wanglab/gogpt-training-data huggingface dataset:
Protein: LD27161p (Q8MRI5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNKIASNKSLIKTNYNDVKSKVSTTRIMTPASGSSPVSGSGSGSVSRTASSPRASPSVSASARRSPSATPKVPPKMLLAKRPSSSSGKVNATPSPPPHATPPTRQPLDKGSVGAGSVGGGGARAVKTPKSPTSPTTPTTPTSPPAKRLQTSLVSRGRSYSKDSHKSSHTDLSLMCNASSSRPSNSASGSGSPKLLANTQLRAAKKRDVRNLSISPTDLGPPPKTQQTTKGQSTRSKSSATPTPTPTSIHKRLNGTLASTAAIATPIKGVATKSGATNKLQQSAKTKSTASIKSPAIVGVSEESLRSGVDQTELQELNNGQSATGCPTPPMARDSKRTSIGNELPCETEAKLKRCEDQQDPQASTTASPLPMINPQEQEASGQVKEATITTANEPNALSLPDEISNSVSSTTMLATPRVDIAAQYPVLKPFTENGELDCARLAKFFQDTQFERKEEQRQILGLSVMVQFMSKELDAVACKENKHQCARTKGTLEKTILLLQHTQKDCERLREDLEDKGLEWIQRQQEKEYLHRTELKQAEEKLMEVQLRAKLKFCELESQLRAKDEESKQAQEAYRMEVSHKLALKQEHLRTAEQKIQELQTRLQQVETEEQGHREELIRKENIHTARLAEANQREQDLIDRVKSLTKELNTLKANKEHNERDLRDRLALSQDEISVLRTSSQRRSPCTSLPDNASAELNRLTSEADSLRCVLELKQAEISALSKAKADLIHESEERLKLSNRVALLEAQNEMLRTELEAKTEKEKEIQQKMEELQKAYKYESIKRTRLTYDKEELQYHLKQRSLQLQSAESKLQDLSTGSHDNSLSSHSRCSLGRSGLEIAVTTSSPTSPVMKGMIERNDSVSWTLEIEDESFKGNTSKIVRRAGSLRSNNERCPIQRRQTLTSNGHSNGSATNGGSSPAHPNPLSQSMSATALLRSSSNSGESEGRPLSRARSKSMCIKASATSSAVCESSGQRKKPQDELSLADWPEDIPLCSSSPQAPGIEMRPRSSTMKLMSSEAKKFQEIQESAGEAMVSGANSEDESCSASSEDIMRSSSASSTASGGSLSKRPKQPPSRMSIEEALPCTPMEVSWSEDAADANGLA
Protein: Opt7p (A0A1D8PL16)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSKEAEFVKTISKEGDPQVDVLERDAESNSENALEPDVEELPKVVREIVPLEDDPTIPVLTFRYFILSIIFIIPGAFIDTMNSFRTTSAAYSIFFVQIASHWCGKWLARILPKKQVGFGRLSFNLNPGPWSIKETALITITANSGATGSMGTNPLALAELFYGETVNPAVAIFFMWMIVFIGYSFAGIARNFLLYDPQFTWPQALMQTTLFQTQSKSDKDAKQASKQMKVFFFVLIGLCIWQFFPEYIFPMTSSLAFLCWVAPENYTANFIGSGLGGMGFLNLSLDWSNITSSIMLYPYWVQVVQFAAFVLGAWILIPAAKWGDLSSYPYGLMSNSLFLGNGTKYPTTELLTPNLRLNETRYEELGPVHLGAQRAWNMFFDYAAYVSGFMWVVAFGYKSLSGSLKRLVKSRKQKGSINLQYTDRLNKLQAAYEEVPLYWYAILFLCAFVTLLVIFATNSLFMPWWCLLVGVAFGAVIVTPLVWLYALSNFQLPIGTFNELLYGYMIQNKTSRHPAGAMVYGAVGGDLFYRAQYILNDQKIAHYMHISQRAVFFSQIFGELIGVPINYAALRWVISSKRDFLDGTKVDKLHQWTGQTIVSYNTNAVQYVILGPDRLFKNYPVLPYGFLLGAGALLVLYLLHRLFPKSKLKFHLWNTTVFFSTMSTFYGNLSTGYFSRFIGGTITMFWAFRYKHSLWKKYNYLLAAALDTGLNLSILLIFLFFSAGKTVNFPEWWGNNGKSVERCFAMS
