wanglab/gogpt-training-data huggingface dataset:
Protein: cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed] (P09456)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
Subcellular location: Cell membrane {ECO:0000250}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Protein kinase cAMP-dependent X-linked catalytic subunit
- Protein kinase cAMP-dependent type I regulatory subunit beta
- cAMP-dependent protein kinase type II-beta regulatory subunit
- 5'-AMP-activated protein kinase subunit beta-2
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- Hormone-sensitive lipase
- A-kinase anchor protein 1, mitochondrial
- A-kinase anchor protein 10, mitochondrial
Sequence:
MASGSMAASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEARQIQSLQKSGIRTDSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV
Protein: Glutathione reductase (GRase) (EC 1.8.1.7) (Q2RWK9)
Organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta
- Acetyltransferase component of pyruvate dehydrogenase complex
- Glutathione hydrolase proenzyme
- Gamma-glutamyltransferase
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- Glutathione synthetase
- Thioredoxin-related
- 2-oxoglutarate dehydrogenase E1 component
- Glutathione-dependent peroxiredoxin
- Glutathione peroxidase
Sequence:
MADYDYDLLTIGAGSGGVRASRLAGGFGARVAVVEGSRIGGTCVMRGCVPKKLLVYGAQYANDLEDMIGYGWSMGGVAFDWPSLITAKNRELDRLEGVYRTMLRNGNVALLEGRARFLDAHSVDIDGKTVTADKILIAVGGWPQMPVIPGIEHAITSNEALDLMVMPERLTIVGGGFIAVEFASIFNALGVDVSVVIRKDKILRGFDADIRDTLTEELVRRGITIVPGTVINRIDKRPGGGYRLIRTPGEAIDTDLVMYATGRAPNTAGLGLEAAGVKVAASGAVIVDEWNRTTVDTIYAIGDVTDRIALTPVAINEAIAFAHTVFNDTPRVMDYENVASAVFSQPPVGTVGLTEEQARARGPVRIFRTRFRAMKHVLAGRDEKTMMKLVVDARTDRVLGCHMVGADAPEIIQGLAVALKCGATKAQFDATIGIHPTAAEEFVTMRDPVPEPVFAQPAD
Protein: 2-oxoglutarate dehydrogenase complex component E1 (EC 1.2.4.2) (2-oxoglutarate dehydrogenase, mitochondrial) (Alpha-ketoglutarate dehydrogenase) (Thiamine diphosphate (ThDP)-dependent 2-oxoglutarate dehydrogenase) (F1Q5B8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHRLRTCAARLRPITASQTAKNLSQQGPAATPRTFQPLRCFSSPVAAEPFLNGTSSNYVEEMYYAWLENPKSVHKSWDIFFRNANAGAPPGTAYQSPPPLGVSLAGLAQAQSLVGAQPNVEKLVEDHLAVQSLIRAYQVMGHHNANLDPLGISCVNFDEAPVATGFQHVGFYGLEESDLDKVFRLPTTTFIGGDESALPLREIIRRLEMAYCQHIGVEFMFINDLDQCQWIRQKFERPGVMQFSLEEKRTLLARMVRSTRFEEFLQRKWSSEKRFGLEGCESLIPALKTIIDKSSENGVDTVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINRVTNRNITLSLVANPSHLEAVNPVVQGKTKAEQFYSGDTDGKRVMSILLHGDAAFAGQGIVYETFHLSDLPSYTTHGTVHVVANNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVMYVCNVAAEWRATFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIKKQKGVLQKYAEKLIAEGAVTRQEYEEEIAKYDKICEEAHSRSKDEKILHIKHWLDSPWPGFFTLDGQPKSISCPSTGLPEEELAQIGQVASSVPVEDFTIHGGLSRILKGRGDMIKNRTVDWALGEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQNVDKRICIPMNHMSPNQAPYTVCNSSLSEYGVLGFELGFAMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLPHGMEGMGPEHSSARPERFLQMCNDDPDFNPKITDDFDVRQLYDCNWIVVNCSNPANYFHVIRRQILLPFRKPLIVFTPKSLLRHPEAKSNFDQMLPGTHFQRVITDDGPPAQNPSEVKRIVFCTGKIYYELTRERKARNMENSVAITRIEQLSPFPFDLVRAETEKFPNADLVWCQEEHKNQGYYDYVKPRMRTTINRTKPVWYAGREPAAAPATGNKNTHLLELKRFLDTAFNLDAFKDHI
Protein: Fetal and adult testis-expressed transcript protein (Cancer/testis antigen 43) (CT43) (Tumor antigen BJ-HCC-2) (Q969F0)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of endoplasmic reticulum (ER)-mitochondria coupling. Negatively regulates the ER-mitochondria distance and Ca(2+) transfer from ER to mitochondria possibly implicating it in the regulation of apoptosis. May collaborate with RNF183 to restrain BIK protein levels thus regulating apoptotic signaling.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:26567849, ECO:0000269|PubMed:27402544}. Mitochondrion outer membrane {ECO:0000269|PubMed:27402544}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27402544}; Single-pass membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305|PubMed:27402544}. Note=Localized to specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. Also associated with the outer surface of mitochondria at sites that are not in close contact with the ER. {ECO:0000269|PubMed:27402544}.
