wanglab/gogpt-training-data huggingface dataset:
Protein: TATA-box-binding protein (TATA sequence-binding protein) (TATA-binding factor) (TATA-box factor) (Transcription initiation factor TFIID TBP subunit) (P20226)
Organism: Homo sapiens (Human)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C. TBP forms the TFIID-A module together with TAF3 and TAF5. TBP is a general transcription factor that functions at the core of the TFIID complex. During assembly of the core PIC on the promoter, as part of TFIID, TBP binds to and also bends promoter DNA, irrespective of whether the promoter contains a TATA box. Component of a BRF2-containing transcription factor complex that regulates transcription mediated by RNA polymerase III. Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter. SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:27007846}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB1
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 6
- Transcription factor IIIB 50 kDa subunit
- Transcription initiation factor IIA subunit 1
- Transcription initiation factor TFIID subunit 3
- Transcription initiation factor TFIID subunit 7
- General transcription factor IIE subunit 1
- Transcription factor IIIB 90 kDa subunit
Sequence:
MDQNNSLPPYAQGLASPQGAMTPGIPIFSPMMPYGTGLTPQPIQNTNSLSILEEQQRQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQAVAAAAVQQSTSQQATQGTSGQAPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRAEIYEAFENIYPILKGFRKTT
Protein: Homologous-pairing protein 2 homolog (Nuclear receptor coactivator GT198) (PSMC3-interacting protein) (Proteasome 26S ATPase subunit 3-interacting protein) (Tat-binding protein 1-interacting protein) (TBP-1-interacting protein) (Q9P2W1)
Organism: Homo sapiens (Human)
Function: Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1-promoted homologous pairing. May inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3. Acts as a tissue specific coactivator of hormone-dependent transcription mediated by nuclear receptors.
Subcellular location: Nucleus {ECO:0000269|PubMed:11739747}.
Interaction partners:
- Meiotic nuclear division protein 1 homolog
- DNA repair protein RAD51 homolog 1
- Breast cancer type 1 susceptibility protein
- Meiotic recombination protein DMC1/LIM15 homolog
- 26S proteasome regulatory subunit 6A
Sequence:
MSKGRAEAAAGAAGILLRYLQEQNRPYSSQDVFGNLQREHGLGKAVVVKTLEQLAQQGKIKEKMYGKQKIYFADQDQFDMVSDADLQVLDGKIVALTAKVQSLQQSCRYMEAELKELSSALTTPEMQKEIQELKKECAGYRERLKNIKAATNHVTPEEKEQVYRERQKYCKEWRKRKRMATELSDAILEGYPKSKKQFFEEVGIETDEDYNVTLPDP
Protein: Ubiquitin-ribosomal protein eS31 fusion protein (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; Small ribosomal subunit protein eS31 (40S ribosomal protein S27a)] (P62992)
Organism: Bos taurus (Bovine)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31]: Nucleus, nucleolus {ECO:0000250|UniProtKB:P62979}.
