wanglab/gogpt-training-data huggingface dataset:
Protein: MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAP-K5) (MAPKAPK-5) (MK-5) (MK5) (EC 2.7.11.1) (p38-regulated/activated protein kinase) (PRAK) (Q8IW41)
Organism: Homo sapiens (Human)
Function: Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement.
Subcellular location: Cytoplasm. Nucleus. Note=Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export.
Interaction partners:
- Mitogen-activated protein kinase 6
- Heat shock protein beta-1
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 4
- Mitogen-activated protein kinase 11
- DnaJ homolog subfamily B member 1
- Mitogen-activated protein kinase 13
- Heat shock protein beta-2
- Septin-7
Sequence:
MSEESDMDKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALRHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKIDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPILRKRKLLGTKPKDSVYIHDHENGAEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQEAWKYNRECKLLRDTLQSFSWNGRGFTDKVDRLKLAEIVKQVIEEQTTSHESQ
Protein: Ras-related protein Rap-1b (EC 3.6.5.2) (Q6TEN1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Probable GTP-binding protein that possesses GTPase activity. May play a role in endothelial cell polarity and endothelial barrier function (By similarity).
Subcellular location: Cell membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cell junction {ECO:0000250}. Note=May shuttle between plasma membrane and cytosol. {ECO:0000250}.
Interaction partners:
- Ras-related protein Rap-1b
- CRK SH3-binding GNRP
- non-specific serine/threonine protein kinase
- Rap guanine nucleotide exchange factor
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
- Plexin C1
Sequence:
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNSCAFLESSAKSKINVNEIFYDLVRQINRKTPVTGKPRKKSTCQLL
Protein: Linker for activation of T-cells family member 1 (36 kDa phosphotyrosine adapter protein) (pp36) (p36-38) (O43561)
Organism: Homo sapiens (Human)
Function: Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9489702, ECO:0000269|PubMed:9729044}; Single-pass type III membrane protein {ECO:0000269|PubMed:9489702, ECO:0000269|PubMed:9729044}. Note=Present in lipid rafts.
Interaction partners:
- Lymphocyte cytosolic protein 2
- Growth factor receptor-bound protein 2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- GRB2-related adapter protein 2
- Tyrosine-protein kinase ZAP-70
- Tyrosine-protein kinase Lck
- Proto-oncogene vav
- Tyrosine-protein kinase SYK
- Tyrosine-protein kinase ITK/TSK
- GRB2-related adapter protein
Sequence:
MEEAILVPCVLGLLLLPILAMLMALCVHCHRLPGSYDSTSSDSLYPRGIQFKRPHTVAPWPPAYPPVTSYPPLSQPDLLPIPRSPQPLGGSHRTPSSRRDSDGANSVASYENEGASGIRGAQAGWGVWGPSWTRLTPVSLPPEPACEDADEDEDDYHNPGYLVVLPDSTPATSTAAPSAPALSTPGIRDSAFSMESIDDYVNVPESGESAEASLDGSREYVNVSQELHPGAAKTEPAALSSQEAEEVEEEGAPDYENLQELN
Protein: Probable transcriptional regulator (Q9I516)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- DUF2024 family protein
Sequence:
MSAIALYDYLERLTSLMRAWSREQPLVAELQPVQLSALHYLARCNRYSDTPLGVTEYLGLTKGTVSQSLKVLEGRGLISKLPDARDRRSVHLRLTDAGRALIEAVIPPQFLEQAVTALGEKGEHLQGLLRDLLVVIQRQEDVPGFGLCRSCRFHQRRAGSPFCGLTGEPLSDADAELICREHQACG
Protein: Ribonuclease Y (RNase Y) (EC 3.1.-.-) (O31774)
Organism: Bacillus subtilis (strain 168)
Function: Endoribonuclease that initiates mRNA decay. Initiates the decay of all SAM-dependent riboswitches, such as yitJ riboswitch. Involved in processing of the gapA operon mRNA, it cleaves between cggR and gapA. Is also the decay-initiating endonuclease for rpsO mRNA. Involved in degradation of type I toxin-antitoxin system bsrG/SR4 RNAs and a minor role in degradation of type I toxin-antitoxin system bsrE/SR5 degradation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20572937}; Single-pass membrane protein {ECO:0000269|PubMed:20572937}. Note=Dispersed along membrane with a few foci at septation sites and cell poles; in the absence of dynA fewer foci are seen, in the absence of minJ no foci are seen. {ECO:0000269|PubMed:23060960}.
