chain (EC 1.4.1.13) (Glutamate synthase subunit beta) (GLTS beta chain) (NADPH-GOGAT) (P09832)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate.
Interaction partners:
- Glutamate synthase large chain
- Glutamine synthetase
- NADP-specific glutamate dehydrogenase
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreA
- NADH-quinone oxidoreductase subunit F
- Carbamoyl phosphate synthase large chain
- Bifunctional protein PutA
- Formate dehydrogenase H
- Glutamine--fructose-6-phosphate aminotransferase
- Amidophosphoribosyltransferase
Sequence:
MSQNVYQFIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTLPEVCGRVCPQDRLCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSMRGGLENEDADGVYAALPFLIANTKQLMGFGETRDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEENMPGSRREVKNAREEGVEFKFNVQPLGIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPHNMEWLAKHSVELDSQGRIIAPEGSDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWLEV
Protein: PAR-domain protein 1, isoform C (Q8IQ98)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRMDYQMPPPALALQQQQQHGMQHQQQQLQLLQNVQQQQQQQQQQQQQHQQQQLLGNMSQTAALPPLSSLPLQVVHNLPHLLAGNSGGNTGNNPNTSNSNLNVACNNNLLRGNMQHQQQQQQLLNNLSNGNNVASGTLPPPTQLLQHHLQHLAHVNVNAAAAVVAVAANNLQQQQQQQQHASSNNVTGGSPGSNSNNNNNNNNILNHNNLNIIINNHASLNNNNNNSNNNNNNNNNPATPNANLAASNNATPTVNTASAVAQQQQAHENSLVNSLVGVINNSNNNNNNTNNNNNNNTNSNSNNNNNNSVGGDDNNRWTQFQVQQLWKQHANYLNGKSTSNSKEIICPDDKYKEEGDIWNVEAQTAFLGPNLWDKTLPYDADLKVTQYADLDEFLSENNIPDGLPGTHLGHSSGLGHRSDSLGHAAGLSLGLGHITTKRERSPSPSDCISPDTLNPPSPAESTFSFASSGRDFDPRTRAFSDEELKPQPMIKKSRKQFVPDELKDDKYWARRRKNNIAAKRSRDARRQKENQIAMRARYLEKENATLHQEVEQLKQENMDLRARLSKFQDV
Protein: Calsequestrin (Q08BX6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004564}.
Interaction partners:
Sequence:
MKWRWVIWGVLLSLGYQCWSETGLDFPEYDGKDRVHQLTAKNYKSVMKKYDVMVIYLHKPVGEDRMARKQFEVEELALELAAQVLDGLDDEDIGFGLVDSKKDRAVAKKLGMLEVDSIYIFADDEIIEYDGALAADTLLEFLYDVIEDPVEIISNDRELKGFHNIEEDMKLMGFFKSNKSPYFIEYDDAAEEFHPFIKFFATFEPKIAKKLNLKMNEVDFYEPFMDKPVTIPGKPYMEDDIINFIEDHDRPTLRKLEPHSMYEIWEDDINGQHIVAFAEESDPDGYEFLEILKEVAQENTENPELSIIWIDPDDFPLMVPYWEKTFGIDLSSPQIGVVDVENADSVWMEMDDEEHMPTADQLDAWIEDVMTGNINPNDENQYHDDDDEDDDDHDDEDDDDHDDDDDDEDEDHDDDDDDEDLDDDDDEDLDEDDDDDEDHDDDD
Protein: Auxin-responsive protein SAUR66 (Protein SMALL AUXIN UP RNA 66) (Q9C7Q1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May promote auxin-stimulated organ elongation, such as hypocotyls, stamen filaments and petals.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:F4I1H5}; Peripheral membrane protein {ECO:0000250|UniProtKB:F4I1H5}.