Interaction partners:
- Emerin
- E3 ubiquitin-protein ligase RNF183
Sequence:
MAGGPPNTKAEMEMSLAEELNHGRQGENQEHLVIAEMMELGSRSRGASQKKQKLEQKAAGSASAKRVWNMTATRPKKMGSQLPKPRMLRESGHGDAHLQEYAGNFQGIRFHYDRNPGTDAVAQTSLEEFNVLEMEVMRRQLYAVNRRLRALEEQGATWRHRETLIIAVLVSASIANLWLWMNQ
Protein: FT-interacting protein 3 (Multiple C2 domain and transmembrane region protein 3) (Q9M2R0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for proliferation and differentiation of shoot stem cells in the shoot apical meristem (SAM), thus determining the appropriate balance between the maintenance of shoot stem cells and their differentiation into other aboveground plant parts via the control of subcellular localization and intercellular trafficking of STM in the shoot apex. Prevents intracellular trafficking of STM to the plasma membrane in cells in the peripheral shoot meristem region thus facilitating STM recycling to the nucleus to maintain stem cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9FL59}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29259105, ECO:0000269|PubMed:29742441}. Vesicle {ECO:0000250|UniProtKB:Q9C8H3}. Cell membrane {ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9C8H3}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ribose-phosphate pyrophosphokinase 4
- Protein C2-DOMAIN ABA-RELATED 7
- Protein FLOWERING LOCUS T
- Protein STRUBBELIG
- Ribose-phosphate pyrophosphokinase 1, chloroplastic
- Ribose-phosphate pyrophosphokinase 5, chloroplastic
- CAP superfamily protein
Sequence:
MQRPPPEDFSLKETRPHLGGGKLSGDKLTSTYDLVEQMQYLYVRVVKAKELPGKDMTGSCDPYVEVKLGNYKGTTRHFEKKSNPEWNQVFAFSKDRIQASFLEATVKDKDFVKDDLIGRVVFDLNEVPKRVPPDSPLAPQWYRLEDRKGDKVKGELMLAVWFGTQADEAFPEAWHSDAATVSGTDALANIRSKVYLSPKLWYLRVNVIEAQDLIPTDKQRYPEVYVKAIVGNQALRTRVSQSRTINPMWNEDLMFVAAEPFEEPLILSVEDRVAPNKDEVLGRCAIPLQYLDRRFDHKPVNSRWYNLEKHIMVDGEKKETKFASRIHMRICLEGGYHVLDESTHYSSDLRPTAKQLWKPNIGVLELGILNATGLMPMKTKDGRGTTDAYCVAKYGQKWIRTRTIIDSFTPRWNEQYTWEVFDPCTVVTVGVFDNCHLHGGEKIGGAKDSRIGKVRIRLSTLETDRVYTHSYPLLVLHPNGVKKMGEIHLAVRFTCSSLLNMMYMYSQPLLPKMHYIHPLTVSQLDNLRHQATQIVSMRLTRAEPPLRKEVVEYMLDVGSHMWSMRRSKANFFRIMGVLSGLIAVGKWFEQICNWKNPITTVLIHLLFIILVLYPELILPTIFLYLFLIGIWYYRWRPRHPPHMDTRLSHADSAHPDELDEEFDTFPTSRPSDIVRMRYDRLRSIAGRIQTVVGDLATQGERLQSLLSWRDPRATALFVLFCLIAAVILYVTPFQVVALCIGIYALRHPRFRYKLPSVPLNFFRRLPARTDCML
Protein: Trypsin zeta (EC 3.4.21.4) (P42280)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Uncharacterized protein, isoform A