Protein: Reduction in Cnn dots 1, isoform F (EC 3.-.-.-) (A0A0B4KFX4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSFFDCFNDFLQSGGNLVQNVSQEQEQKIADQELDGVIELMPPTTPTPSESSSTISAPSESSFSEKMEHSYMRDTPVRSDVHNGLTPARNILVRHPPQCPSCHTYPPQHEELSEIQQAHVPPYDEVVAKEAMNECARIAKYVKNNNSDEQDWVARVNKFNWTPMQEMVFEKVCSILDQDQLARLANDKRQHEPIHRRISSDKSASRFRKLLASVAWESRITQWIHALLMEHLSPSYMASYLEILQTLKTKLPTLVDKMLFGRPLNNSQELLAPVMKKRWEPNIMPKSRQLTHNAIMVVLPNMPTTGTVSDRMQKWYQALSTITQVVQISLPNTNNRIGNQNLDHVAETIVSITRVKINELRTENPSRGIILVGFNAGAALALQVALSESVACVVCMGFAYNTIRGPRGTPDDRMLDIKAPILFVIGQNSARTSQEEMEGLRERMQSESSLVVVGSADDALRVPKSKRRIEGVTQSMVDYMVVEEIFEFVNRTLSNPPGPRMPTCLMHQQGYQRLPKQSPHILADGNANKAVQQMRKRKMDGGLDDSMGQPSKTKFVPHIGRPRTRPLPNVGGSARSVSQKGAPHPDQPKLSGEEPNQSIEFILDDAQDYGDAQTTAGGSASLPKVITPGVLGKQLPPVNLAAGTKIKMIPSSQFVQIKSLPSQSKLINYTLNKPSVGTSSTANIGSVVKTLPCSSVSGQQIITLKTPSGQTQQFATAATSTGAAGSSTSTGTGQKKYTVFKNANGMTMLHLTKSVPTTGSSSGSANMDLSNIIDMPIVFADNEGNIPEHQQADKDIKPAPIRSANKSPLIISQKIIKEANKPSGMVTSGSITAVSKPGNIVLNKGLQQLLNSSPGGTLATQNKVVYLNRSTIKPMGNVAPGTHRVPIRIVSTPNTGGAVTTTASSSPIMVDPATGSKVAKTVNVQTIKPTGSVLAQGTIRQAGNVGTKSYLQMINTAPGASKTVAGDGKGSVRNIYFKSATGLKQLPVQMLGNRIPGGAVISSTASASSGSPGLRRVVNIGPVSKVTATSTTSSSIAATLTHNKM
Protein: Protein DMP8 (AtDMP8) (O80493)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in membrane remodeling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20712629}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:20712629}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein GAMETE EXPRESSED 2
- Protein HAPLESS 2
Sequence:
MEKTEESVGIRVYTTTTTQNPSPTSSRSPKPVPLSSLPMLPAGAAAGGGKGRKRRMVAKGVQKTVSKTSMLVNFLPTGTLLMFEMVLPTIYRDGDCNGINTLMIHLLLLLCAMSCFFFHFTDSFKASDGKIYYGFVTPRGLAVFMKPPSPGFGGGDVIAEKEIPVTDERYKLRVNDFVHSVMSVLVFMAIAFSDRRVTGCLFPGKEKEMDQVMESFPLMVGIVCSALFLVFPTSRYGVGCMST
Protein: Candida glabrata strain CBS138 chromosome C complete sequence (Q6FWW1)
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 J complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- 1-phosphatidylinositol 4-kinase
- Rab GDP dissociation inhibitor
- Exocyst complex component SEC15
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome C complete sequence
Sequence:
MSNEDYGYDYDYLFKIVLIGDSGVGKSNLLSRFTTNEFNIDSKSTIGVEFATRTIDVDGKKIKAQIWDTAGQERYRAITSAYYRGAVGALIVYDISKSSSYENCHHWLSELRENADDNVAVGLIGNKSDLAHLRAVPTEEAKQFASENQLLFTETSALNSDNVDLAFKELITAIHQKVSKHQVELSNANKPGAGPNGPTISLTPAPNEKKKSSSNNCC
