wanglab/gogpt-training-data huggingface dataset:
Protein: TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 2) (TAK1-binding protein 2) (TAB-2) (TGF-beta-activated kinase 1-binding protein 2) (Q9NYJ8)
Organism: Homo sapiens (Human)
Function: Adapter required to activate the JNK and NF-kappa-B signaling pathways through the specific recognition of 'Lys-63'-linked polyubiquitin chains by its RanBP2-type zinc finger (NZF). Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin chains. The RanBP2-type zinc finger (NZF) specifically recognizes Lys-63'-linked polyubiquitin chains unanchored or anchored to the substrate proteins such as RIPK1/RIP1: this acts as a scaffold to organize a large signaling complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1. Regulates the IL1-mediated translocation of NCOR1 out of the nucleus (By similarity). Involved in heart development.
Subcellular location: Membrane {ECO:0000269|PubMed:10882101, ECO:0000269|PubMed:24434549}; Peripheral membrane protein {ECO:0000269|PubMed:10882101}. Endosome membrane {ECO:0000269|PubMed:24434549}; Peripheral membrane protein {ECO:0000269|PubMed:10882101}. Lysosome membrane {ECO:0000269|PubMed:24434549}; Peripheral membrane protein {ECO:0000269|PubMed:10882101}. Cytoplasm, cytosol {ECO:0000269|PubMed:10882101, ECO:0000269|PubMed:24434549, ECO:0000269|PubMed:36681779}. Note=Following IL1 stimulation, translocation occurs from the membrane to cytosol (PubMed:10882101). Interaction with TRIM38 promotes translocation from cytosol to endosome and lysosome (PubMed:24434549). {ECO:0000269|PubMed:10882101, ECO:0000269|PubMed:24434549}.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 7
- NF-kappa-B essential modulator
- Polyubiquitin-C
- Nuclear receptor corepressor 1
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 3
- Receptor-interacting serine/threonine-protein kinase 1
- Interleukin-1 receptor-associated kinase 1
- Tumor necrosis factor
- TNF receptor-associated factor 6
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
Sequence:
MAQGSHQIDFQVLHDLRQKFPEVPEVVVSRCMLQNNNNLDACCAVLSQESTRYLYGEGDLNFSDDSGISGLRNHMTSLNLDLQSQNIYHHGREGSRMNGSRTLTHSISDGQLQGGQSNSELFQQEPQTAPAQVPQGFNVFGMSSSSGASNSAPHLGFHLGSKGTSSLSQQTPRFNPIMVTLAPNIQTGRNTPTSLHIHGVPPPVLNSPQGNSIYIRPYITTPGGTTRQTQQHSGWVSQFNPMNPQQVYQPSQPGPWTTCPASNPLSHTSSQQPNQQGHQTSHVYMPISSPTTSQPPTIHSSGSSQSSAHSQYNIQNISTGPRKNQIEIKLEPPQRNNSSKLRSSGPRTSSTSSSVNSQTLNRNQPTVYIAASPPNTDELMSRSQPKVYISANAATGDEQVMRNQPTLFISTNSGASAASRNMSGQVSMGPAFIHHHPPKSRAIGNNSATSPRVVVTQPNTKYTFKITVSPNKPPAVSPGVVSPTFELTNLLNHPDHYVETENIQHLTDPTLAHVDRISETRKLSMGSDDAAYTQALLVHQKARMERLQRELEIQKKKLDKLKSEVNEMENNLTRRRLKRSNSISQIPSLEEMQQLRSCNRQLQIDIDCLTKEIDLFQARGPHFNPSAIHNFYDNIGFVGPVPPKPKDQRSIIKTPKTQDTEDDEGAQWNCTACTFLNHPALIRCEQCEMPRHF
Protein: DNA-directed RNA polymerase subunit (EC 2.7.7.6) (D4A5A6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- RNA polymerase II subunit J
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase subunit
Sequence:
MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDVTRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPTSPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPEDSDEEN
Protein: Adenylyltransferase and sulfurtransferase MOCS3 homolog (UBA4 homolog) (Ubiquitin-like protein activator 4 homolog) [Includes: Adenylyltransferase (EC 2.7.7.-); Sulfurtransferase (EC 2.8.1.-)] (Q386S6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049}.