Interaction partners:
- Polyribonucleotide nucleotidyltransferase
- DEAD-box ATP-dependent RNA helicase CshA
- Ribonuclease J1
- Ribonuclease J2
- ATP-dependent 6-phosphofructokinase
- Stage 0 sporulation protein YaaT
- Ribonuclease 3
- Ribonuclease R
- 2',3'-cyclic-nucleotide 2'-phosphodiesterase
- 3'-5' exoribonuclease YhaM
Sequence:
MTPIMMVLISILLILLGLVVGYFVRKTIAEAKIAGARGAAEQILEDAKRDAEALKKEALLEAKDEIHKLRIDAEQEVRERRNELQKQENRLLQKEENLDRKHEGIDKREAMLEKKDHSLNERQQHIEEMESKVDEMIRMQQSELERISSLTRDEAKQIILERVENELSHDIAIMTKETENRAKEEADKKAKNILSLALQRCAADHVAETTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRRETARIALDKLVQDGRIHPARIEEMVEKSRREVDDYIREMGEQTTFEVGVHGLHPDLIKILGRLKFRTSYGQNVLKHSMEVAFLAGLMASELGEDAKLAKRAGLLHDIGKAIDHEVEGSHVEIGVELATKYKEHPVVINSIASHHGDEEPTSIIAVLVAAADALSAARPGARSETLENYIRRLEKLEEISESYEGVEKSFAIQAGREVRIMVKPDSINDLEAHRLARDIRKRIEDELDYPGHIKVTVIRETRAVEYAK
Protein: Myogenin (P20428)
Organism: Rattus norvegicus (Rat)
Function: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation, cell cycle exit and muscle atrophy. Essential for the development of functional embryonic skeletal fiber muscle differentiation. However is dispensable for postnatal skeletal muscle growth; phosphorylation by CAMK2G inhibits its transcriptional activity in respons to muscle activity. Required for the recruitment of the FACT complex to muscle-specific promoter regions, thus promoting gene expression initiation. During terminal myoblast differentiation, plays a role as a strong activator of transcription at loci with an open chromatin structure previously initiated by MYOD1. Together with MYF5 and MYOD1, co-occupies muscle-specific gene promoter core regions during myogenesis. Cooperates also with myocyte-specific enhancer factor MEF2D and BRG1-dependent recruitment of SWI/SNF chromatin-remodeling enzymes to alter chromatin structure at myogenic late gene promoters. Facilitates cell cycle exit during terminal muscle differentiation through the up-regulation of miR-20a expression, which in turn represses genes involved in cell cycle progression. Binds to the E-box containing (E1) promoter region of the miR-20a gene. Plays also a role in preventing reversal of muscle cell differentiation. Contributes to the atrophy-related gene expression in adult denervated muscles. Induces fibroblasts to differentiate into myoblasts.
Subcellular location: Nucleus. Note=Recruited to late myogenic gene promoter regulatory sequences with SMARCA4/BRG1/BAF190A and SWI/SNF chromatin-remodeling enzymes to promote chromatin-remodeling and transcription initiation in developing embryos. {ECO:0000250}.
Interaction partners:
- Paired box 7
- Transcription factor 12
- Transcription factor E2-alpha
- Myosin-4
- Myocyte-specific enhancer factor 2D
- Growth/differentiation factor 8
- Myocyte-specific enhancer factor 2C
- Myosin-3
- Paired box 3
- Myocyte-specific enhancer factor 2A
Sequence:
MELYETSPYFYQEPHFYDGENYLPVHLQGFEPPGYERTELSLSPEARGPLEEKGLGTPEHCPGQCLPWACKVCKRKSVSVDRRRAATLREKRRLKKVNEAFEALKRSTLLNPNQRLPKVEILRSAIQYIERLQALLSSLNQEERDLRYRGGGGPSRWYPVNATPTAPPAVRSGAMHWSLVPTQEIICSQLTLQVPTTCTPLRPSWTASRWRICLSPSQMKPCPTEIVCQAGCAWEPLSWCQTPPLLQQGPFKWGCPGAQKTALGCHKPDYPPSIHIRLTPSPAREFN
Protein: Mitogen-activated protein kinase kinase kinase 10 (EC 2.7.11.25) (Mixed lineage kinase 2) (xMLK2) (Q7T2V3)
Organism: Xenopus laevis (African clawed frog)
Function: Activates the JUN N-terminal pathway. Essential for pronephros and cement gland development.