Protein: Catalase A (EC 1.11.1.6) (O52762)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Interaction partners:
- Catalase HPII
- Glycolate oxidase subunit GlcE
- Glycolate oxidase subunit GlcD
- Catalase
- Kynureninase
- Glycolate oxidase iron-sulfur subunit
Sequence:
MEEKTRLTTAAGAPVVDNQNVQTAGPRGPMLLQDVWFLEKLAHFDREVIPERRMHAKGSAAYGTFTVTHDITPYTRAKIFSQVGKKTDMFLRFSTVAGERGAADAERDIRGFSMRFYTEQGNWDLVGNNTPVFYLRDPLKFPDLNHVVKRDPRTNLRNATFKWDFFSHLPESLHQLTIDFSDRGLPKSYRHIHGFGSHTFSFINANNERFWVKFHFKTQQGIENLTNAEAAEVIAQDRESSQRDLYESIEKGDFPRWKMYVQIMPEKEAATYRYNPFDLTKVWPHGDYPLIEVGFFELNRNPDNYFAEVEQAAFTPANVVPGIGFSPDKMLQGRLFSYGDAHRYRLGVNHHQIPVNAARCPHQVYHRDGGMRVDGNNAHQRVTYEPNSFNQWQEQPDFSEPPLSLEGAADHWNHRVDDDYYSQPAALFHLFTDEQKQRLFANIAEDIRDVPEQIQRRQIGLFLKVDPAYGKGVADALGLKLD
Protein: Calponin homology and LIM domain-containing protein (CH-LIM) (Q55GV9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in the regulation of phagocytosis. May repress rab21.
Interaction partners:
- Protein VASP homolog
- LIM domain-containing protein F
- Ras-related protein Rab-21
Sequence:
MIKANWTSTSAFNLELALDESRDWIERVINQKFPSDFQSSLRDGIFLCKLINQIQPNSVPKYNQSPSTDFAKRENIQLFIKSAKHSMGLRDTQLFESQDLFESIRIRNIAITLYWLGRAARASQTYKGPQLDLLKFQGMNCSACKKAITNNDYLTTMTQQFHTSCAVCCSCSCKLDPKKKFYQESNNFWCENCMLGATNLGGSNNSSGGKNKSNNNNNNKCSGCFGSLEKGYVPDENDKEKKYCTSCICDLCHDPLIGNFQVKDGKKVCDSCSCKSCGKSLEDGYYEEGISKYCEPCAKDRNKPKQVMDKDGHDHHHHNHNKPTTTTTTTNSNSPLAKKKSDSCKMCDKPVDNKTKKYGDDRDKYCTPHEKDGTCGKCNGELVGSAISVMDKNFHPQCFKCDSCNKNLNQNDQIKKSPTTGNPLCGPCSSNNNKSSKNCHDCKKPISGSSVEALDRPYHPNCLKCYSCSKNLKEDFTEVDNEPFCNPCASQLNQYTSGNQKQPKQGGSPFITSGWLDSDRCVVCVKPLNGEVAKIFDSFYHKGCFKCTDKSCNAPLLTGYFPHDKKPYCQKCSIKIQQSTTTDHCAKCSKPIIEGSILKVAGKVYHKSCYDNEKHTSSSSSSSSVNCFKCKSQITGTQFVRLDQKDYCMKCSPSASSSTTVTHGERLNYGMTVDPRSGKRVFNTSK
Protein: Tektin bundle-interacting protein 1 (Uncharacterized protein C19orf71 homolog) (Q2M2T2)
Organism: Bos taurus (Bovine)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. Located at the center of the tektin bundle where may function to recruit tektins or stabilize the bundle.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A6H6Q4}.