Interaction partners:
- Small ribosomal subunit protein eS24
- 40S ribosomal protein S30
- 40S ribosomal protein S30
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein eS17
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK
Protein: Nuclear receptor co-repressor 2 (A0A0G2JU91)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSGSTQPVAQTWRAAEPRYPPHGISYPVQIARPHTDVGLLEYQHHPRDYTSHLSPGSIIQPQRRRPSLLSEFQPGSERSQELHLRPESRTFLPELGKPDIEFTESKRPRLELLPDTLLRPAPLLATGQPSGSEDLTKDRSLAGKLEPVSPPSPPHADPELELTPSRLSKEELIQNMDRVDREITMVEQQISKLKKKQQQLEEEAAKPPEPEKPVSPPPIESKHRSLVQIIYDENRKKAEAAHRILEGLGPQVELPLYNQPSDTRQYHENIKINQAMRKKLILYFKRRNHARKQWEQRFCQRYDQLMEAWEKKVERIENNPRRRAKESKVREYYEKQFPEIRKQRELQERMQSRVGQRGSGLSMSAARSEHEVSEIIDGLSEQENLEKQMRQLAVIPPMLYDADQQRIKFINMNGLMDDPMKVYKDRQVTNMWSEQERDTFREKFMQHPKNFGLIASFLERKTVAECVLYYYLTKKNENYKSLVRRSYRRRGKSQQQQQQQQQQQQQQQQQQMARSSQEEKEEKEKEKEADKEEEKQDAENEKEELSKEKTDDTSGEDNDEKEAVASKGRKTANSQGRRKGRITRSMANEANHEETATPQQSSELASMEMNESSRWTEEEMETAKKGLLEHGRNWSAIARMVGSKTVSQCKNFYFNYKKRQNLDEILQQHKLKMEKERNARRKKKKTPAAASEETAFPPAAEDEEMEASGASANEEELAEEAEASQASGNEVPRVGECSGPAAVNNSSDTESVPSPRTEATKDAGPKPASTEALPAATQPPVPPPEEPATVPDEPCPAPDASGPPSPVASPPPAAPPAAVDKDEQDQAATVPQTEDAKEQKSEAEELVIDVGKTEEPEAPEEPPESVKSDHKEETEEEPEDKAKGPEAIETVSEAPLKVEEAGSKAAVTKGSSSGATQDSDSSATCSADEVDEPEGGDKGRLLSPRPSLLTPAGDPRASTSPQKPLDLKQLKQRAAAIPPIVTKVHEPPREDTVPPKPAPPVPPPTQHLQPEGDVSQQSGGSPRGKCRSPVPPAEKEAEKASFFPAFPAEGPKLPTEPPRWTSGLPFPIPPREVIKTSPHAADPSAFSYTPPGHPLPLGLHDSARPVLPRPPISNPPPLISSAKHPGVLERQLGTISQQGMSVQLRVPHSEHAKAPMGPLTMGLPLAVDPKKLAPFSGVKQEQLSPRGQAGPPESLGVPTAQETSVLRGTALGSTASGSITKGLPSTRTADGPSYRGSITHGTPADVLYKGTISRIVGEDSPSRLDRAREDTLPKGHVIYEGKKGHVLSYEGGMSVSQCSKEDGRSSSGPPHETAAPKRTYDMMEGRVGRTITSASIEGLMGRAIPEQHSPHLKEQHHIRGSITQGIPRSYVEAQEDYLRREAKLLKREGTPPPPPPPRDLTETYKTRPLDPLGPLKLKPTHEGVVATVKEAGRSIHEIPREELRRTPELPLAPRPLKEGSITQGTPLKYDSGVPSSGSKKHDVRSIIGSPGRPFPALHPLDIMADARALERACYEESLKSRSGTSSGAGGSITRGAPVVVPELGKPRQSPLAYEDHGAPFTSHLPRGSPVTTREPTPRLQEGSLLSSKASQDRKLTSTPREIAKSPHSTVPEHHPHPISPYEHLLRGVTGVDLYRGHIPLAFDPTSIPRGIPLEAAAAAYYLPRHLAPSPTYPHLYPPYLIRGYPDTAALENRQTIINDYITSQQMHHNAASAMAQRADMLRGLSPRESSLALNYAAGPRGIIDLSQVPHLPVLVPPTPGTPATAIDRLAYLPTAPPPFSSRHSSSPLSPGGPTHLAKPTATSSSERERERERERDKSILTSTTTVEHAPIWRPGTEQSSGAGGSSRPASHTHQHSPISPRTQDALQQRPSVLHNTSMKGVVTSVEPGTPTVLRWARSTSTSSPVRPAATFPPATHCPLGGTLEGVYPTLMEPVLLPKETSRVTRPERPRVDAGHAFLTKPPAREPASSPSKSSEPRSLAPPSSSHTAIARTPAKSLAPHHASPDLPAPTSASDLHREKTQSKPFSIQELELRSLGYHSGAGYSPDGVEPISPVSSPSLTHDKGLSKPLEELEKSHLEGELRHKQPGPMKLSGEAAHLPHLRPLPESQPSSSPLLQTAPGIKGHQRVVTLAQHISEVITQDYTRHHPQQLSGPLPAPLYSFPGASCPVLDLRRPPSDLYLPPPDHGTPARGSPHSEGGKRSPEPSKTVLSSSEDAIEPVSPPEGMTEPGHARSTAYPLLYRDGEQGEPRMGSKSPGNTSQPPAFFSKLTESNSAMVKSKKQEINKKLNTHNRNEPEYNIGQPGTEIFNMPAITGAGLMTCRSQAVQEHASTNMGLEAIIRKALMGKYDQWEEPPPLGANAFNPLNASASLPAAAMPITTADGRSDHPLTSPGGGGKAKVSGRPSSRKAKSPAPGLAPGDRPPSVSSVHSEGDCNRRTPLTNRVWEDRPSSAGSTPFPYNPLIMRLQAGVMASPPPPGLAAGSGPLAGPHHAWDEEPKPLLCSQYETLSDSE
Protein: Gustatory receptor (A1Z881)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363108}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363108}.