Interaction partners:
- Ubiquitin-related modifier 1 homolog
- cysteine desulfurase
- Mercaptopyruvate sulfurtransferase, putative
- Centrosomal protein of 19 kDa
- Small ubiquitin protein, putative
- cysteine desulfurase
- Aminotransferase class V domain-containing protein
- Cytoplasmic tRNA 2-thiolation protein 1
- Autophagocytosis associated protein, putative
Sequence:
MNVLEDLEAQVATARLRLHELEERLHEERNRVNSCGADVLTSSGPSSIDNSGGSTAGETPSFVSSSGSLTKSDVERFSRQIVLEDIGAKGMDRIRRGRVLLVGAGGLGSTAALYLVAAGVGELCIVDFDTVEHSNLHRQIIHNTMRVGMSKAESAVQSCLALNPRAKIRAITAPFTPANAEELVRGCDVVVDGSDNVATRYLINDAAARYRRPLVSGSALRWEGQLSVYCGGLSCPCYRCLFPTPPPASAVGSCNDTGVVGPVPGCIGCLQATEALKLLAGAGDVLEGRLLLLDALRMQLRVVRLRGRQKDCPACGEAAKLNVGKSLQQLAAERPEYVMPSCASGALRSANMLPAEANVAPSVYFSVLQKLLRGERMSWMTLDVRPKEQYDMAHLPHSVSLPLKQLEMWKRDGVLQNEWEKFVNSVPCASRGPMDVYVICRRGISSVKAMQVLLPLQEWCPKSCGTDVDGKAAIHQNPGKRFRFINVDGGLNRYHREVDRNFPFY
Protein: Sister chromatid cohesion protein PDS5 homolog C (Precocious dissociation of sisters protein 5-C) (AtPDS5C) (Q8GUP3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex. Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication (By similarity). Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q29RF7}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein SCC2
- Wings apart-like protein 1
- Wings apart-like protein 2
- Histone H3.1
- Histone H3.3
- Protein CHROMOSOME TRANSMISSION FIDELITY 7
- Structural maintenance of chromosomes protein 1
- Sister chromatid cohesion 1 protein 4
- Eukaryotic translation initiation factor 2 subunit alpha homolog
Sequence:
MSDSDKELENQIIEAGEKLIDPPSSLDELLSFLDKLFVSLAEVEQSPPDSMQNALTPLMKGLVGGKLFKHSDVDVKVAVAACISEITRITAPDAPYDDDQMKEVFKLIVSSFEDLVDKSSRSYAKRISILETVAKVRSCVVMLDLECDALLIEMFQHFLKAIRDHHSGNVFSSMENIMTLVLEESEDIPSEMLSPILHSVKKDDEISQVSRRLAEQVLSNCASKLKTYLTEAVKSSGVPLDKYSNIVASICEGTFSALQQDQVVANEKEDSQGHIKRETEVEKAAEISTPERTDAPKDESGKSGVSNGVAQQNDSSVDTDSMKKQDDTGAKDEPQQLDNPRNTDLNNTTEEKPDVEHQIEEKENESSSVKQADLSKDSDIKEETEPAELLDSKDVLTSPPVDSSVTAATSSENEKNKSVQILPSKTSGDETANVSSPSMAEELPEQSVPKKTANQKKKESSTEEVKPSASIATEEVSEEPNTSEPQVTKKSGKKVASSSKTKPTVPPSKKSTSETKVAKQSEKKVVGSDNAQESTKPKEEKKKPGRGKAIDEESLHTSSGDNEKPAVSSGKLASKSKKEAKQTVEESPNSNTKRKRSLGQGKASGESLVGSRIKVWWPMDQAYYKGVVESYDAAKKKHLVIYDDGDQEILYLKNQKWSPLDESELSQDEEAADQTGQEEDASTVPLTKKAKTGKQSKMDNSSAKKGSGAGSSKAKATPASKSSKTSQDDKTASKSKDSKEASREEEASSEEESEEEEPPKTVGKSGSSRSKKDISSVSKSGKSKASSKKKEEPSKATTSSKSKSGPVKSVPAKSKTGKGKAKSGSASTPASKAKESASESESEETPKEPEPATKAKSGKSQGSQSKSGKKRKR
Protein: Interleukin-23 receptor (IL-23 receptor) (IL-23R) (Q8K4B4)
Organism: Mus musculus (Mouse)
Function: Associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response to infection in peripheral tissues. IL23 may be responsible for autoimmune inflammatory diseases and be important for tumorigenesis (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Interleukin-12 receptor subunit beta-1