- Bazooka, isoform B
- FI02848p
- Peptidase M14 domain-containing protein
- Peptidase S1 domain-containing protein
- Zinc carboxypeptidase A 1
- Peptidase S1 domain-containing protein
- Trypsin theta
- Peptidase S1 domain-containing protein
- trypsin
Sequence:
MSSSWIVGLLAFLVSLVALTQGLPLLEDLDEKSVPDGRIVGGYATDIAQVPYQISLRYKGITTPENPFRHRCGGSIFNETTIVTAAHCVIGTVASQYKVVAGTNFQTGSDGVITNVKEIVMHEGYYSGAAYNNDIAILFVDPPLPLNNFTIKAIKLALEQPIEGTVSKVSGWGTTSPGGYSSNQLLAVDVPIVSNELCDQDYEDFGDETYRITSAMLCAGKRGVGGADACQGDSGGPLAVRDELYGVVSWGNSCALPNYPGVYANVAYLRPWIDAVLAGL
Protein: Follistatin-related protein 1 (Follistatin-like protein 1) (Q567W5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MIIRTRFLFIALSFVCCYAEGVRSKSKVCANVLCGAGRECSVTEKGEPTCLCIEQCKPHNHPVCGSNGKMYQNHCELHRDACLTGVKIQISHDGQCEEKKMEKIINSPIVCYLADRNELRSRVIEWLQSEVEPDGWFSKGSNFSDVLLKYFQSYDNGDAQLDSAELLKFIQHNETAVNITSPYAEDENNRLLRSLCVDALIELSDENADWKLSFDEFLNCLRPGFNPPERKCALEDETYEDGAETQMECNRCICACGNWVCTAVICDGSNKLQALEEMEGNNQEMTEEEWVQRVAELNKHQETVEKMKMGDKEV
Protein: NADPH oxidase (Q2PEN8)
Organism: Epichloe festucae
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSYYYPGGSDAGSERPSERSRWTPLTRMLLSGEMTQEKQQELSPREKFDRWMINEGYRRVFVFVFMLTHALIFSFASVHYALKDSLQSARDIFGFTFTIARASALVLHIDVGIILFPVCRTLISLMRQTPLNGIIQFDKNITFHITTAWSIVFFSWVHTIAHWNNFAQVAAKNKLGFYGWLLANFASGPGWTGYVMLIALMGMVITSVEKPRRANYERFWYTHHMFIVFFFFWSLHGAFCMIQPDVAPFCTSIGASAIGVFWQYWMYGGFIYLAERVAREIRGRHKTYISKVIQHPSQVCEIQIKKENTKTRAGQYIFFCCPAVSLWQYHPFTLTSAPEEDYISIHMRCQGDFTMAVSQALGCEWGKKEDTSKVVGIDGDSNGVDPALQKVLPRVYVDGPFGSASEDVFKYETAILVGAGIGVTPFASILKSIWYRMNYPQKKTRLSKVYFFWICRDFGSFEWFRSLLLAVEAQDVENRIEIHTYLTAKIKADDATNIMINDANADKDTITGLRSPTNFGRPNWDMIFRGIRKIHCPGEAGVFFCGPKGLGSSLHVYCNKYTEPGFSYVWGKENF
Protein: LSD1 zinc finger family protein (F4JUW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQDQLVCHGCRNLLMYPRGASNVRCALCNTINMVPPPPPPHDMAHIICGGCRTMLMYTRGASSVRCSCCQTTNLVPESSFTLLFDNILKVLKTKLLDGPGGLAHSNQVAHAPSSQVAQINCGHCRTTLMYPYGASSVKCAVCQFVTNVNMSNGRVPLPTNRPNGTACPPSTSTSTPPSQTQTVVVENPMSVDESGKLVSNVVVGVTTDKK
Protein: E3 ubiquitin-protein ligase HECTD3 (EC 2.3.2.26) (HECT domain-containing protein 3) (HECT-type E3 ubiquitin transferase HECTD3) (Q3U487)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus facilitating cell cycle progression by regulating the turn-over of TRIOBP (By similarity). Mediates also ubiquitination of STX8.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:18821010}.
Interaction partners:
Sequence:
MAGPGPGAALESPRQLLGRVRFLAEAARSLRAGLPLPAALAFVPREVLYKLYKDPAGPSRVLLPVWEAEGLGLRVGAVGAAPGTGSGPLRAARDSIELRRGACVRTTGEELCNGHGLWVKLTKEQLAEHLSDCSLDEGWLLVCRPAEGGARLVPIDTPDHLQRQQQLFGVDYRPVLRWEQVVDLTYSHRLGSRPQPAEAYTEAIQRLLYVPPTWTYECDEDLIHFLYDHLGKEDENLGSVKQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEGDNLKKLSDVNIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPASLVRYPRLEGTDPEVLYRRAVLLQRFIKILDSVLHHLVPAWDHTLGTFSEIKQVKQFLLLSRQRPSLVAQCLRDSESSKPSFMPRLYINRRLAMEHRACPSRDPACKNAVFTQVYEGLKPSDKYEKPLDYRWPMRYDQWWECKFIAEGIIDQGGGFRDSLADMSEELCPSSADTPVPLPFFVRTANQGNGTGEARDMYVPNPSCRDFAKYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSKDFPAVDSVLVKLLEVMEGVDKETFEFKFGKELTFTTVLSDQQVVELIPGGTGIVVEYEDRSRFIQLVRKARLEESKEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLTRFEDFEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPARIYIYPDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYAAYNCVAIDTDMSPWEE
Protein: Glutamine synthetase cytosolic isozyme 1-5 (EC 6.3.1.2) (Glutamate--ammonia ligase GLN1;5) (GLN1;5) (Q8GXW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm.
Interaction partners:
- Ferredoxin--nitrite reductase, chloroplastic
- Ferredoxin-dependent glutamate synthase 2, chloroplastic
- Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial
- Glutamate synthase 1, chloroplastic
- Glutamate dehydrogenase 1
- Glutamate dehydrogenase 2
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Carbamoyl phosphate synthase small chain, chloroplastic
- glutamate dehydrogenase
- Glutamate--glyoxylate aminotransferase 1
Sequence:
MTSPLSDLLNLDLSDTKKIIAEYIWIGGSGMDIRSKARTLPGPVSNPTKLPKWNYDGSSTDQAAGDDSEVILYPQAIFKDPFRKGNNILVMCDAYRPAGDPIPTNNRHKAVKIFDHPNVKAEEPWFGIEQEYTLLKKDVKWPLGWPLGGFPGPQGPYYCAVGADKAFGRDIVDAHYKACLYSGLSIGGANGEVMPGQWEFQISPTVGIGAGDQLWVARYILERITEICGVIVSFDPKPIQGDWNGAAAHTNFSTKSMRKDGGLDLIKEAIKKLEVKHKQHIAAYGEGNERRLTGKHETADINTFSWGVADRGASVRVGRDTEKEGKGYFEDRRPSSNMDPYLVTSMIAETTIL
Protein: PRORP domain-containing protein (Q38E68)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MSSDCAGPPRQRVRREDDIPLDFSALPAVQELIIKNNRQTKLKRRLKTSDFVNESFSELGCRAVADRTSVGVLSSFLKECTEKHRILPRSSSVARVLYSFVENGLLHEGQALLQQILQAEASLRSKVMDEKVATISLRLLTESDEVNLGLAERIISMLPEGSHKRRLFSPLLEHAARTGDTTLAFKALRMGRQKQLEFWDVDYKQLLRCLQSAAKGTDISALITELLECMVDHHPVVGKTNGEALQQLLGGELTEVNDETGMCCRCSTRVHTFDFAPDDRVTLLRDIETKLIAPRVESGSHYEPGKVVELTERKERWEEFAVFKDTLSRLDYDAVIDGANVGYYGLSNWYRGAKEALLRSRGVDPSTLPEYELCEIPLPVDVPPKFSLIDEMLTEAQKLRKKSVVMLHSRHVRSPSKENLVWLEKWGQESSLIVCPGFLNDDYCWLFAAIHRPNCLVVSNDQMRDHHFSLLSRRSFLRWRQRHLVTYRARFSWATGAVSLLLSLPRPYAVWVQRGQLSPSHWHVPVRTTLDVIDQATNRKTESEMEVDKNGDDFCNAWLCTAAINR