Interaction partners:
- Gustatory receptor for bitter taste 66a
- Gustatory and pheromone receptor 33a
- Gustatory receptor
- Gustatory and pheromone receptor 32a
- Gustatory receptor 8a
- Gustatory receptor for bitter taste 93a
- Putative gustatory receptor 22f
Sequence:
MAFTSSQLCSLLTKFTALNGLNTYYFDTKTNAFRVSSKLKIYCAIHHALCVLALAHMSYSTASNLRVSVTVLTIGGTMACCVKSCWEKAQGIRNLARGLVTMEQKYFAGRPSGLLLKCRYYIKITFGSITLLRIHLIQPIYMRRLLPSQFYLNVGAYWLLYNMLLAAVLGFYFLLWEMCRIQKLINDQMTLILARSGQRNRLKKMQHCLRLYSKLLLLCDQFNSQLGHVAIWVLACKSWCQITFGYEIFQMVAAPKSIDLTMSMRVFVIFTYIFDAMNLFLGTDISELFSTFRADSQRILRETSRLDRLLSMFALKLALHPKRVVLLNVFTFDRKLTLTLLAKSTLYTICCLQNDYNKLKA
Protein: Iodotyrosine deiodinase (EC 1.21.1.1) (Halotyrosine dehalogenase) (B9K712)
Organism: Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E)
Function: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine. Activity towards 2-iodophenol is weak.
Interaction partners:
- Acetamidase
- Vitamin B12-dependent ribonucleotide reductase
Sequence:
MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF
Protein: Methyl-accepting chemotaxis protein PctC (Q9HW93)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Responds to L-His, L-Pro and gamma-aminobutyrate (GABA). Also involved in repellent responses to trichloroethylene (TCE), chloroform and methylthiocyanate. Also mediates chemotaxis to histamine, but does not bind histamine.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Chemotaxis protein CheA
- Chemotaxis protein methyltransferase 1
- Chemotaxis protein CheA
- Chemotaxis protein methyltransferase 2
- Probable chemoreceptor glutamine deamidase CheD
- Probable purine-binding chemotaxis protein
- Chemotaxis protein CheW
- Chemotaxis protein CheA
- Protein-glutamate methylesterase/protein-glutamine glutaminase 2
- Protein-glutamate methylesterase/protein-glutamine glutaminase 1
Sequence:
MLRSLSFAKKILLAAALVVVFAFSCFILYNDYRQREAVRTDTENYLGEIGTLTASNIQSWLEGRMHLVEGLASQLALLDQPDEANIARQLEQPVFSRNFASVYLGEAASGTFTMRPYDAMPEGYDPRTRAWYKDALAADRLIVTEPFVDAGTGEQILAMSLPVRHAGQLLGVAAGDMKLETLTAILNSLKFDGAGYAFLVSDAGKILLHPDSGLVLKTLAEAYPKGAPNIVPGVHEVELDGSSQFVSFTPVKGLPGVTWYVALVLDRDTAYSMLSEFRTSAIVATLIAVVGIMLLLGMLIRVLMQPLTDMGRAMQDIAQGEGDLTKRLKVTSNDEFGTLANAFNRFVERIHESIREVAGTARQLHDVAQLVVNASNSSMANSDEQSNRTNSVAAAINELGAAAQEIARNAADASHHASDANHQAEDGKQVVEQTIRAMNELSEKISASCANIEALNSRTVNIGQILEVIKGISEQTNLLALNAAIEAARAGEAGRGFAVVADEVRNLAHRAQESAQQIQKMIEELQVGAREAVATMTESQRYSLESVEIANRAGERLGSVTSRIGEIDSMNQSVATATEEQTAVVDSLNMDITEINTLNQEGVENLQATLRACGELETQAGRLRHLVDSFKI
Protein: Histone H2B (Q8IBV7)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000451}.