Interaction partners:
Sequence:
MDGLPKDEAFLWQSSKDNKENGVWSDVQSYGVSNPLWMAVFDYEPTAEEELTLRRGDLVEILSKDSTVSGDEGWWTGKIKDKVGIFPSNYVVSDDKYTTLTGAPKQCPLPLEIEFDELNLDEIIGVGGFGKVYKGLWRDEEVAVKAVRHDPDEDINVTAENVRQEAKIFCMLCHPNIIALTGVCLKPPHLCLVMEYARGGPLHRALAGKKVPAHVLVNWAVQIAKGMTYLHNEAIVPIIHRDLGSSNILILEKAENDDLFNKTLNITDFGLAREWQKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFVRILEACWDPDPHSRPTFSCILEQLTTIEQSAMFQMPLESFHSLQEDWRLEIQQMFDELRTKEKELRSREEELVRAAEEQRILEDLLKRREQELAEREIDIVERELNIIMYQMYQEKPKVKKRKGNFKKSRLKLKDGNRISLPSGFEHKITVQASPMLDKCKGQGTSSYSPPGSPLIIPRLRAIRLTPVDGSKTWGRSSVLKKEEVTTSNKKKGRTWGPSSTQQKERVGGEERLKTLGEGNKQWSSSAPNLGKSPKHTPISVGFASLTEMEEYADSDGSVPQSPYSQSYLTLPVQSDHRSHPEDTAHAGAPSSDSPKRGSQSRRKSELVLLGCASLLAAVALGSDLSELVPQEEKRKGIFQWAGRGPRRRASSPSRSMSYGEDSVIPSSSVTLISLSSISDCNSTRSLIRSDSDDIGLDHDNVSSGRGVKEDRGQQPNVGSNPLVDYKVESFKRDPKQSLTPTHVTVGRNNTTETRGHRRTPSDGAIRQVTQGHKRSPSDGSTPYQCEPEPSPFPRLPDPHFVFPPPVRRKDTGVERPTSLEFAPRPRPSSNRPRMDPWKFVSLSQTHSSSPSSGGGDACSSGSAEGAQVADVEETLLDMEVEGQRLDSTVPLCGLGLRPTTDPFFKYGNRRVLMKELSISLLQYKVESGVLL
Protein: Probable Xaa-Pro aminopeptidase pepP (EC 3.4.11.9) (Aminoacylproline aminopeptidase) (Prolidase) (Q96WX8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Interaction partners:
- Probable Xaa-Pro aminopeptidase P
- Multifunctional tryptophan biosynthesis protein
Sequence:
MTSLDSILADKYPAKAHARRVAEGLKALGHSGGAIYLEAQKTRLIEDNDEPVPFRQRRPFFYLSGCLLPDSSLVYNIDSDQLTLFIPPINPDDVIWSGLPLSAAEALERYDVDNVLETTEVNATLANIAASHANNSTAFAIAEQVSEGTKFEGFSETNFNVLKGVIERTRVVKDSYEIALLRKANDISAKGHIAAIKASKSATNEREIEAAFIATCIANGAREQSYHPIVACGQNGATLHYGKNDEDLIDPVTNRRKDNVLIDAGAEYRTYCADITRAFPLNGKFLPETRQIYEIVLRMQLECIDMLKEGVQWEDVHAHAHRVAIRGLLELGILRGSEDELFDKRISVAFFPHGLGHYLGMDTHDTGGNPNYEDTDTMFRYLRVRGRLPAGSVITVEPGIYFCRFIIEPFLKNPDLQKYIDVGTLNRYWRVGGVRIEDNVHITKDGHDNLTTAPKTIEEVESLAA
Protein: ATP synthase subunit beta, chloroplastic (EC 7.1.2.2) (ATP synthase F1 sector subunit beta) (F-ATPase subunit beta) (Q6ENG7)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
Interaction partners:
- ATP synthase subunit a, chloroplastic
- ATP synthase epsilon chain, chloroplastic
- Uncharacterized protein
- ATP synthase subunit alpha
- ATP synthase subunit alpha, chloroplastic
- ATP synthase subunit alpha
- ATP synthase subunit b, chloroplastic
- ATP synthase CF0 subunit I
- ATP synthase subunit gamma, mitochondrial
- ATPase F1/V1/A1 complex alpha/beta subunit N-terminal domain-containing protein
Sequence:
MRTNPTTSRPGVSTIEEKSTGRIDQIIGPVLDVTFPPGKLPYIYNALVVKSRDTDGKQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTSATFPIHRSAPAFIELDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEKNLEESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLASKGIYPAVDPLDSTSTMLQPRIVGNEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEASTKAINLEEENKLKK
Protein: Odorant-binding protein 19b (Q9VR95)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- General odorant-binding protein 19d
- General odorant-binding protein 57b
- GH25962p
- Chemosensory protein A 87a
- General odorant-binding protein 19a
- Odorant-binding protein 56g
- General odorant-binding protein 57c
- Chemosensory protein A 7a
- General odorant-binding protein 83a
Sequence:
MMQCSRMTTTLKMTNLLLAVACAAVLMGSATADEEEGSMTVDEVVELIEPFGDACTPKPSRENIVEMVLNKEDAKHETKCFRHCMLEQFELMPEDQLQYNEDKTVDMINMMFPDREDDGRRIVKTCNEELKAEQDKCEAAHGIAMCMLREMRSSGFKIPEIKE
Protein: Vitelline membrane protein Vm32E (Q9VKI3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Major early eggshell protein.
Subcellular location: Secreted {ECO:0000269|PubMed:2495206}.
Interaction partners:
- Vitelline membrane protein Vm34Ca
- Defective chorion protein, FC177 isoform
- IP19021p
- Chorion protein S36
- Chorion protein S19
- Vitelline membrane protein Vm26Aa
- Chorion protein c at 7F
- Chorion protein b at 7F, isoform A
- Chorion protein S16
- Chorion protein S38
Sequence:
MQIVALTLVAFVAIAGASCPYAAPAPAYSAPAASSGYPAPPCPTNYLFSCQPNLAPAPCAQEAPAYGSAGAYTEQVPHYVGSPNREQLQQFHQRIGMAALMEELRGLGQGIQGQQY
Protein: ARGONAUTE 1 (D6RUV9)
Organism: Nicotiana tabacum (Common tobacco)
Interaction partners:
Sequence:
MVRKKRTDVPGGAESFESHETGGGRGGAQRPSQQQQHQHQHQQGGGRGWAPQHGGHGGRGGGGAPRGGMGPQQSYGGPPEYYQQGRGTQQYQRGGGQPQRRGGMGGRGAPSGPPRSPVPELHQATQTPHQPVPYGRPSETYSEAGSSSQPPEPTTQQVTQQFQQLVVLPEAAATQAIQPASSKSMRFPLRPGKGSTGIRCIVKANHFFAELPDKDLHQYDVSITPVVSSRGVNRAVMEQLVKLYRESHLGKRLPAYDGRKSLYTAGPLPFVQKDFKITLIDDDDGPGGASCRREREFKVVIKLAARADLHHLGMFLQGRQADAPQEALQVLDIVLRELPTSRYCPVGRSFYSPHLGRRQPLGEGLESWRGFYQSIRPTQMGLSLNIDMSSTAFIEPLPIIDFVSQLLNRDISSRPLSDADRVKIKKALRGVKVEVTHRGNMRRKYRISGLTSQATRELTFPVDERGTMKAVVEYFRETYGFVIRHTQLPCLQVGNTQRPNYLPMEVCKIVEGQRYSKRLNERQITALLKVTCQRPQEREHDILQTVHHNAYADDPYAKEFGIKISEKLAQVEARVLPAPWLKYHDTGREKDCLPQVGQWNMMNKKMVNGGTVNNWICVNFSRNVQDTVARGFCSELAQMCMISGMNFNPNPVLPPVSARPDQVERVLKTRFHDAMTNLQPHGRELDLLIVILPDNNGSLYGDLKRICETELGIVSQCCLTKHVFKMSKQYLANVSLKINVKVGGRNTVLVDALSRRIPLVSDRPTIIFGADVTHPHPGEDSSPSIAAVVASQDWPEITKYAGLVSAQAHRQELIQDLYKTWQDPVRGPVTGGMIKELLISFRRATGQKPQRIIFYRDGVSEGQFYQVLLFELDAIRKACASLEPNYQPPVTFVVVQKRHHTRLFANNHRDRNAVDRSGNILPGTVVDSKICHPTEFDFYLCSHAGIQGTSRPAHYHVLWDENNFTADALQSLTNNLCYTYARCTRSVSIVPPAYYAHLAAFRARFYMEPETSDSGSVTSAAASNRGGVGAMGRSTRAPGAGAAVRPLPALKENVKRVMFYC
Protein: Alpha-glucosidase (EC 3.2.1.20) (Maltase) (Q9P6J3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized family 31 glucosidase C30D11.01c
- Alpha-glucosidase
- Invertase
- Putative amidase PB8B6.03
- Uncharacterized family 31 glucosidase C1039.11c
- Hexokinase-1