Protein: WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 1 (Growth and differentiation factor-associated serum protein 2) (GASP-2) (mGASP-2) (Q8R0S6)
Organism: Mus musculus (Mouse)
Function: Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease-inhibitor activity (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MPAPQPFLPLLFVFVLIHLTSETNLLPDPGSHPGMCPNELSPHLWVDAQSTCERECTGDQDCAASEKCCTNVCGLQSCVAARFPSGGPAVPETAASCEGFQCPQQGSDCDIWDGQPVCRCRDRCEKEPSFTCASDGLTYYNRCYMDAEACLRGLHLHVVPCKHILSWPPSSPGPPETTARPTPGAAPMPPALYNSPSPQAVHVGGTASLHCDVSGRPPPAVTWEKQSHQRENLIMRPDQMYGNVVVTSIGQLVLYNAQLEDAGLYTCTARNAAGLLRADFPLSVLQRATTQDRDPGIPALAECQADTQACVGPPTPHHVLWRFDPQRGSCMTFPALRCDGAARGFETYEACQQACVRGPGDVCALPAVQGPCQGWEPRWAYSPLLQQCHPFVYSGCEGNSNNFETRESCEDACPVPRTPPCRACRLKSKLALSLCRSDFAIVGRLTEVLEEPEAAGGIARVALDDVLKDDKMGLKFLGTKYLEVTLSGMDWACPCPNVTAVDGPLVIMGEVREGVAVLDANSYVRAASEKRVKKIVELLEKKACELLNRFQD
Protein: Uncharacterized sulfatase YdeN (EC 3.1.6.-) (P77318)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Anaerobic sulfatase-maturating enzyme homolog YdeM
- Anaerobic sulfatase-maturating enzyme homolog AslB
Sequence:
MKSALKKSVVSTSISLILASGMAAFAAHAADDVKLKATKTNVAFSDFTPTEYSTKGKPNIIVLTMDDLGYGQLPFDKGSFDPKTMENREVVDTYKIGIDKAIEAAQKSTPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNTDAQDGIPLTETFLPELFQNHGYYTAAVGKWHLSKISNVPVPEDKQTRDYHDNFTTFSAEEWQPQNRGFDYFMGFHAAGTAYYNSPSLFKNRERVPAKGYISDQLTDEAIGVVDRAKTLDQPFMLYLAYNAPHLPNDNPAPDQYQKQFNTGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDGPLPLNGAQKGYKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAADISIPKDLKLDGVSLLPWLQDKKQGEPHKNLTWITSYSHWFDEENIPFWDNYHKFVRHQSDDYPHNPNTEDLSQFSYTVRNNDYSLVYTVENNQLGLYKLTDLQQKDNLAAANPQVVKEMQGVVREFIDSSQPPLSEVNQEKFNNIKKALSEAK
Protein: Growth hormone-releasing hormone receptor (GHRH receptor) (Growth hormone-releasing factor receptor) (GRF receptor) (GRFR) (Q02644)
Organism: Rattus norvegicus (Rat)
Function: Receptor for GRF, coupled to G proteins which activate adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone gene transcription and growth hormone secretion.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Somatoliberin
- Guanine nucleotide-binding protein G
- Pituitary-specific positive transcription factor 1
- Homeobox protein prophet of Pit-1
- Growth hormone secretagogue receptor type 1
- Appetite-regulating hormone
- Growth hormone receptor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