Interaction partners:
- Histone H4
- Histone H3
- Histone H2A
- Histone H3
- Histone H3-like centromeric protein CSE4
- PH domain-containing protein, putative
- Histone H2A
- FACT complex subunit
- Chromatin remodeling protein
- RuvB-like helicase
Sequence:
MSGKGPAQKSQAAKKTAGKTLGPRHKRKRRTESFSLYIFKVLKQVHPETGVTKKSMNIMNSFINDIFDRLVTEATRLIRYNKKRTLSSREIQTAVRLLLPGELSKHAVSEGTKAVTKYTTSAA
Protein: GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 1) (ARTC1) (Mono(ADP-ribosyl)transferase 1) (YAC-1) (CD antigen CD296) (Q60935)
Organism: Mus musculus (Mouse)
Function: Has ADP-ribosyltransferase activity toward GLP1R.
Subcellular location: Sarcoplasmic reticulum membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
Sequence:
MKIPAMMSLLLVSVGLRDGVQVQSYSISQLDIFSQETPLDMAPASFDDQYAGCLADMTAALPDLNHSEFQANKVYADGWAQANNQWQERRAWGSVWGSLPPSPPGFRDEHGVALLAYTANSPLHKEFNAAVREAGRSRAHYLHHFSFKTLHFLLTEALQLLRSHRSRGCQQVYRGVHGLRFRPAGPGATVRLGGFASASLKNVAAQQFGEDTFFGIWTCLGAPIRGYSFFPEEEEVLIPPFETFQVINTSRPTQGPARIYLRALGKRSTYNCEYIKEKKCRSGPCWLGSSAPGSISASCSLLLLLLFLVLSALPENPGLQQLTRC
Protein: NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (Q9Z1E3)
Organism: Mus musculus (Mouse)
Function: Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and pro-inflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P25963}. Nucleus {ECO:0000250|UniProtKB:P25963}. Note=Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export. {ECO:0000250|UniProtKB:P25963}.