- Interleukin-23 subunit alpha
- Tyrosine-protein kinase JAK2
- Interleukin-12 subunit beta
- Signal transducer and activator of transcription 3
- Interleukin-10
- Non-receptor tyrosine-protein kinase TYK2
- Interferon gamma
- Interleukin-22
- Interleukin-6
Sequence:
MSHLTLQLHVVIALYVLFRWCHGGITSINCSGDMWVEPGEIFQMGMNVSIYCQEALKHCRPRNLYFYKNGFKEEFDITRINRTTARIWYKGFSEPHAYMHCTAECPGHFQETLICGKDISSGHPPDAPSNLTCVIYEYSGNMTCTWNTGKPTYIDTKYIVHVKSLETEEEQQYLASSYVKISTDSLQGSRKYLVWVQAVNSLGMENSQQLHVHLDDIVIPSASIISRAETTNDTVPKTIVYWKSKTMIEKVFCEMRYKTTTNQTWSVKEFDANFTYVQQSEFYLEPDSKYVFQVRCQETGKRNWQPWSSPFVHQTSQETGKRNWQPWSSPFVHQTSQTVSQVTAKSSHEPQKMEMLSATIFRGHPASGNHQDIGLLSGMVFLAIMLPIFSLIGIFNRSLRIGIKRKVLLMIPKWLYEDIPNMENSNVAKLLQEKSVFENDNASEQALYVDPVLTEISEISPLEHKPTDYKEERLTGLLETRDCPLGMLSTSSSVVYIPDLNTGYKPQVSNVPPGGNLFINRDERDPTSLETTDDHFARLKTYPNFQFSASSMALLNKTLILDELCLVLNQGEFNSLDIKNSRQEETSIVLQSDSPSETIPAQTLLSDEFVSCLAIGNEDLPSINSYFPQNVLESHFSRISLFQK
Protein: Collagen type XI alpha 2 chain (F6T0B3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Procollagen C-endopeptidase enhancer 1
- Collagen beta
Sequence:
MERCSRCHRLLLLLPLVLGLSAAPGWAGAPSVDVLRALRFPSLPDGVRKSKGVCPADVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRSGLQAPLLTLYSAQGVQQLGLELGRPVRFLYEDQRGRPQASAQPIFRGLSLADGKWHHVAVAVKGQSVTLIVDCKKRVTRPLPRSVHPVLDTHGVVIFGAHVLDDEVFEGDVQELLIVPGVQAAYQSCGQKDLECEREQRDGPQTQKPHRAQRSPKKEPARLHKPQNQEPQQQVAHGPRGLKGEKGEPAVLEPGMFVEGPPGPEGPAGLAGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGPPGPPGTSLMLPFRFGSSGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGARGMPGEPGVKGDRGFDGLPGLPGEKGQRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPHGPKGSLGPQGEPGPPGQQGTPGTQGLPGPQGAIGPHGEKGPRGKPGLPGMPGSDGLPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGEKGEDGFPGFKGDIGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPTGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPPGPAGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGAAGESGPMGERGHPGPPGPPGEQGLPGTAGKDGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPAGPPGPAGSPGERGAAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGTKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPFGEKGETGDVGPMGPPGPPGPRGPAGPNGADGPQGPPGGVGNLGPPGEKGEPGESGSPGVQGEPGVKGPRGERGEKGESGQAGEAGPPGPKGPTGDDGPKGNPGPVGFPGDPGPPGEAGPRGQDGAKGSQGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGTPGPEGRQGEKGAKGDPGAVGAPGKTGPVGPAGPAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDAGAKGEKGHPGLIGLIGPTGEQGEKGDRGLPGPQGSPGQKGETGIPGASGPIGPGGPPGLPGPSGPKGAKGATGPAGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSKLMQDEEATPTGGAPGSPAGLEEIFGSLDSLREEIEQMRRPTGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGVSQDGPLKLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPTRRGGVLLGPVCFMG
Protein: Aspartyl aminopeptidase (EC 3.4.11.21) (Q54M70)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Likely to play an important role in intracellular protein and peptide metabolism.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Uncharacterized protein DDB_G0289357
- Uncharacterized protein DDB_G0286393
- RBR-type E3 ubiquitin transferase
- Cellular retinaldehyde-binding/triple function domain-containing protein
- Alpha-mannosidase G
Sequence:
MEQYLPQAKEFISFIDKSPSPYHAVQYFSEILKSKGFIHLSEKQMWDIQPNKKYFFTRNQSCISAFAVGGKYKPGNGFNIAAAHTDSPNFKVRPVSKVESVGYQQVGVETYGGGLWYTWFDRDLTVAGRVIVKSGDGSYESKLVHIKKPILRIPSLAIHLDRSVNTDGFKYNTQNHLVPMIASKLSEPVESKSTTTTTTTESPKTSDPQDVNSSTTKHHAVLLELLSKELGCSVGDIQNFDLSVCDTQPAAIGGALDEFIFSPRCDNLGMSYCAMIGLLNVKESTLAQEENVLNVILFDNEEVGSSSPQGACAPLINDTISRVNSSMFASTCKPHELNNFIDLTLRNSFLISADMAHAIHPNYTANHEPLHRPALNKGPVIKYNANLRYASNGPTSFVILDICKKNGIPIQEFLVKNDSPCGSTIGPIISGTYGIRTVDIGNPQLSMHSIRETCGVADITHGINLIQKYFEQFTKLDIIKSDLE
Protein: MAP kinase kinase PBS2 (EC 2.7.12.2) (Polymyxin B resistance protein 2) (Suppressor of fluoride sensitivity 4) (P08018)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Seems to phosphorylate HOG1 on a tyrosine residue.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- High osmolarity signaling protein SHO1
- Serine/threonine-protein kinase STE11
- Mitogen-activated protein kinase HOG1
- MAP kinase kinase kinase SSK2
- Serine/threonine-protein kinase SSK22
- Osmolarity two-component system protein SSK1
- Phosphorelay intermediate protein YPD1
- Osmosensing histidine protein kinase SLN1
- NAP1-binding protein 2
- Protein phosphatase 2C homolog 1
Sequence:
MEDKFANLSLHEKTGKSSIQLNEQTGSDNGSAVKRTSSTSSHYNNINADLHARVKAFQEQRALKRSASVGSNQSEQDKGSSQSPKHIQQIVNKPLPPLPVAGSSKVSQRMSSQVVQASSKSTLKNVLDNQETQNITDVNINIDTTKITATTIGVNTGLPATDITPSVSNTASATHKAQLLNPNRRAPRRPLSTQHPTRPNVAPHKAPAIINTPKQSLSARRGLKLPPGGMSLKMPTKTAQQPQQFAPSPSNKKHIETLSNSKVVEGKRSNPGSLINGVQSTSTSSSTEGPHDTVGTTPRTGNSNNSSNSGSSGGGGLFANFSKYVDIKSGSLNFAGKLSLSSKGIDFSNGSSSRITLDELEFLDELGHGNYGNVSKVLHKPTNVIMATKEVRLELDEAKFRQILMELEVLHKCNSPYIVDFYGAFFIEGAVYMCMEYMDGGSLDKIYDESSEIGGIDEPQLAFIANAVIHGLKELKEQHNIIHRDVKPTNILCSANQGTVKLCDFGVSGNLVASLAKTNIGCQSYMAPERIKSLNPDRATYTVQSDIWSLGLSILEMALGRYPYPPETYDNIFSQLSAIVDGPPPRLPSDKFSSDAQDFVSLCLQKIPERRPTYAALTEHPWLVKYRNQDVHMSEYITERLERRNKILRERGENGLSKNVPALHMGGL
Protein: Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2'] (A0A6M3G9R1)
Organism: Pangolin coronavirus
Subcellular location: Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000256|ARBA:ARBA00034689, ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04099}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04099}. Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000256|HAMAP-Rule:MF_04099}.