Sequence:
MDSLLWATWVLCLLNLWGVALGHLHLECDFITQLRDDELACLQAAEGTNNSSMGCPGTWDGLLCWPPTGSGQWVSLPCPEFFSHFGSDPGAVKRDCTITGWSDPFPPYPVACPVPLELLTEEKSYFSTVKIIYTTGHSISIVALCVAIAILVALRRLHCPRNYIHTQLFATFILKASAVFLKDAAVFQGDSTDHCSMSTILCKVSVAVSHFATMTNFSWLLAEAVYLSCLLASTSPRSKPAFWWLVLAGWGLPVLCTGTWVGCKLAFEDTACWDLDDSSPYWWIIKGPIVLSVGVNFGLFLNIICILLRKLGPAQGGLHTRAQYCNYLLPWSCPLPQVPRERTDLGPSSHEITVQESGTRNCQLPWRLSKSTLLLIPLFGIHYIIFNFLPDSAGLGIRLPLELGLGSFQGFVVAVLYCFLNQEVRTEISRKWYGHDPELLPARRTCTEWTTPPRSRVKVLTSEC
Protein: Fatty acid synthase (EC 1.1.1.100) (EC 1.3.1.39) (EC 2.3.1.38) (EC 2.3.1.39) (EC 2.3.1.41) (EC 2.3.1.85) (EC 3.1.2.14) (EC 4.2.1.59) (A5YV76)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MEEVVIAGMSGKLPESENLEEFWANLIGGVDMVTADDRRWKAGLYGLPRRMGKLKDLSRFDASFFGVHSKQANTMDPQLRMLLEVTYEAIVDGGINPASLRGTSTGVWVGVSSSDASEALSRDPETLVGYSMIGCQRAMMANRLSFFFDFKGPSITIDTACSSSLLALQSAYQAIRGGECSAAVVGGLNVLLKPNSSLQFMKLGMLSQDGTCRSFDAEGTGYCRAEAVVAVLLTKKSLARRVYATILNAGTNTDGSKEQGVTFPSGDVQEQLIRSLYAPAGPDPESLEYIEAHGTGTKVGDPQELNGIVNALCATRREPLLIGSTKSNMGHPEPASGVAALIKVLLSLEHGVWAPNLHYHTPNPEIPALQDGRLQVVDRPLPIRGGNVGINSFGFGGSNVHVILQPNSRPAPPPAQHAALPRLLQASGRTLEAVQTLLEQGLRHSRDLAFVGMLNEIAAVSPVAMPFRGYAVLGGEAGSQEVQQVPGSKRPVWFICSGMGAQWQGMGLSLMRLDRFRDSILRSDQALKPLGLRVSDLLLSTDEAVLDDIVSSFVSLTSIQIALIDLLTSLGLQPDGIIGHSLGEVACGYADGCLTQEEAVLSSYWRGYCIKEANVLPGAMAAVGLSWEECKQRCPPGIVPACHNSKDTVTISGPQAAMSEFLQQLKREDVFVKEVRTGGIAFHSYFMESIAPTLLRQLRKVILDPKPRSKRWLSTSIPEAQWQGSLARTFSAEYSVNNLVSPVLFQEALQHVPAHAVVVEIAPHALLQAVLKRSLESSCTIIPLMKKDHRDNLEFFLSNVGRLHLAGVSVNPNGLFPPVEFPAPRGTPLISPHXKWDHSQAWDVPSAADFPSGSSCSSVAVYKFDVSPESPDHYLVDHCIDGRVLFPGTGYLWLTWKTLARALSQNLEETPVVFEDVTLHQATILPKTGTVSLEVRLLEASHAFEVSDSNGSLIASGKVYQWESPDPKLFDTRAAVDPADSTAEFRLSQGDVYKDLRLRGYDYGPFFQLVLESDLEGNRGRLQWNDSWVSFLDAMLHMSILAPGQLGLYLPTRFTSIRIDPVTHRQKLYTLQDTTQAADVVVDRNLNTVVAGGALFLGAHSSVAPRRPQEHLKPILEKFCFTPHVESGCLAGNTALQEELQLCRGLAQALQTKVAQQGLKMVVPGLDGAQAPREAPQQSLPRLLAAACQLQLNGNLQLELGQVLAQERPLLCDDPLLSGLLDAPALKACVDTALENMASPKMKVVEVLAGDGQLYSRIPALLNTQPVMDLDYTATDRNPQALEAAQAKLEQLHVTQGQWDPANPAPGSLGKADLLVCNCALATLGDPAVAVGNMAATLKEGGFLLLHTLLAGHPLGEMVGFLTSPEQGGRHLLSQDQWESLFAGASLHLVALKRSFYGSVLFLCRQQTPQDSPVFLSVEDTSFRWVDSLKDILADASSRPVWLMAVGCSTSGVVGMVNCLRKEPGGHRIRCVLVSNLSSTSPAPEMHPSSSELQKVLQGDLVMNVYRDGAWGAFRHFPLEQDRPEKQTEHAFVNVLSRGDLSSIRWVCSPLHYALPASCQDRLCSVYYTSLNFRDVMLATGKLSPDSIPGKWLTRDCMLGMEFSGRDASGRRVMGMVPAEGLATSVLLLQHATWEVPSTWTLEEAASVPIVYTTAYYSLVVRGRMQPGESVLIHSGSGGVGQAAIAIALSRGCRVFTTVGSAEKRAYLQARFPQLDETCFANSRDTSFEQHVLRHTAGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHALGMAVFLKNVTFHGILLDSLFEEGGATWQEVSELLKAGIQEGVVQPLKCTVFPRTKVEAAFRYMAQGKHIGKVVIQVREEEQGPAPRGLPPIALTGLSKTFCPPHKSYVITGGLGGFGLQLAQWLRLRGAQKLVLTSRSGIRTGYQARQVREWRRQGVQVLVSTSNASSLDGARSLITEATQLGPVGGVFNLAMVLRDAVLENQTPEFFQDVSKPKYSGTANLDRVTREACPELDYFVIFSSVSCGRGNAGQANYGFANSAMERICEKRRHDGLPGLAVQWGAIGDVGVVLETMGTNDTVIGGTLPQRIASCLEVLDLFLSQPHPVLSSFVLAEKKAAAPRDGSSQKDLVKAVAHILGIRDVASINPDSTLVDLGLDSLMGVEVRQILEREHDLVLSMREVRQLSLRKLQELSSKTSTDADPATPTSHEDSPVRQQATLNLSTLLVNPEGPTLTRLNSVQSAERPLFLVHPIEGSITVFHGLAAKLSIPTYGLQCTGAAPLDSIQSLASYYIECIRQVQPEGPYRIAGYSYGACVAFEMCSQLQAQQSATPGNHSLFLFDGSHTFVLAYTQSVRAKMTPGCEAEAEAKAMYFFVQQFTDMEQGKVLEALIPLQGLEARVAATVDLITQSHAGLDRHALSFAARSFYQKLRAAENYWPQATYHGNVTLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESILSIIHSCLAEPRVSVREG
Protein: Phosphodiesterase 4B, cAMP specific (G3UZY9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
KNSPKEFTASESEVCIKTFKEQMRLELELPKLPGNRPTSPKISPRSSPRNSPCFFRKLLVNKSIRQRRRFTVAHTWKLLAMVLCNLVCRLLSHCFSHWNDLYSAMESGMPSERKMNGQRAP
Protein: Gamma-terpinene synthase, chloroplastic (EC 4.2.3.114) (Alpha-terpinene synthase) (EC 4.2.3.115) (Terpene synthase 2) (OvTPS2) (E2E2P0)
Organism: Origanum vulgare (Wild marjoram)
Function: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents. Monoterpene synthase which catalyzes the conversion of geranyl diphosphate (GPP) to gamma-terpinene and the minor products alpha-thujene, alpha-terpinene, myrcene, sabinene, (+)-R-limonene, alpha-pinene and alpha-phellandrene.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MATLSMQVSILSKEVKNVNNIGMRASKPMVARRVSTTRLRPICSASLQVEEETRRSGNYQASIWNNDYVQSFNTNQYKDEKHLKKKEELIAQVKILLNTKMEAVKQLELIEDLRNLGLTYYFQDEVKKILTSIYNDHKCFKNEQVGDLYFTSLGFRLLRLHGFDVSEEVFDFFKNEDGSDFKASLGENIKDVLQLYEASFLIREGEVILEQARVFSTKHLEKKVDEGINDEKLLAWIRHSLALPLHWRIQRLEARWFLDAYRARKDMIPLIFELGKIDFHIIQETQLEELQEVSKWWTNSNLAEKLPFVRDRIVECYFWALGLFEPHEYGYQRKMAAIIITFVTIIDDVYDVYGTLDELQLFTDAIRKWDFQSISTLPYYMQVCYLALYTYASELAYDILKDQGFNSIAYLQRSWLSLVEGFFQEAKWYYAGYTPTLAEYLENAKVSISSPTIISQVYFTLPNSTERTVVENVFGYHNILYLSGMILRLADDLGTTQFELKRGDVQKAIQCYMKDNNATEKEGAEHVKYLLREAWKEMNTAMADPECPLSEDLVDAAANLGRASQFIYLEGDGHGVQHSEIHNQMGGLIFEPYV
Protein: Elongation factor G, chloroplastic (cEF-G) (Elongation factor EF-G/SCO1) (Protein SNOWY COTYLEDON 1, chloroplastic) (AtSCO1) (Q9SI75)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Required for the eoplasts redifferentiation into chloroplasts after germination.
Subcellular location: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_03063, ECO:0000269|PubMed:16525888, ECO:0000269|PubMed:17629920}.