Interaction partners:
- Proto-oncogene c-Rel
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- NF-kappa-B inhibitor beta
- Transcription factor p65
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Nuclear factor NF-kappa-B p105 subunit
- NF-kappa-B essential modulator
- F-box/WD repeat-containing protein 1A
- S-phase kinase-associated protein 1
- Nuclear factor NF-kappa-B p100 subunit
Sequence:
MFQPAGHGQDWAMEGPRDGLKKERLVDDRHDSGLDSMKDEEYEQMVKELREIRLQPQEAPLAAEPWKQQLTEDGDSFLHLAIIHEEKPLTMEVIGQVKGDLAFLNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQTCTPQHLHSVLQATNYNGHTCLHLASIHGYLAIVEHLVTLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDTESEFTEDELPYDDCVFGGQRLTL
Protein: Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB (EC 3.2.1.113) (Mannosidase alpha class 1A member 2) (Processing alpha-1,2-mannosidase IB) (Alpha-1,2-mannosidase IB) (P39098)
Organism: Mus musculus (Mouse)
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
- Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Histone-lysine N-methyltransferase EZH2
- alpha-1,2-Mannosidase
- Polycomb protein Suz12
- Protein Jumonji
- Polycomb protein EED
Sequence:
MTTPALLPLSGRRIPPLNLGPPSFPHHRATLRLSEKFILLLILSAFITLCFGAFFFLPDSSKHKRFDLGLEDVLIPHVDAGKGAKNPGVFLIHGPDEHRHREEEERLRNKIRADHEKALEEAKEKLRKSREEIRAEIQTEKNKVAQAMKTKETRVLPPVPVPQRVGVSGGDPEDMEIKKKRDKIKEMMKHAWDNYRTYGWGHNELRPIARKGHSTNIFGSSQMGATIVDALDTLYIMGLHDEFMDGQRWIEENLDFSVNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKTKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVGRNWGWASAGSSILAEFGTLHMEFVHLSYLTGDLTYYNKVMHIRKLLQKMERPNGLYPNYLNPRTGRWGQYHTSVGGLGDSFYEYLLKAWLMSDKTDHEARRMYDDAVEAIEKHLIKKSRGGLVFIGEWKNGHLERKMGHLACFAGGMFALGADGSRKDKAGHYLELGAEIARTCHESYDRTALKLGPESFKFDGAVEAVAVRQAEKYYILRPEVIETYWYLWRFTHDPRYRQWGWEAALAIEKSCRVSGGFSGVKDVYAPTPVHDDVQQSFFLAETLKYLYLLFSGDDLLPLDHWVFNTEAHPLPVLRLANSTLSGNPAVR
Protein: [histone H3]-trimethyl-L-lysine(27) demethylase (EC 1.14.11.68) (G3V9U4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Retinoblastoma-binding protein 5
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Histone H3.3
- Histone H3
- Histone H3.1
- ATP synthase F
- ATP synthase F
- Histone-lysine N-methyltransferase EZH2
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- Polycomb protein EED
Sequence:
MHRAVDPPGARSAREAFALGGLSCAGAWSSCPPHPPPRNSWLPGGRCSASIGQPPLSAPLPPSHGNSSGHPNKPYYASGTPTPRPLHGKLESLHGCVQALLREPAQPVLWEQLGQLYESEHDSEEAICCYHRALRYGGSFAELGPRIGRLQQAQLWNLHAGSCQHRAKVLPPLEQVWNLLHLEHKRNYGAKRGGPPVKRSAEPPVVQPMPPAALSGPSGEEGLSPGGKRRRGCSSEQEQRHSLPHPHPYPAPAYTAHPPSHRLGPATPLGPGPRPPGAESHGCLPATRPPGSDLRESRVQRSRMDSSVSPAASTACVPYAPSRPPGLPGTSSSSSSSNNTGLRGVEPSPGIPGADHYQNPALEIAPHQARLGPSAHSSRKPFLTAPAAAPHLSLPSGTPSSPPPPCPRLLRPPPPPAWMKGSACRSAREDGEILGELFFGAEGPPRPPPPPLPHRDGFLGPPNPRFSVGTQDSHTPPTPPTTTSSSSSSSSSNSHSSSPTGPVPFPPPPYLARSIDPLPRPSSPTLSSQDPPLPPLTLALPPAPPSSCHQNTSGSFRRSESPRPRVSFPKTPEVGQGPPPGSLSKAPQPVPPGVGELPARGPRLFDFPPTPLEDQFEEPAEFKILPDGLANIMKMLDESIRKEEEQQQQEAGAVPPPPLKEPFASLRSSLPSDTAPAATTAAATPTTTTTTTTQEEEKKPPPALPPPPPLAKFPPPPQPPPPPPASPASLLKSLASVLEGQKYCYRGTGAAVSTRPGSVPATQYSPSPASGATAPPPTSVAPSAQGSPKPSVSSSSQFSTSGGPWVRERRAGEEPAPGPVTPAQLPPPLPLPPARSESEVLEEISRACETLVERVGRSAINPADPVDIADPVDSGTEPQPPPAQAKEESGGVAVAAAGPGSGKRRQKEHRRHRRTCRDSVGRRPREGRAKAKAKAPKEKSRRVLGNLDLQSEEIQGREKARPDVGGASKVKTPTTPAPPPAPAPSAQPTPPSAPVPGKKTREEAPGPPGVSRADMLKLRSLSEGPPKELKIRLIKVESGDKETFIASEVEERRLRMADLTISHCAADVMRASKNAKVKGKFRESYLSPAQSVKPKINTEEKLPREKLNPPTPSIYLESKRDAFSPVLLQFCTDPRNPITVIRGLAGSLRLNLGLFSTKTLVEASGEHTVEVRTQVQQPSDENWDLTGTRQIWPCESSRSHTTIAKYAQYQASSFQESLQEEKESEDEESEEPDSTTGTSPSSAPDPKNHHIIKFGTNIDLSDAKRWKPQLQELLKLPAFMRVTSTGNMLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFAVHEHYWETISAFCDRHGVDYLTGSWWPILDDLYASNIPVYRFVQRPGDLVWINAGTVHWVQATGWCNNIAWNVGPLTAYQYQLALERYEWNEVKNVKSIVPMIHVSWNVARTVKISDPDLFKMIKFCLLQSMKHCQVQRESLVRAGKKIAYQGRVKDEPAYYCNECDVEVFNILFVTSENGSRNTYLVHCEGCARRRSAGLQGVVVLEQYRTEELAQAYDAFTLAPASTSR
Protein: Dit-like phage tail protein N-terminal domain-containing protein (H9C1A8)
Organism: Pectobacterium phage ZF40 (Bacteriophage ZF40)
Interaction partners:
Sequence:
MSIVGVFDKSRPEIGGIFFDAILEESSELRTDVSEYPLETGQTANDNAVTRPMTVTMTVAISDNPVKALMAEAGQFSGIAGIGAGVAVGAVGSILGGGAAALAGLAASAGLAFAASGSKRSESALLEIRKLQVEKSILTVVGVNSSYDDMIITNTRVQKNKQNEGGQEIVVEMRALLIKNRNDSAATTNRNLPAGDSAATQGQANVNLGEVTPQ
Protein: Vacuolar protein 8 (O43028)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Lipid-anchor {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000269|PubMed:16823372}; Lipid-anchor {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative lipase atg15
- Autophagy protein 13
- Palmitoyltransferase pfa3
- Taz1-interacting factor 1
- Palmitoyltransferase akr1
- Palmitoyltransferase swf1
- Serine/threonine-protein kinase atg1
- Alkaline phosphatase
Sequence:
MGNCLSCCEKSKDEQYEPLLADREREAVADLLSFLEDRNEVNFYSEEPLRALTILAYSDNLDLQRSAALAFAEITEKDVREVDRETIEPVLFLLQSPDAEIQRAASVALGNLAVNAENKALVVKLNGLDLLIRQMMSPHVEVQCNAVGCITNLATLDENKSKIAHSGALGPLTRLAKSKDIRVQRNATGALLNMTHSYENRQQLVSAGTIPVLVSLLPSSDTDVQYYCTTSISNIAVDAVHRKRLAQSEPKLVRSLIQLMDTSSPKVQCQAALALRNLASDERYQIEIVQSNALPSLLRLLRSSYLPLILASVACIRNISIHPLNESPIIDAGFLRPLVDLLSCTENEEIQCHAVSTLRNLAASSERNKRAIIEANAIQKLRCLILDAPVSVQSEMTACLAVLALSDEFKSYLLNFGICNVLIPLTDSMSIEVQGNSAAALGNLSSNVDDYSRFIECWDSPAGGIHGYLVRFLSSEDSTFAHIAAWTIVQLLEAGVPRLTAFIQSSDDIIELLNDIVARDANNGEYEDGEGDVILLSGRALHLIEQDTDS