Interaction partners:
Sequence:
MLFFFFLHFALVNSQCVNLTGRAAIQPSFTNSSQRGVYYPDTIFRSNTLVLSQGYFLPFYSNVSWYYALTKTNSAEKRVDNPVLDFKDGIYFAATEKSNIVRGWIFGTTLDNTSQSLLIVNNATNVIIKVCNFQFCYDPYLSGYYHNNKTWSTREFAVYSSYANCTFEYVSKSFMLDIAGKSGLFDTLREFVFRNVDGYFKIYSKYTPVNVNSNLPIGFSALEPLVEIPAGINITKFRTLLTIHRGDPMPNNGWTVFSAAYYVGYLAPRTFMLNYNENGTITDAVDCALDPLSEAKCTLKSLTVEKGIYQTSNFRVQPTESIVRFPNITNLCPFGEVFNATTFASVYAWNRKRISNCVADYSVLYNSTSFSTFKCYGVSPTKLNDLCFTNVYADSFVVRGDEVRQIAPGQTGRIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFHPTNGVGYQPYRVVVLSFELLKAPATVCGPKQSTNLVKNKCVNFNFNGLTGTGVLTESSKKFLPFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLIGAEHVNNTYECDIPIGAGICASYQTQTNSRSVSSQAIIAYTMSLGAENSVAYANNSIAIPTNFTISVTTEILPVSMTKTSVDCTMYICGDSIECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGFNFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQSAPHGVVFLHVTYVPSQEKNFTTTPAICHEGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGSCDVVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYIWLGFIAGLIAIIMVTIMLCCMTSCCSCLKGCCSCGSCCKFDEDDSEPVLKGVKLHYT
Protein: RNA-binding (RRM/RBD/RNP motifs) family protein (F4HUQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Endoplasmic reticulum vesicle transporter protein
- RNA-binding protein BRN1
- Vesicle-associated protein 2-1
- Bifunctional TENA-E protein
- Uncharacterized protein At4g14342
- Vesicle-associated membrane protein 724
- Eukaryotic aspartyl protease family protein
- Serine/threonine-protein kinase/endoribonuclease IRE1a
- Transport/golgi organization-like protein
- Vesicle-associated membrane protein 714
Sequence:
MAYHSIPSSGFHYLNSPFGDTTFTKVFVGGLAWETQSETLRRHFDQYGDILEAVVITDKNTGRSKGYGFVTFRDPEAARRACVDPTPIIDGRRANCNLASLGRSRPPMQYAVIPHAPGRVRPPSPYVGSVQSPRGLHFGSHPYHQPPTYNYQQGVVYPYGVTPYGPDYMYSQSQGFYGPYMGQQYLQVYGVPGAVNSPGYQYGQLSHTIPGAHGYTAGQGYSHPGSHVLQLGATSPMSAIQSPYPSPSAPTHQRVIVQTPPQYIQSSGSDQTTG
Protein: VQ motif-containing protein 9 (AtVQ9) (Q9M9F0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as a negative regulator of salt stress response. Functions as repressor of WRKY8 transcription factor by decreasing the DNA-binding activity of WRKY8 and acts antagonistically with WRKY8 to regulate sodium and potassium homeostasis under salt stress.