Interaction partners:
- Auxin-responsive protein SAUR20
- Uncharacterized protein At4g24700
- Protein trichome birefringence-like 12
- AT2G45990 protein
- Probable LRR receptor-like serine/threonine-protein kinase At1g51810
- Carboxyl-terminal proteinase-like protein
- Uncharacterized protein T14D3.50
- Probable serine protease EDA2
- Expressed protein
- Pathogenesis-related thaumatin superfamily protein
Sequence:
MMNTKKLIKMFRKWQQRAALHRKRISFQRPSTRSTTVEKGCFVVYTADNTRFAFPISYLSNSVFQEILEISEEEFGLPTGGPITLPFDSVFLEYLIKLIKRRMDGDTEKALLMSISSARCSLQKQEQSTQQLLVF
Protein: Lectin29Ca (Q6GUX1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYKYATCIFSIFALWNFWGVFAKKQDTSTGTNELPKAPMPYYTIENIDMHQQHWFTYNSLRQNGTLWRIGNMEQRLEMRLQSFQNQMETQLRALKQQIEPYMENVKMSNKIKMYVFKKIGSRHFYLEKQKKMPWDSAYDTCRQMGGHLANILDEKELNEIFSEETKKKYWVDINSRANDGASWISTPSGRDVPFLKWKPNLATNIHNHCVYINSNEMYFENCANDNYFACQAEQWA
Protein: Kinesin-like protein (Q00084)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
SSRSHAIFQVHIRITERKTDTKRTVKLSMIDLAGSERAASTKGIGVRFKEGATINKSLLALGNCINKLADALKHIPYRDSNLTRILKDSLGGNCRTLMVANVSMSSLTYEDTYNTLKY
Protein: Ribose-phosphate pyrophosphokinase 2 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase 2) (P38620)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: 5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (PRS2, PRS3, PRS4 and PRS5).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 4
- Ribose-phosphate pyrophosphokinase 5
- Amidophosphoribosyltransferase
- Transketolase 1
- Transketolase 2
- Phosphoribomutase
- Ribokinase
- ADP-ribose pyrophosphatase
- Ribose-5-phosphate isomerase
Sequence:
MSTNSIKLLAGNSHPGLAELISQRLGVPLSKVGVYQYSNKETSVTIGESIRDEDVYIIQTGYGEHEINDFLMELLILIHACKTASVRRITAVIPNFPYARQDKKDKSRAPITAKLIANLLETAGCDHVITMDLHASQIQGFFHIPVDNLYGEPSVLNYIRTKTDFNNAILVSPDAGGAKRVASLADKLDMNFALIHKERQKANEVSRMLLVGDVAGKSCLLIDDMADTCGTLVKACDTLMDHGAKEVIAIVTHGIFSGSAREKLINSRLSRIVCTNTVPVDLDLDIVDQVDISPTIAEAIRRLHNGESVSYLFTHAPV
Protein: Subtilisin-like serine protease Pen c 1 (EC 3.4.21.-) (Alkaline serine protease) (allergen Pen c 1) (Q9Y749)
Organism: Penicillium citrinum
Function: Serine protease. Hydrolyzes azocasein. Cleaves peptide bonds of the oxidized insulin B chain preferably at 15-Leu-|-Tyr-16, but also at 4-Gln-|-His-5 and 24-Phe-|-Phe-25, and to a lesser extent at 5-His-|-Leu-6 and 25-Phe-|-Tyr-26. Hydrolyzes amide bonds between amino acids and 7-amino-4-methylcoumarin (AMC) in vitro.
Subcellular location: Secreted {ECO:0000255, ECO:0000269|PubMed:10103041}.
Interaction partners:
Sequence:
MGFLKVLATSLATLAVVDAGTLLTASNTDAVIPSSYIVVMNDDVSTAEFNTHREWATNVHARLSRRKNGETGPGKHFEINGLKGYTASFDESTAKDIANDPAVKYIEPDMIVNATANVVQSNVPSWGLARISSKRTGTTSYTYDSTAGEGVVFYGVDTGIDISHSDFGGRAKWGTNVVDNDNTDGNGHGTHTASTAAGSKYGVAKKATLVAVKVLGADGSGTNSGVISGMDWAVKDAKSRGANGKYVMNMSLGGEFSKAVNDAAANVVKSGIFLSVAAGNEAENASNSSPASAAEVCTIAASTSTDGSASFTNFGSVVDLYAPGQSITAAYPGGGSKTLSGTSMAAPHVAGVAAYLMALEGVSAGNACARIVQLATSSISRAPSGTTSKLLYNGINV
Protein: AP-1 complex subunit gamma-1 (Clathrin assembly protein complex 1 gamma large chain) (Clathrin assembly protein large gamma chain) (Gamma-adaptin) (Q12028)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin. Component of the AP-1-related (AP-1R) complex, an adapter protein complex that mediates sorting of cargo SNARE SNC1. In contrast to the APM1-containing AP-1 complex, AP-1R is incapable of sorting CHS3.