Protein: Beta-adaptin-like protein (F4JNZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MSGHDSKYFSTTKKGEIPELKEELNSQYKCDDSVHFSVTDWDIVTLVKLRLDKRKDAVKKVIAAMTVGKDVSSLFTDVVNCMQTENLELKKLVYLYLINYAKSQPDLAILAVNTFVKDSQDPNPLIRALAVRTMGCIRVDKITEYLCDPLQKCLKDDDPYVRKTAAICVAKLFDINAELVEDRGFLEALKDLISDNNPMVVANAVAALAEIQENSSSPIFEINSTTLTKLLTALNECTEWGQVFILDALSKYKAADPREAENIVERVTPRLQHANCAVVLSAVKMILQQMELITSTDVIRNLCKKMAPPLVTLLSAEPEIQYVALRNINLIVQKRPTILAHEIKVFFCKYNDPIYVKMEKLEIMIKLASDRNIDQVLLEFKEYATEVDVDFVRKAVRAIGRCAIKLERAAERCISVLLELIKIKVNYVVQEAIIVIKDIFRRYPNTYESIIATLCESLDTLDEPEAKASMIWIIGEYAERIDNADELLESFLENFPEEPAQVQLQLLTATVKLFLKKPTEGPQQMIQVVLNNATVETDNPDLRDRAYIYWRLLSTDPEAAKDVVLAEKPVISDDSNQLDPSLLDELLTNISTLSSVYHKPPEAFVTRLKTTVQKTEDEDFAEGSEAGYSSSNPVDSAASPPGNIPQPSGRQPAPAVPAPVPDLLGDLMGLDNAAIVPVDDPITQSGPPLPVVVPASSGQGLQISAQLSRKDGQVFYSMLFENNSQSVLDGFMIQFNKNTFGLAAAGSLQIPPLHPATSARTMLPMVLFQNMSAGPPSSLLQVAVKNNQQPVWYFTDKIILHALFGEDGRMERGTFLETWRSLPDSNEVLKEFPGITITSVESTIELLTAFNMFFIAKRKNGNQDVIYLSAKDPRDVPFLIELTAMVGQPGLKCAVKTPTPEIAPLFFEALELLFKA
Protein: Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase (EC 2.4.1.260) (Alpha-1,6-mannosyltransferase ALG12) (Asparagine-linked glycosylation protein 12) (EMS-mutagenized BRI1 suppressor 4) (A8MR93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for N-linked oligosaccharide assembly. Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor dolichol-PP-Man(7)GlcNAc(2).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:20023196}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dol-P-Glc:Glc
- Alpha-1,2-mannosyltransferase ALG9
- Dol-P-Man:Man
- dolichyl-phosphate beta-glucosyltransferase
- GDP-Man:Man
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- GPI mannosyltransferase 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Alpha-mannosidase I MNS5
Sequence:
MPTDSKMAKFLQSYGYDLILGSVAAIYVVMAPYTKVEESFNVQSMHDILYHRHHLDSYDHLEFPGVVPRTFIGAFIVSVFASPVVSIISCLGFPKVYSLVAARLVLGCIILSTLRFFRIQIKKKFGNQVETFFVLFTSLQFHFLFYCTRPLPNILALGLVNLAYGNWLKGNFYPALSFLIFATVIFRCDTMLLLGPIGLELLLTKSISFWKALKYCVGTALLAVGLTIFVDSIMWKKFVWPEFEVFWFNSILNRSSDWGTHSIHWYFTSALPRSLLVAYPLSLLGTLVDRRVPFFIVPVLSFVILYSKLPHKELRFIISSVPMFNLSAAVAASRIYNNRKKTIWKLVNMVMLAFFAISAGCTVVTFMASYYNYPSGYALKRLHQIGHPANVAGEEWVHIDTFGAMNGISRFCEDDFPWRYSKEEEIVVEELRNRNFTYLVNEHSSVDGYKCLFYEEGFERLELRRGFPPIVLVKKAKVYLHREMKKEDPFHKKWPGC