Interaction partners:
- EF-hand domain-containing family member C2
- Calaxin
- Outer dynein arm-docking complex subunit 4
- Outer dynein arm-docking complex subunit 1
- Tektin-3
- Outer dynein arm-docking complex subunit 2
- EF-hand calcium binding domain 6
- EF-hand calcium binding domain 6
- EF-hand domain-containing protein 1
- Piercer of microtubule wall 1 protein
Sequence:
MQTLRRQAAWPCVPRGTLEVDFPPPLYSDDYLSQEGPRWTPAIKQATRWKYTPMGRDAAGQLWYTGLTNSDSREAWYTLPRAPDSPYREAYARWHGCYGHRERSLPSAYTQRLRETAWYDPIIPAQYTDPSTRWGSVLWKDRPIRGKEFAINRHRFGVEALWRASDYVRYLSAPQRPRYTAQNYRQWGLEPYCPATNQRPPPVYTPSH
Protein: Type IV pilus biogenesis factor PilY1 (Pilus-associated adhesin PilY) (S0HPF7)
Organism: Pseudomonas aeruginosa (strain PAK)
Function: Involved in pilus assembly, twitching motility and adhesion to host cells. Primes type IV pili (T4P) assembly and is required for inclusion of minor pilins PilV, PilW and PilX to the surface pili (By similarity). Stabilizes assembled pilus fibers likely by antagonizing retraction mediated by PilT. Calcium-binding and calcium release by PilY1 seem to be essential for twitching motility and for regulation of pilus retraction dynamics of PilT. Adhesin for human tissue specifically recognizing a host receptor localized or enriched on basolateral epithelial cell surfaces. Binds host integrins in an calcium-dependent manner in vitro and this interaction may be employed by the bacterium to mediate host epithelial cell binding in vivo.
Subcellular location: Fimbrium {ECO:0000269|PubMed:20080557}. Membrane {ECO:0000269|PubMed:8899718}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q02GC2}. Note=Colocalizes with the T4P fraction when surface pili are present (PubMed:20331639, PubMed:8899718). Sheared surface fraction when PilV, PilW and PilX are also present (By similarity). {ECO:0000250|UniProtKB:Q9HVM8, ECO:0000269|PubMed:20331639, ECO:0000269|PubMed:8899718}.
Interaction partners:
Sequence:
MKSALHQIGKTSLAAALSGAVLLSAQTTHAAALSVSQQPLMLIQGVAPNMLVTLDDSGSMAYAYAPDSLVNSRNNVYFASNSYNPMYFDPNTQYKLPKKVTLSNGQIQVQDYSKPSFTAAWRNGFTQEGRVNLSRDYRPTVQYQGGSGAGTESSIDWYGAPAFYYQYSGGRGCSLTTSSCYTRVEISGAAQQQNFANWYSFYRTRALATQTAANLAFYSLPENARISWQLLNSSSCLIGSGSSNCYNNYLRDFTGQHRVNFFNWLENLSVGGGTPLRQAMTRAGEFLKKTGVNGPYAYRPGTQTSPEYSCRGSYHILMTDGLWNNDSASVGNADSTSRSLPDGKSYSSQTPYRDAASNTLADQAFHYWATDARPDIDDNIKPYIPYPDQANPSAEYWNPRNDPATWQHMVTYTLGLGLTTSLTSPKWEGSTYSGGYDEIAAGRLSWPNASNNHSNNVYDLWHAAVNSRGEFFSADSPDQLVAAFQDILNRISGKDLPASRPAISSSLQEDDTGDKLTRFAYQTSFASDKNWAGDLTRYSLTTQDKATVQTKLWSAQSILDAMPNGGAGRKIMMAGSGTSGLKEFTWGSLSADQQRQLNRDPDRNDVADTKGQDRVAFLRGDRSKENSDNFRTRNSILGDIINSSPATVGKAQYLTYLAQPIEPSGNYSTFAEAQKTRAPRVYVGANDGMLHGFDTDGNETFAFIPSAVFEKLHKLTARGYQGGAHQFYVDGSPVVADAFFGGAWHTVLIGSLRAGGKGLFALDVTDPANIKLLWEIGVDQEPDLGYSFPKPTVARLHNGKWAVVTGNGYSSLNDKAALLIIDLETGAITRKLEVTGRTGVPNGLSSPRLADNNSDGVADYAYAGDLQGNLWRFDLIAGKVNQDDPFSRANDGPAVASSFRVSFGGQPLYSAVDSAGAAQAITAAPSLVRHPTRKGYIVIFGTGKYFENADARADTSRAQTLYGIWDQQTKGEAAGSTPRLTRGNLQQQTLDLQADSTFASTARTIRIASQNPVNWLNNDGSTKQSGWYLDFMVNGTLKGEMLIEDMIAIGQVVLLQTITPNDDPCADGASNWTYGLDPYTGGRTSFTVFDLARQGVVDSKSDYSYNKQNVAVSGTEQKGLGGLTLSTNEQGNPEVCSSGECLTVNPGPNTRGRQNWRPIEGKN
Protein: Rac family small GTPase 2 (A0A8I6A1P8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MCGSHLWLRLTLQRVEHTGMKCLRLGDWTVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLRDDKDTIEKLKEKKLAPITYPQGLALAKDIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQPTRQQKRPCSLL
Protein: Ankyrin repeat and SOCS box protein 1 (ASB-1) (Q9Y576)
Organism: Homo sapiens (Human)
Function: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Mediates Notch-induced ubiquitination and degradation of TCF3/E2A and JAK2. May play a role in testis development (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:33431678}.
Interaction partners:
- Cullin-5
- Elongin-B
- RING-box protein 2
- Elongin-C
- TRAF3-interacting protein 1
- Cytokine-inducible SH2-containing protein
Sequence:
MAEGGSPDGRAGPGSAGRNLKEWLREQFCDHPLEHCEDTRLHDAAYVGDLQTLRSLLQEESYRSRINEKSVWCCGWLPCTPLRIAATAGHGSCVDFLIRKGAEVDLVDVKGQTALYVAVVNGHLESTQILLEAGADPNGSRHHRSTPVYHASRVGRADILKALIRYGADVDVNHHLTPDVQPRFSRRLTSLVVCPLYISAAYHNLQCFRLLLLAGANPDFNCNGPVNTQGFYRGSPGCVMDAVLRHGCEAAFVSLLVEFGANLNLVKWESLGPESRGRRKVDPEALQVFKEARSVPRTLLCLCRVAVRRALGKHRLHLIPSLPLPDPIKKFLLHE
Protein: DNA repair protein rlp1 (RecA-like protein 1) (O74331)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for normal levels of meiotic recombination. Acts in the recombinational pathway of double-strand break (DSB) repair together with rhp51, rhp55 and rad22. Required for the full extent of DNA recombination and cell survival under condition of a replication fork collapse.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- DNA repair protein rdl1
- Zinc finger SWIM domain-containing protein sws1
- Swi5-dependent recombination DNA repair protein 1