- Hexokinase-2
- Putative invertase
- Glucan 1,3-beta-glucosidase 2
- Glucan 1,3-beta-glucosidase 1
Sequence:
MKVVPSEKIKPNWWRETSVYQIYPASFKDSNGDGFGDLEGIISKVDYLKALNVESIWLCPIYPSPLKDMGYDVSDYKQIDSRYGTLEDLDRLMKALHERDMKLVMDLVLNHTSDQHEWFKESRSSKTNPKRDWYFWKPARYNEKGERLPPNNWRSYFDTSAWEWDEATQEYYLHLWSVGQPDLNWETPKVREAVHDILRFWLDRGVDGFRLDAINMISKDQRFLDAPITDDRYEYQLAYQYYANGPRIHEYLNGIGNILTEYDAFSVGEMPYVLDTNEILHVVGADRRELTMIFQFDFVDLDLDPNQHKYIEGSWELSDLKKSLKKWQSALLSGGGWNASFIENHDQTRTVSRYLSDSPKYRAYSSKLMALFIIFQSGTPFVFQGQELALANIPRDWPIDEYLDVETQNFWKLFMSGNPSQEEIEKTMDIVNKRARDNGRTPMHWDSSPNGGFTKAGVKPWMRVTNDYKEWNAANQVNDPESPYTFWSKALELRKELKDAVVYGSFELISEEDPSIVAFVRESSTYKLIILLNFTGNKVSYDCPLNLTSYEILLDNYKDFICMTSPVTLNPYQAVLLKL
Protein: Thyroid hormone receptor alpha (Nuclear receptor subfamily 1 group A member 1) (c-erbA-1) (c-erbA-alpha) (P63058)
Organism: Mus musculus (Mouse)
Function: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. Isoform Alpha-deltaE6 does not bind DNA, inhibits the activity of isoform Alpha-1, and stimulates myoblast differentiation.
Subcellular location: Nucleus.; SUBCELLULAR LOCATION: [Isoform Alpha-deltaE6]: Cytoplasm. Note=Sequesters isoform Alpha-1 into this compartment.; SUBCELLULAR LOCATION: [Isoform Alpha-2]: Cytoplasm {ECO:0000269|PubMed:20078863}. Nucleus {ECO:0000269|PubMed:20078863}. Note=When overexpressed found in the cytoplasm where it colocalizes with TACC1. {ECO:0000269|PubMed:20078863}.
Interaction partners:
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Nuclear receptor corepressor 1
- Retinoic acid receptor RXR-alpha
- Actin, cytoplasmic 1
- Mediator of RNA polymerase II transcription subunit 1
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Thyroid hormone receptor beta
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Nuclear receptor coactivator 1
- Phosphatidylinositol 3-kinase regulatory subunit gamma
Sequence:
MEQKPSKVECGSDPEENSARSPDGKRKRKNGQCPLKSSMSGYIPSYLDKDEQCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPTYSCKYDSCCVIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEQNRERRRKEEMIRSLQQRPEPTPEEWDLIHVATEAHRSTNAQGSHWKQRRKFLPDDIGQSPIVSMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESDTLTLSGEMAVKREQLKNGGLGVVSDAIFELGKSLSAFNLDDTEVALLQAVLLMSTDRSGLLCVDKIEKSQEAYLLAFEHYVNHRKHNIPHFWPKLLMKEREVQSSILYKGAAAEGRPGGSLGVHPEGQQLLGMHVVQGPQVRQLEQQLGEAGSLRGPVLQHQSPKSPQQRLLELLHRSGILHSRAVCGEDDSSEASSLSSSSDTEDTEVCEDQAGKAASP
Protein: Serine protease EspP (EC 3.4.21.-) [Cleaved into: Secreted autotransporter protein EspP (Extracellular serine protease plasmid-encoded EspP); Autotransporter protein EspP translocator] (Q7BSW5)
Organism: Escherichia coli O157:H7
Function: Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis.