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- AP-1 complex subunit sigma-1
- AP-1 complex subunit beta-1
- AP-1 complex subunit mu-1-I
- AP-2 complex subunit beta
- Clathrin heavy chain
- Polyphosphatidylinositol phosphatase INP53
- Epsin-3
- Epsin-5
- Adaptin medium chain homolog APM2
- AP-2 complex subunit sigma
Sequence:
MGSSLRSFIKDVRGAKTLADERAIITKQSAKIRTKLRDDHLPHEKRRVNIQKLLYLYILGEKTHFGQVESINLIASDDFVDKRLGYLAATLLLDESEDLLTLLTNMLNNDLHHPNKYAVSLALTSLGFLSSPELARDLYPDVENIIKNSRDPFLLKKALQCAAKLIFKDVSLLEIFNIEDITKILSSHSICTHGVLLGVTKIIQSILLIGLNRKKDEDEDEDGIDYSNDILSPLSLLLRDFFIRLENMNSKNIEPGYDVQGICDPFLQCEIIYTLKLYFQVGELLNSNNVLDYKDNFCDLLTRIATNTDSTKNSGQAILYETVKTIFSLDLNQPLRVLGINILAKFLAGKDNNTKYVSLNTLLKVVPQEPTAVQRHRKFISHCLQDTDVSIRMRALELSFAILDDSNLVELVNELMKFLAKQDEDSKDLIIYTIDHLIDTFDTRVVKDESWKLDVFFNILKLVGSFINYEKINDILIIINNTSQLSDKSEFLRKMLTISLNGTSAEISEENIGWQLVLIWCIGEYGDLVLNEGNKNGADIINESSITDYLLTLQELYTATNLKIINYILTAALKLSVRFHDAKNIEKLRQLILSYTDSTDLSLQMKSNQYEIFFNQSISVKKIILETMPKFEKITEEQDNGKALSKNLISNEPVDLLSDLLGEDSKAESKASTGDNVKPIDILEEIFGEKNDIAQVPKNANKEESINHSSAVEANSGVTLPLDANKIYDSSSLNVYASLLSANSGLAHLDLYFQAKSLISDLKTFCAVPKAQKLTLGQLYPSSTINASQICKQSLKISGSGKLKLRVKLDFHLNGSSSITNEQFDHKFDETL
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FVH7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome A complete sequence
Sequence:
MKELLYFTLLAGAQAYLKLDFTRVPSASVLEKRADDLSPVPLRNDVDQYIVQLAVGTPPQMVSVQLDTGSADLWFSGADNPYCKTNKKKAPKSKDLQPVDNSGFPTNPDQIGKKARNLDCKKYGFFNMSSSSTFKNNDTDIFLYYEDLSFVRGTWGTDVVSLGGLNISGVNFAVAEISNSSSGVLGVSLPSEESTYSINSNGTTNATNYQYSNLPLQLKEQGIIDKVTYSIYLNDTKSKYGSILFGAVDHSKYTGTLYTLPLVNSEYDVVNKPYELDITLNGIGYQSMSSNMTLYDQKVAALIDSGTTISEFPDEIVEVVAKQMNATVDPNGNGIRLAKCPSKKDNAKLLFNLGGALIYVDIKEFTTKVKGKCYLEIIPSGAESDLVILGDNFMRSVYTVFDLEANEVSIAQANFNSSLPAQIEEIKSTVPSAVKAPQYYNTFSAIASISSVTGDIFGPEATAYMAPPANVSNSSNSSNSSAVSLERRSYDNAATPLRLNSIILIGVAAILATIFM
Protein: Alpha-onocerin synthase LCD (EC 5.4.99.66) (A0A125SXN2)
Organism: Lycopodium clavatum (Stag's-horn clubmoss)
Function: Oxidosqualene cyclase involved in the biosynthesis of alpha-onocerin, a triterpenoid characterized by a symmetrical structure due to cyclizations at both termini of dioxidosqualene that inhibits acetylcholinesterase. Catalyzes the second half of the cyclization, exclusively from pre-alpha-onocerin.