- Uncharacterized protein C651.12c
- Uncharacterized protein C22G7.03
Sequence:
MNAAEWVAELKRKSQIESFKEQKGLVYDDHIEKVLYSGSVNGTLLVIEGNSCSGKTELLYHLASNVLLRSSQELVLIVSSEWDWSIKRLTFILHERLISSRGVSQTCKCNCAVKLENESTVHLQNAAREDGTDEDINSNSVNDVSLSSGETMLQFPEHEEQHECNREMEQLYESASSTVYPCSFWEDAERKIDAQCAILWPMEFSGVVESIPQSTKDLLRIWKEAKIQMHEDFRCNKTEFNEACFDASSSRLGCILMDGLSTFYWQLRLERGYTQVYADLQNRLCTSSKLFGCPVVCTNWLLNNKQHLPIQCKRFRSERRANARFYLENCVSKLGETFYLSVKGVQTKTEMASPYSQQEMEKV
Protein: Secretoglobin family 1D member 1 (Lipophilin-A) (O95968)
Organism: Homo sapiens (Human)
Function: May bind androgens and other steroids, may also bind estramustine, a chemotherapeutic agent used for prostate cancer. May be under transcriptional regulation of steroid hormones.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Mammaglobin-B
- Secretoglobin family 1D member 2
- Mammaglobin-A
Sequence:
MRLSVCLLLLTLALCCYRANAVVCQALGSEITGFLLAGKPVFKFQLAKFKAPLEAVAAKMEVKKCVDTMAYEKRVLITKTLGKIAEKCDR
Protein: Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4) (Q13485)
Organism: Homo sapiens (Human)
Function: In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (By similarity). Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15799969, ECO:0000269|PubMed:17327236}. Nucleus {ECO:0000269|PubMed:15799969}. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with R-SMAD (PubMed:15799969). PDPK1 prevents its nuclear translocation in response to TGF-beta (PubMed:17327236). {ECO:0000269|PubMed:15799969, ECO:0000269|PubMed:17327236}.
Interaction partners:
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 2
- Ski-like protein
- Mothers against decapentaplegic homolog 9
- Lymphoid enhancer-binding factor 1
- Mothers against decapentaplegic homolog 5
- TGF-beta receptor type-1
- Catenin beta-1
- Ski oncogene
- Transcription factor E2F4
Sequence:
MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPSSMMVKDEYVHDFEGQPSLSTEGHSIQTIQHPPSNRASTETYSTPALLAPSESNATSTANFPNIPVASTSQPASILGGSHSEGLLQIASGPQPGQQQNGFTGQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD
Protein: Peptidase T (EC 3.4.11.4) (Aminotripeptidase) (Tripeptidase) (L9PepTR) (Tripeptide aminopeptidase) (Q76HM5)
Organism: Lactococcus lactis subsp. lactis (Streptococcus lactis)
Function: Cleaves the N-terminal amino acid of tripeptides.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}.
Interaction partners:
Sequence:
MKYEKLLPRFLEYVKVNTRSDENSTTTPSTQALVEFAHKMGEDMKALGLKDVHYLESNGYVIGTIPANTDKKVRKIGLLAHLDTADFNAEGVNPQILENYDGESVIKLGDTEFTLDPKDFPNLKNYKGQTLVHTDGTTLLGSDDKSGVAEIMTLADYLLNINPDFEHGEIRVGFGPDEEIGVGADKFDVADFDVDFAYTVDGGPLGELQYETFSAAGAVIEFQGKNVHPGTAKNTMVNALQLAIDYHNALPEFDRPEKTEGREGFFHLLKLDGTPEEARAQYIIRDHEEGKFNERKALMQEIADKMNAELGQNRVKPVIKDQYYNMAQIIEKDMSIIDIAKKAMENLDIVPIIEPIRGGTDGSKISFMGLPTPNLFAGGENMHGRFEFVSVQTMEKAVDTLLEIIRLNNEVVK
Protein: LD18634p (Nervous fingers 1) (Zinc-finger transcription factor nerfin-1) (Q9V3B8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Scalloped, isoform Q
- Basic helix-loop-helix neural transcription factor TAP
- Worniu
- Transcriptional coactivator yorkie
Sequence:
MAQIQTPIPIPAPAEPIEKLSHPHSIGIQLQHKGMPHGLGLLTTVASLPPKYRSRYLNLKTRCEIPLDLTLKLPSPLPSSDVPMAATFAEVYSENTSASSSEVQGEVTKVEELPVKPPTPPQSPAGKRKLSRESYDDEPAKMAKKEEEVPVETVESTPAKPVKVAESAPKTNKASTSSGKPSRNKATRKLKFDEETSSPVSGTVIRPLEDITDGSMQYSNGDIDPKYNIVEITEETKAELAAIKNVIGDYVCRLCKIKFEDAFGLARHRCACIVLLEYRCPECGKQFNCPANLASHRRWHKPRKEASKKENRNTTNQPEKQQQVEKKSEEELAFDCQECGKKFKRAAYLRKHQLTHQKKEKPAEKQLEMKPTTTTITGSFHFNQAVSTSSSASSSHSDEGVYVVGSNARENYDYDNDYLSDSSSSASSAGYGRLQIVEHGLTEEESIAAAALTNLRNCASVIQHTTMAH
Protein: Bromodomain protein 1 (Q8IJ72)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MMLEDFNTLPLIKSIREDSLDDVLKFLENNYKDYEVNENGEAKKTIELVDKQTQATPLFYVTARKSDEESVEISKLIIEKYAICNPISKDLMKQTCLFYAAREGHLNLCNYLIEKGCNPNDQDNFGQTCLFYASREGKTDCVLTLIKKGANPNLLDLNKQTCLFYACRDGRYDTVKCLLENGVNPSIKDAQRRTALTFAKGNGHNNIINLLKNVGTLSRSSIDSNAQLGNITMLRRNSSSYIAASSPNESNLNNLTVQAENVSNVNLKTEDNQLRKKYKLQYKPLSDEDPLLWVDAPLIKIKEFERKFPELALWPRNVSQSNVEVNNANDAFNKQWYLLANQLILSLSKYEGGHIFEKLVDAKKQNCPDYYDVIKNPMSFSCIKTKLKKGQYAYPSEFVKDVQLIFDNCSLYNTSNSVVAITGKNIETYFNNQLIVMGYNNFILKEKKINDMLKLVEEENIKWSKEKEDQIEEIDELENNQEDSSKKD
Protein: PAX3- and PAX7-binding protein 1 (PAX3/7BP) (GC-rich sequence DNA-binding factor 1) (P58501)
Organism: Mus musculus (Mouse)
Function: Adapter protein linking the transcription factors PAX3 and PAX7 to the histone methylation machinery and involved in myogenesis. Associates with a histone methyltransferase complex that specifically mediates dimethylation and trimethylation of 'Lys-4' of histone H3. Mediates the recruitment of that complex to the transcription factors PAX3 and PAX7 on chromatin to regulate the expression of genes involved in muscle progenitor cells proliferation including ID3 and CDC20.
Subcellular location: Nucleus {ECO:0000269|PubMed:22862948}.