Subcellular location: [Serine protease EspP]: Periplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Secreted autotransporter protein EspP]: Secreted. Cell surface.; SUBCELLULAR LOCATION: [Autotransporter protein EspP translocator]: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane. {ECO:0000250}.
Interaction partners:
- Chaperone SurA
- Periplasmic serine endoprotease DegP
- Outer membrane protein assembly factor BamA
- Chaperone protein Skp
- Adhesin
- Intimin
- Serine protease
- T3SS secreted effector NleA/EspI
- Catalase-peroxidase 1
- Translocated intimin receptor Tir
Sequence:
MNKIYSLKYSHITGGLIAVSELSGRVSSRATGKKKHKRILALCFLGLLQSSYSFASQMDISNFYIRDYMDFAQNKGIFQAGATNIEIVKKDGSTLKLPEVPFPDFSPVANKGSTTSIGGAYSITATHNTKNHHSVATQNWGNSTYKQTDWNTSHPDFAVSRLDKFVVETRGATEGADISLSKQQALERYGVNYKGEKKLIAFRAGSGVVSVKKNGRITPFNEVSYKPEMLNGSFVHIDDWSGWLILTNNQFDEFNNIASQGDSGSALFVYDNQKKKWVVAGTVWGIYNYANGKNHAAYSKWNQTTIDNLKNKYSYNVDMSGAQVATIENGKLTGTGSDTTDIKNKDLIFTGGGDILLKSSFDNGAGGLVFNDKKTYRVNGDDFTFKGAGVDTRNGSTVEWNIRYDNKDNLHKIGDGTLDVRKTQNTNLKTGEGLVILGAEKTFNNIYITSGDGTVRLNAENALSGGEYNGIFFAKNGGTLDLNGYNQSFNKIAATDSGAVITNTSTKKSILSLNNTADYIYHGNINGNLDVLQHHETKKENRRLILDGGVDTTNDISLRNTQLSMQGHATEHAIYRDGAFSCSLPAPMRFLCGSDYVAGMQNTEADAVKQNGNAYKTNNAVSDLSQPDWETGTFRFGTLHLENSDFSVGRNANVIGDIQASKSNITIGDTTAYIDLHAGKNITGDGFGFRQNIVRGNSQGETLFTGGITAEDSTIVIKDKAKALFSNYVYLLNTKATIENGADVTTQSGMFSTSDISISGNLSMTGNPDKDNKFEPSIYLNDASYLLTDDSARLVAKNKASVVGDIHSTKSASIMFGHDESDLSQLSDRTSKGLALGLLGGFDVSYRGSVNAPSASATMNNTWWQLTGDSALKTLKSTNSMVYFTDSANNKKFHTLTVDELATSNSAYAMRTNLSESDKLEVKKHLSGENNILLVDFLQKPTPEKQLNIELVSAPKDTNENVFKASKQTIGFSDVTPVITTRETDDKITWSLTGYNTVANKEATRNAAALFSVDYKAFLNEVNNLNKRMGDLRDINGEAGAWARIMSGTGSASGGFSDNYTHVQVGVDKKHELDGLDLFTGFTVTHTDSSASADVFSGKTKSVGAGLYASAMFDSGAYIDLIGKYVHHDNEYTATFAGLGTRDYSTHSWYAGAEAGYRYHVTEDAWIEPQAELVYGSVSGKQFAWKDQGMHLSMKDKDYNPLIGRTGVDVGKSFSGKDWKVTARAGLGYQFDLLANGETVLRDASGEKRIKGEKDSRMLMSVGLNAEIRDNVRFGLEFEKSAFGKYNVDNAVNANFRYSF
Protein: DENN domain-containing protein 3 (A2RUS2)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) activating RAB12. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB12 into its active GTP-bound form. Regulates autophagy in response to starvation through RAB12 activation. Starvation leads to ULK1/2-dependent phosphorylation of Ser-472 and Ser-490, which in turn allows recruitment of 14-3-3 adapter proteins and leads to up-regulation of GEF activity towards RAB12 (By similarity). Also plays a role in protein transport from recycling endosomes to lysosomes, regulating, for instance, the degradation of the transferrin receptor and of the amino acid transporter PAT4. Starvation also induces phosphorylation at Tyr-858, which leads to up-regulated GEF activity and initiates autophagy (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A2RT67}. Note=Transiently recruited to membranes to activate RAB12. {ECO:0000250|UniProtKB:A2RT67}.