Subcellular location: Nucleus {ECO:0000269|PubMed:23451802}.
Interaction partners:
- WRKY transcription factor 8
- VQ motif-containing protein 29
- Calmodulin-binding protein 25
- Sigma factor binding protein 2, chloroplastic
- Sigma factor binding protein 1, chloroplastic
- VQ motif-containing protein 22
- VQ motif-containing protein 8, chloroplastic
- VQ motif-containing protein 18
- VQ motif-containing protein 20
- VQ motif-containing protein 19
Sequence:
MDKSCNSSGDSSAVSASATSSTGNNTTNRDHYLRQLNKLSHKISKPTNSSSSVSVANREIDLPPPPPLQINQGNLHQHQPPVYNINKNDFRDVVQKLTGSPAHERISAPPQQPIHHPKPQQSSRLHRIRPPPLVHVINRPPGLLNDALIPQGSHHMNQNWTGVGFNLRPTAPLSPLPPLPPVHAAAESPVSSYMRYLQNSMFAIDSNRKEFSGLSPLAPLVSPRWYQQQENAPPSQHNSFPPPHPPPPSSAVSQTVPTSIPAPPLFGCSSSPKSPYGLLSPSILLSPSSGQLGFPVSPTTVPLPSPKYKGH
Protein: Diphthine methyltransferase (EC 3.1.1.97) (Diphthamide biosynthesis protein 7) (WD repeat-containing protein rrt2) (O74865)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate in diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (eft201 and eft202).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Diphthine--ammonia ligase
- Diphthine methyl ester synthase
- Diphthamide biosynthesis protein 4
- 2-
- 2-
- Diphthamide biosynthesis protein 3
Sequence:
MSETGIIPKSTDYTDWPADVCKYSQVFEDVLVVGTYMLDESTKLRHGKLVLYDTKEDVLKRVFDMHCDAILDFKWSPHDASVLAVAHSTGHVSFYRHQFRAELMFLRGIKVADSSVLMLSLDFSDSGKELAVSMSNGSVLIIDIDSGVIKNKWKEHDYEAWTCHYSRQDNNLLYSGGDDAALVCYDQRIPNSCIWRDIQVHHSGVVSILSRAPFGPYIATGEYGDFMHTLDTRNIGKPLFSANLGGGVWRLEHMETTENYHKVLGILMHRGAQVLRISNDFSSIDASKRIFKEHESMCYGGDWRHTDGLLATCSFYDKRVCLWEDI
Protein: Seed storage protein (Q9M4Q7)
Organism: Ricinus communis (Castor bean)
Interaction partners:
Sequence:
QGQSRRDQHQKVRQIREGDVIALHAGVAQWIYNNGRSPLVLVQIIDTSNPANQLDQNHRDFFLAGNPQREVQSQRGERGRTSERRSTSTGSAHDNSGNVFSGMDERVIAESFNINTDLARKLRGENDLRGIIVSVEHDLEMLAPQRSQEEEREEREEEAQRQLERSPRARFNGLEETFCTRRLRHNINKPSEADIYNPRAGRVTSVNSHNLPILRYLQLSIQKAVLYKNALMTPHWNINAHSIRYITRGSGRVQIVNENGDSVFDGQVQRGQMFTVPQNFVVITKASNEGLEWVSFKTNDNAKINQLAGRVSAIRSMPEEVVANAFQVSVEDARRLKDNRQEVTLLSPGSRST
Protein: Beta-crystallin A3 [Cleaved into: Beta-crystallin A3, isoform A1, Delta4 form; Beta-crystallin A3, isoform A1, Delta7 form; Beta-crystallin A3, isoform A1, Delta8 form] (P14881)
Organism: Rattus norvegicus (Rat)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Alpha-crystallin A chain
- Filensin
- Alpha-crystallin B chain
- Beta-crystallin B1
- Gap junction alpha-8 protein
Sequence:
METQTVQRELETLPTTKMAQTNPMPGSMGPWKITIYDQENFQGKRMEFTSSCPNVSERSFDNVRSLKVECGAWIGYEHTSFCGQQFILERGEYPRWDAWSGSNAYHIERLMSFRPICSANHKESKITIFEKENFIGRQWEICDDYPSLQAMGWFNNEVGSMKIQCGAWVCYQYPGYRGYQYILECDHHGGDYKHWREWGTHAQTSQIQSIRRIQQ