Interaction partners:
Sequence:
MFRKARRVNVRKRNDSEEEERERDEEQEPPPLLPPPASGEEPGPGGGDRAPAGESLLGPGPLPPPPSAHHPGLGAEAGGGISGGAEPGNGLKPRKRPRENKEVPRASLLSFQDEEEENEEVFKVKKSSYSKKIVKLLKKEYKEDLEKSKIKTELNTAADSDQPLDKTCHAKDTNPEDGVVISEHGEDEMDMESEKEEEKPKAGGAFSNALSSLNVLRPGEIPDAAFIHAARKKRQLARELGDFTPHDSEPGKGRLVREDENDASDDEDDDEKRRIVFSVKEKSQRQKIAEEIGIEGSDDDALVTGEQDEELSRWEQEQIRKGINIPQVQASQPSEVNVYYQNTYQTMPYGASYGIPYSYTAYGSSDAKSQKTDNTVPFKTPSNEMAPVTIDLVKRQLKDRLDSMKELHKTNQQQHEKHLQSRVDSTRAIERLEGSSGGIGERYKFLQEMRGYVQDLLECFSEKVPLINELESAIHQLYKQRASRLVQRRQDDIKDESSEFSSHSNKALMAPNLDSFGRDRALYQEHAKRRIAEREARRTRRRQAREQTGQMADHLEGLSSDDEETSTDITNFNLEKDRILKESSKVFEDVLESFYSIDCIKAQFEAWRSKYYMSYKDAYIGLCLPKLFNPLIRLQLLTWTPLEAKCRDFETMLWFESLLFYGCEDREQEKDEADVALLPTIVEKVILPKLTVIAETMWDPFSTTQTSRMVGITMKLINGYPSVVNADNKNTQVYLKALLLRMRRTLDDDVFMPLYPKNVLENKNSGPYLFFQRQFWSSVKLLGNFLQWYGIFSNKTLQELSIDGLLNRYILMAFQNSEYGDDSIRKAQNVINCFPKQWFVNLKGERTISQLENFCRYLVHLADTIYRNSIGCSDVEKRNARENIKQIVKLLASVRALDHAISVASDHNVKEVKSLIEGK
Protein: Serine/threonine-protein kinase ATG1 (EC 2.7.11.1) (Autophagy-related protein 1) (Q52EB3)
Organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
Function: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8 (By similarity). Autophagy is essential to fungal development, production of appressorium turgor, and pathogenicity in rice blast disease.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17416896}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
Interaction partners:
- Autophagy-related protein 13
- Autophagy-related protein 9
- Autophagy-related protein 8
- Autophagy-related protein 2
- Autophagy-related protein 101
- Serine/threonine-protein kinase TOR
- Beclin-1
- Autophagy-related protein 11
- non-specific serine/threonine protein kinase
- Phosphatidylinositol 3-kinase VPS34
Sequence:
MADRSARRARPGDDSVGQFVIGAEIGKGSFAQVYMGKHKVSGAAVAIKSVELARLNKKLKENLYGEINILKTLRHPHIVALHDCVESATHINLMMEYCELGDLSLFIKKREKLSTNPATHDMARKYPNVPNSGLNEVVIRHFLKQLSSALKFLRESNLVHRDVKPQNLLLLPSPEFREVNKLARPILTASQDSLVPVAGLASLPMLKLADFGFARVLPSTSLAETLCGSPLYMAPEILRYERYDAKADLWSVGTVLFEMIVGRPPFRASNHVELLRKIEAAEDVIKFPRETTISSEMKGLTRALLKRNPVERISFENFFAHPVIISSIPGLVEDDIPKPEASEQRSSSKDTRAASKSDDPIASPRKYSFRRHPTDNDQIRDQFRRVEPPSSAAESAPSRQTSAFSGIAAEARKQAAAEASARTGQSSRNEPGDNLVPRRPQAQPSTSAPSKPGLYEERRRGISNASLNRSNRESSSPTSAALANDSARAPPQQTSRRVQAEEREKAAQDVAFERDYVVVEKKHVEVNAFADEMAANPRLGGQGTPLSPKSGQIVRRATQQGNPTSTTGAIPAAPSRTMQIAQGTQRHYHERGTSLSASPGSTASFITKAIQDASLRLLGIKYPAGLTKGASPPELYNPYPAYPTPSPPVGLISSGKQSTPVDEDARVAQLIEEHATRSDVVYGFAEVKYKQLVPLAPSAEHGLGGTTLEDMPTGEEDVLTVEAIVSLSEEALVLYVKALTLLAKSMDIASLWWARKNRGDQANNALSSTRDSVNTQTLSLRINSAVQWVRSRFNEVLEKAEVVRLRLMDAQKRLPDDHPSHPSNHPQGSESVNGASAEGVFLTVGVTAEKLMYDRALEMSRTAAINEITNEDLAGCEISYVTAIRMLEAVLDNDEDAPKRRLSANMDDSGGDGEDGHAEINADDQQAVQKMIHMIRSRLTSVRSKVRMISNASKAQQQSQPQSLIRRRSGDVTPRSVPSYSS