Interaction partners:
- Ras-related protein Rab-12
- Serine/threonine-protein kinase ULK1
- BOS complex subunit NCLN
Sequence:
MRSLRKKREKPRPEQWKGLPGPPRAPEPEDVAVPGGVDLLTLPQLCFPGGVCVATEPKEDCVHFLVLTDVCGNRTYGVVAQYYRPLHDEYCFYNGKTHRECPGCFVPFAVCVVSRFPYYNSLKDCLSCLLALLKPCKDFEVDSHIKDFAAKLSLIPSPPPGPLHLVFNMKSLQIVLPARADPESPILDLDLHLPLLCFRPEKVLQILTCILTEQRIVFFSSDWALLTLVTECFMAYLYPLQWQHPFVPILSDQMLDFVMAPTSFLMGCHLDHFEEVSKEADGLVLINIDHGSITYSKSTDDNVDIPDVPLLAAQTFIQRVQSLQLHHELHAAHLLSSTDLKEGRAHRRSWQQKLNCQIQQTTLQLLVSIFRDVKNHLNYEHRVFNSEEFLKTRAPGDHQFYKQVLDTYMFHSFLKARLNRRMDAFAQMDLDTQSEEDRINGMLLSPRRPTVEKRASRKSSHLHVTHRRMVVSMPNLQDIAMPELAPRNSSLRLTDTAGCRGSSAVLNVTPKSPYTFKIPEIHFPLESKCVQAYHAHFVSMLSEAMCFLAPDNSLLLARYLYLRGLVYLMQGQLLNALLDFQNLYKTDIRIFPTDLVKRTVESMSAPEWEGAEQAPELMRLISEILDKPHEASKLDDHVKKFKLPKKHMQLGDFMKRVQESGIVKDASIIHRLFEALTVGQEKQIDPETFKDFYNCWKETEAEAQEVSLPWLVMEHLDKNECVCKLSSSVKTNLGVGKIAMTQKRLFLLTEGRPGYLEISTFRNIEEVRRTTTTFLLRRIPTLKIRVASKKEVFEANLKTECDLWHLMVKEMWAGKKLADDHKDPHYVQQALTNVLLMDAVVGTLQSPGAIYAASKLSYFDKMSNEMPMTLPETTLETLKHKINPSAGEAFPQAVDVLLYTPGHLDPAEKVEDAHPKLWCALSEGKVTVFNASSWTIHQHSFKVGTAKVNCMVMADQNQVWVGSEDSVIYIINVHSMSCNKQLTAHCSSVTDLIVQDGQEAPSNVYSCSMDGMVLVWNVSTLQVTSRFQLPRGGLTSIRLHGGRLWCCTGNSIMVMKMNGSLHQELKIEENFKDTSTSFLAFQLLPEEEQLWAACAGRSEVYIWSLKDLAQPPQRVPLEDCSEINCMIRVKKQVWVGSRGLGQGTPKGKIYVIDAERKTVEKELVAHMDTVRTLCSAEDRYVLSGSGREEGKVAIWKGE
Protein: G-protein coupled receptor 15 (Q0VDU3)
Organism: Mus musculus (Mouse)
Function: Probable chemokine receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Protein GPR15LG
Sequence:
MEPATALLIVDYYDYTSPDPPFLETPSHLSYTSVFLPIFYTVVFLTGVVGNFILMIALHFKRGNRRLIDIFIINLAASDFIFLVTVPLWMDKEASLGLWRTGSFLCKGSSYVISVNMHCSVFLLTCMSMDRYLAIMHPALAKRLRRRSSAYAVCAVVWIISCVLGLPTLLSRELTHIEGKPYCAEKKPTSLKLMWGLVALITTFFVPLLSIVTCYCCITRRLCAHYQQSGKHNKKLKKSIKIVIIAVAAFTVSWVPFNTFKLLAIVSGFQPEGLFHSEALQLAMNVTGPLAFASSCVNPLIYYVFDSYIRRAIVRCLCPCLKTHNFGSSTETSDSHLTKALSNFIHAEDFIRRRKRSVSL