Protein: Nitrate/nitrite transporter NrtP (Nitrate/nitrite permease) (B1XLL7)
Organism: Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
Function: High-efficiency transport system for both nitrate and nitrite.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:10572142}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nitrate reductase
- Nitrite reductase
- Sulfonate/nitrate transport system ATP-binding protein
- Glutamine synthetase
Sequence:
MLGEMWSFNGRYKILHMTWFAFFLSFVVWFNFPPFATTIAQDFGLDKAQLGTIGLCNVALTVPARIIIGMLLDKYGPRLTYSLLLIYAAVPCLIFATAQSFNQLVLGRLLMGIVGAGFVIGIRMVAEWFPPKDVGTAEGIYGGWGNFGSAFSAFTMVIFGIILAFLPGAFNFGQPESFKILFFPEFNTAILNWRAAIAGTGIIAALYGMLYYFSVSDTPPGKTYHRPKSARGMEVTTKKDFWFLLAMNLPLTLILMVLAWRLQKVNFLNGTGFAIAILALVGLYLFQTYNCWTVNKDLMTGKKRYAPEDRYEFSQVAILELTYIVNFGSELAVVTMLPAFFEGTFSLDKATAGIIASSYAFMNLMSRPGGGLISDKMGSRKWTMVVLTVGMGVGYLLMSSVAGTWPLAIAVLLTMACSFFVQAAEGSTFAIVPLVKRRITGQIAGNVGAYGNVGAVAYLTVLLLLTEASAGANGGEPVMATVNAGFFQVLGITGLIVAFLCAFFLKEPKGSFAEFHEGETEMTATPPIEEEATY
Protein: dTDP-D-glucose 4,6-dehydratase (EC 4.2.1.46) (O95455)
Organism: Homo sapiens (Human)
Interaction partners:
- UDP-glucose 6-dehydrogenase
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Mannose-1-phosphate guanylyltransferase regulatory subunit alpha
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit epsilon
- Galactose-1-phosphate uridylyltransferase
- Interleukin-11 receptor subunit alpha
- UDP-glucose--hexose-1-phosphate uridylyltransferase
- Integral membrane protein GPR180
Sequence:
MSAACWEEPWGLPGGFAKRVLVTGGAGFIASHMIVSLVEDYPNYMIINLDKLDYCASLKNLETISNKQNYKFIQGDICDSHFVKLLFETEKIDIVLHFAAQTHVDLSFVRAFEFTYVNVYGTHVLVSAAHEARVEKFIYVSTDEVYGGSLDKEFDESSPKQPTNPYASSKAAAECFVQSYWEQYKFPVVITRSSNVYGPHQYPEKVIPKFISLLQHNRKCCIHGSGLQTRNFLYATDVVEAFLTVLKKGKPGEIYNIGTNFEMSVVQLAKELIQLIKETNSESEMENWVDYVNDRPTNDMRYPMKSEKIHGLGWRPKVPWKEGIKKTIEWYRENFHNWKNVEKALEPFPV
Protein: Non-histone chromosomal protein HMG-17 (High mobility group nucleosome-binding domain-containing protein 2) (P18437)
Organism: Rattus norvegicus (Rat)
Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Cytoplasmic enrichment upon phosphorylation. {ECO:0000250}.
Interaction partners:
- FAU ubiquitin like and ribosomal protein S30 fusion like 2
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL4
- Elongation factor Tu, mitochondrial
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL9m
Sequence:
MPKRNAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKDANNPAEDGDAKTDQAQKADGAGDAK