Interaction partners:
- Diphthine--ammonia ligase
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Large ribosomal subunit protein bL28c
- Protein STABILIZED1
- Large ribosomal subunit protein bL31c
- At4g01000
- Elongation factor Tu, chloroplastic
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- At1g43860
- Large ribosomal subunit protein bL9c
Sequence:
MAADALRISSSSSGSLVCNLNGSQRRPVLLPLSHRATFLGLPPRASSSSISSSIPQFLGTSRIGLGSSKLSQKKKQFSVFAAAEAEAKRAVPLKDYRNIGIMAHIDAGKTTTTERILYYTGRNYKIGEVHEGTATMDWMEQEQERGITITSAATTTFWDKHRINIIDTPGHVDFTLEVERALRVLDGAICLFDSVAGVEPQSETVWRQADKYGVPRICFVNKMDRLGANFFRTRDMIVTNLGAKPLVLQIPIGAEDVFKGVVDLVRMKAIVWSGEELGAKFSYEDIPEDLEDLAQEYRAAMMELIVDLDDEVMENYLEGVEPDEATVKRLVRKGTITGKFVPILCGSAFKNKGVQPLLDAVVDYLPSPVEVPPMNGTDPENPEITIIRKPDDDEPFAGLAFKIMSDPFVGSLTFVRVYSGKISAGSYVLNANKGKKERIGRLLEMHANSREDVKVALTGDIIALAGLKDTITGETLSDPENPVVLERMDFPDPVIKVAIEPKTKADIDKMATGLIKLAQEDPSFHFSRDEEMNQTVIEGMGELHLEIIVDRLKREFKVEANVGAPQVNYRESISKIAEVKYTHKKQSGGQGQFADITVRFEPLEAGSGYEFKSEIKGGAVPREYIPGVMKGLEECMSTGVLAGFPVVDVRACLVDGSYHDVDSSVLAFQLAARGAFREGMRKAGPRMLEPIMRVEVVTPEEHLGDVIGDLNSRRGQINSFGDKPGGLKVVDSLVPLAEMFQYVSTLRGMTKGRASYTMQLAKFDVVPQHIQNQLSSKDQEVAA
Protein: 4-alpha-glucanotransferase (EC 2.4.1.25) (Amylomaltase) (Disproportionating enzyme) (D-enzyme) (P9WK23)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Glycogen operon protein GlgX homolog
- 1,4-alpha-glucan branching enzyme GlgB
- Glucose-1-phosphate adenylyltransferase
- Glycogen phosphorylase
- Putative maltooligosyl trehalose synthase
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- Maltokinase
- Trehalose synthase/amylase TreS
- Alpha-maltose-1-phosphate synthase
- Glycogen synthase
Sequence:
MTELAPSLVELARRFGIATEYTDWTGRQVLVSEATLVAALAALGVPAQTEQQRNDALAAQLRSYWARPLPATIVMRAGEQTQFRVHVTDGAPADVWLQLEDGTTRAEVVQVDNFTPPFDLDGRWIGEASFVLPADLPLGYHRVNLRSGDSQASAAVVVTPDWLGLPDKLAGRRAWGLAVQLYSVRSRQSWGIGDLTDLANLALWSASAHGAGYVLVNPLHAATLPGPAGRSKPIEPSPYLPTSRRFVNPLYLRVEAIPELVDLPKRGRVQRLRTNVQQHADQLDTIDRDSAWAAKRAALKLVHRVPRSAGRELAYAAFRTREGRALDDFATWCALAETYGDDWHRWPKSLRHPDASGVADFVDKHADAVDFHRWLQWQLDEQLASAQSQALRAGMSLGIMADLAVGVHPNGADAWALQDVLAQGVTAGAPPDEFNQLGQDWSQPPWRPDRLAEQEYRPFRALIQAALRHAGAVRIDHIIGLFRLWWIPDGAPPTQGTYVRYDHDAMIGIVALEAHRAGAVVVGEDLGTVEPWVRDYLLLRGLLGTSILWFEQDRDCGPAGTPLPAERWREYCLSSVTTHDLPPTAGYLAGDQVRLRESLGLLTNPVEAELESARADRAAWMAELRRVGLLADGAEPDSEEAVLALYRYLGRTPSRLLAVALTDAVGDRRTQNQPGTTDEYPNWRVPLTGPDGQPMLLEDIFTDRRAATLAEAVRAATTSPMSCW