Interaction partners:
Sequence:
MWRLRTGSSTVDKADSWLSSLNNHLGRQIWCYDPEAGTPQEREAVEAECARFTANRHQQRQSADTLLRLQFQKEHSANRLPSRITVNEDHEVTEDDVTTTLCRALQFYSQLQTDDGHWSGDHSGPMFFLPGMVIALYVTGALDSVLSEHHQREICRYIYNHQRQDGSWGLHPEGTGTLFGTVLSYVTLRLMGESKSNSNNREALRKAQTWIIDHGGATDVPSWGKFWLAVLGVYEWSGVNPLPPESWLLPKSLIAHPGRLPVLYRFIFLPMSYIYARRLSHHLTKIIEDLRKELYTIPYEDIDWNHARKLGAKEEIVPRSVVQDVILSILHNYVEPIMSHWPGFLLRQKALALIMEHIHHEDETTQYLCVCPVSKALNMLCCWLEDRNSDAFKKHLSRVLDFLWLSEDGMKMQVCNGSQLWDTALSVRALISANLLNECSSMLRRAKLYIENTQIQESYPGDLDHWHRITSKGGWPQSTRDWGWPVSDCTAEALQAVLALSSQSTTDVGEALPEERIHECINVLLSFQKSNGSFAPFDARNPLEGPKIWNHTESPGYKSLDFECVECTSSVIQALAAFNKIYPEHRAKEISISIQEGTRFIERLQNSDGSWSGTWGICFTYATWFGIMGLLASGARYYESIAIQRACEFILSKQLPNGGWGEHFHSFKNKVYTNLEGERAHVVHTSWSMLALLATGQEGRDAIPLHRAAKILINAQMETGDYSQEGVVGAVCGDHTISYATYRCVFPIWALGEYRYKLFGKKNMYI
Protein: Delta-6 fatty acyl desaturase (B7U6V1)
Organism: Rachycentron canadum (Cobia) (Gasterosteus canadus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGGGGQLTEPGSGRAGGVYTWEEVQRHSSRSDQWLVIDRKVYNITQWATRHPGGLRVISHYAGEDATEAFAAFHPDPTFVQKFLKPLQIGELAASEPSQDRNKNAAIIQDFHALRAQAESEGLFQTQPLFFCLHLGHIVLLEALAWLMIWHWGTNWILTLLCAVMLATAQSQAGWLQHDFGHLSVFKKSSWNHLLHKFAIGHLKGASANWWNHRHFQHHAKPNIFRKDPDVNMLSIFVVGATQPVEYGIKKIKHMPYHRQHQYFFLVGPPLLIPVFFHIQIMHTMISRHDWVDLVWSMSYYLRYFCCYVPLYGLFGSLALISFVRFLESHWFVWVTQMNHLPMDIDHEKHRDWLTMQLQATCNIEQSFFNDWFSGHLNFQIEHHLFPTMPRHNYHLVAPHVRALCEKYGIPYQIKTMWQGLTDIVRSLKNSGDLWLDAYLHK
Protein: Laminin subunit gamma 1 (F1MAA7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
- Laminin subunit beta-1
- Laminin subunit alpha-5
- Nidogen-1
- Integrin beta-1
- Integrin alpha-6
- CD44 antigen
- Laminin subunit alpha 3
- Laminin subunit beta-2
- Laminin subunit gamma-2
- Major prion protein
Sequence:
MTGGRRAALALQLQRRLWLLLAVLAAVACWVRAAMDECADEGGRPQRCMPEFVNAAFNVTVVATNTCGTPPEEYCVQTGVTGVTKSCHLCDAGQLHLQHGAAFLTDYNNQADTTWWQSQTMLAGVQYPNSINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGFIRTGGDEQQALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNDPKVLKSYYYAISDFAVGGRCKCNGHASECVKNEFGKLVCNCKHNTYGVDCEKCLPFFNDRPWRRATAESANQCLPCDCNGRSQECYFDPELYRSTGHGGHCTNCRDNTDGAKCERCRENFFRLGNTEACSPCHCSPVGSLSTQCDSYGRCSCKPGVMGDKCDRCQPGFHSLTEAGCRPCSCDPSGSTDECNVETGRCVCKDNVEGFSCERCKPGFFNLESSNPKGCTPCFCFGHSSVCTNAVGYSVYDISSTFQIDEDGWRVEQRDGSEASLEWSSDRQDIAVISDTYFPRYFVAPAKFLGNQVLSYGQNLSFSFRVDRRDTRLSAEDLVLEGAGLRVSVPLIAQGNSYPSETTVKYIFRLHEATDYPWRPALSPFEFQKLLNNLTSIKIRGTYSERSAGYLDDVTLQSARPGPGVPATWVESCTCPVGYGGQFCETCLPGYRRETPSLGPYSPCVLCTCNGHSETCDPETGVCDCRDNTAGPHCEKCSDGYYGDSTLGTSSDCQPCPCPGGSSCAIVPKTKEVVCTHCPTGTAGKRCELCDDGYFGDPLGSNGPVRLCRPCQCNDNIDPNAVGNCNRLTGECLKCIYNTAGFYCDRCKEGFFGNPLAPNPADKCKACACNPYGTVQQQSSCNPVTGQCQCLPHVSGRDCGACDPGFYNLQSGQGCESCDCHALGSTNGQCDIRTGQCECQPGITGQHCERCETNHFGFGPEGCKPCDCHHEGSLSLQCKDDGRCECREGFVGNRCDQCEENYFYNRSWPGCQECPACYRLVKDKVAEHRVKLQELESLIANLGTGDETVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNNSLHSQISRLHNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEPNNMTLLAEEARRLAERHKQEADDIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALESEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAKKGRNTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIASGVQKNATSTKADAERTFSEVTDLDNEVNGMLRQLEEAENELKRKQDDADQDMMMAGMASQAAQEAELNARKAKNSVSSLLSQLTDLLEQLGQLDTVDLNKLNEIEGSLNKAKDEMKVSDLDRKVSNLENEARKQEAAILDYDRDIAEIIKDIHNLEDIKKTLPTGCFNTPSIEKP
Protein: Peptide methionine sulfoxide reductase B3 (AtMSRB3) (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase) (Q9M0Z6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. Involved in cold tolerance. Eliminates MetSO and reactive oxygen species that accumulate at the ER during cold acclimation. MSRB family specifically reduces the MetSO R-enantiomer (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:17956860}.
Interaction partners:
- Peptide methionine sulfoxide reductase A3
- Peptide methionine sulfoxide reductase A2
- Peptide methionine sulfoxide reductase A4, chloroplastic
- Peptide methionine sulfoxide reductase A1
Sequence:
MNIVNSKILFLSFTLLLLLQSSIVESDSICLSSGVASTVAMAAPGSVQKGDEEWRAILSPEQFRILRQKGTEYPGTGEYVNFDKEGVYGCVGCNAPLYKSTTKFNAGCGWPAFFEGIPGAITRTTDPDGRRIEINCATCGGHLGHVFKGEGFATPTDERHCVNSVSLKFTPAASSL
Protein: At1g19690 (NAD(P)-binding Rossmann-fold superfamily protein) (Q147R9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Thylakoid lumenal P17.1 protein
- ADP-glucose phosphorylase
Sequence:
MAVFQLPSLSPEIPFRFTPTPLKFSNRRRINFFRPLSATDDSRSGAPDPESPNQMFILGMGFVGGFFAQQLKESDWVVSGTCRSDSKKKEWEKRGINLHPFSADSPEWSLLDSVKDYTHLLISIPPLADIGDPMLRNVELVRDKLSSGNLRWLCYLSSTSVYGDCGGAWVNENHLPNPKTQSAKVRLAAEQGWLSLGRDLGVSTQILRLGGIYGPGRSAIDTLLKQERLSEGQKRRASRKFTSRVHVEDICQVLKAATEKPASGEIYNIVDDDPAAREEVFEYALELIEKRWPGNITTKPFPFLYESREESSLRGEKRVCNERMKDKLGVKLLYPSYKSGLQSIVENMDNRF