wanglab/gogpt-training-data huggingface dataset:
Protein: RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.31) (Heme-oxidized IRP2 ubiquitin ligase 1 homolog) (HOIL-1) (RING-type E3 ubiquitin transferase HOIL-1) (UbcM4-interacting protein 28) (Ubiquitin-conjugating enzyme 7-interacting protein 3) (Q9WUB0)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.
Interaction partners:
- Sharpin
- E3 ubiquitin-protein ligase RNF31
- NF-kappa-B essential modulator
- Tumor necrosis factor receptor superfamily member 1A
- Tumor necrosis factor
- Baculoviral IAP repeat-containing protein 3
- Baculoviral IAP repeat-containing protein 2
- Receptor-interacting serine/threonine-protein kinase 1
- TNF receptor-associated factor 2
- Spermatogenesis-associated protein 2
Sequence:
MDEKTKKAEEMALSLARAVAGGDEQAAIKYATWLAEQRVPLRVQVKPEVSPTQDIRLCVSVEDAYMHTVTIWLTVRPDMTVASLKDMVFLDYGFPPSLQQWVVGQRLARDQETLHSHGIRRNGDGAYLYLLSARNTSLNPQELQRQRQLRMLEDLGFKDLTLQSRGPLEPVLPKPRTNQEPGQPDAAPESPPVGWQCPGCTFINKPTRPGCEMCCRARPETYQIPASYQPDEEERARLAGEEEALRQYQQRKQQQQEGNYLQHVQLEQRSLVLNTEPTECPVCYSVLAPGEAVVLRECLHTFCRECLQGTIRNSQEAEVACPFIDSTYSCPGKLLEREIRALLSPEDYQRFLDLGVSIAENRSTLSYHCKTPDCRGWCFFEDDVNEFTCPVCTRVNCLLCKAIHEHMNCREYQDDLALRAQNDVAARQTTEMLKVMLQQGEAMHCPQCRIVVQKKDGCDWIRCTVCHTEICWVTKGPRWGPGGPGDTSGGCRCRVNGIPCHPSCQNCH
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I5ZLB3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPQAAYCYLRVVGRGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCEGGDLYRKLKEQKGQLLPESQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHSDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPKVYSAELAELIRTMLSRRPEERPSVRSILRQPYIKHHISLFLEATKAKTSKNNVKNCDSRAKPVAAVVSRKEEPNHEMIPYQPRSSEGSAVHATGEDKCLSQEKPVDIGPLKSPASLEGHTGKQDMNRTAESCATVSRINIDILPAERRDSAKDGTVEEGRPQHVDASNEVDRQCSISQEKERLQGNSKSSDQPENLLPRWSSGGGDGEGNELVKLLYSSGKDQKPQQDQVTSGCILEDQDSIHPRLQPHSSVSEPSLSRQRRQRKREQTNHGRAKSQLQESPPRLVPSHPDTGKADIISTQQSDGNQSGPVARSVNGSRSSSTASSKDRPLSARERRRLKQSQEEMLPSGPAVQRTPSSVEPVKPQEEDQPIPAQRFSSDCNITQVNPTLLREKKRLIHGLSEDELSSSTSSTDKSDGDSREGKSHTNEMRDLVQLMTQTLRLEAKESCEDLHVPNPGSEFRLHRKYRDTLVLHGKAAEEGEPPCVELPPGEWFVLSQGQSRHRVDSKAHTCKLFALFIWMLPKRCIL
Protein: LHFPL tetraspan subfamily member 5b (B0UYJ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Protocadherin-15
- Transmembrane channel-like protein 1
- Calcium and integrin-binding family member 2
- Protocadherin-related 15b.
- Harmonin
- Transmembrane inner ear.
- Transmembrane channel-like protein 2-B
- Cadherin-related 23.
- Myosin VIIAa
Sequence:
MAKEKMLPAQEAAKIYHTNYVRNSRAIGVMWAVFTLFFAIITVVVFIQPYWIGDSVNTPQAGYFGLFRYCIGNPITSELVCKGSVFDFGSIPSGAFRTALFFVGTSMLLIVGTIVCLGLFFFCNAASVYKICAWMQTSSAVLMVMGCMIYPDGWDSAEVKRMCGERTTKYNLGNCTIRWAYILGIISILDAGLLALLAFTLGNRQDKLLPDDFEVEGENNA
Protein: chitinase (EC 3.2.1.14) (Q6FJ23)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- chitinase
- chitin deacetylase
- Protein DSE1
- Candida glabrata strain CBS138 chromosome D complete sequence
- Antagonist of mitotic exit network protein 1
Sequence:
MIQILLPLLFILSTVFAFDINSKTNVAVYWGQNSAGSQKSLASYCQNTEADIFLLSFMNSFPAIGLNFADACTTTFPDGLLQCSQIAEDIKTCQSLGKKVLLSMGGASGAYGFADDAQAEAFATTLWNTFGEGSDISVERPFGQSIVDGFDFDIENNNGKGYAALVSKLRQLFSNGSKQYYISAAPQCPYPDASVGDLLANADVDFAFIQFYNNYCNVEAQFNWDDWKNFAINTSPNKNIKLYLGLPGAPSAAGSGYISNLDNLSKVIKEISSLANFGGISLWDASQATSNVIDGADYLSQMKNILKSAAGSTETPTTSSSYSMPSNLITNTGEQSSSVLVSSVERTTTTLEPTSIISSSSFSDSAPTPTNSHITTTLQPNTNTPPAAAQDSSANVQVSVTPSTTTTTPDSPSNHLNDVSPTPSTPAPSSPANPSPDTPAHTIAKQLNAQYAAGQFNGKSSCQDGELSCSADGKFAMCAHGSWVEMACAAGTTCYAYDSGNSVFTQCNYVDLKASFV
Protein: PR domain zinc finger protein 5 (EC 2.1.1.-) (PR domain-containing protein 5) (Q9CXE0)
Organism: Mus musculus (Mouse)
Function: Sequence-specific DNA-binding transcription factor. Represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1. Regulates hematopoiesis-associated protein-coding and microRNA (miRNA) genes (By similarity). May regulate the expression of proteins involved in extracellular matrix development and maintenance, connective tissue components and molecules regulating cell migration and adhesion. May cause G2/M arrest and apoptosis in cancer cells (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MLGMYVPDRFALKSSRVQDGMGLYTARRVRKGEKFGPFAGEKRMPEDLDENMDYRLMWEVRGSKGEVLYILDATNPRHSNWLRFVHEAPSQERKNLAAIQEGENIFYLAVDDIETDTELLIGYLDSDVEAEEEEQQALTMTKEGKVDHSKGQLAAGSKGHLGCEEDFACPQCESSFPSEEVLTEHLQSLHQKPTGEKEFKCENCGKKFPVRQALQRHFEQHRKACRGEARFVCKADSCGKRLKSKDALRRHQENVHTGDPKRKLICSVCNRKCTSVSSLQEHRKIHEIFDCQECMKKFISANQLKRHMITHSEKRPYNCEICNKSFKRLDQVGAHKVIHSEDKPYQCKLCGKGFAHRNVYKNHKKTHSEERPFQCDACKALFRTPFSLQRHLLIHNSERTFKCHHCDATFKRKDTLNVHVQVVHERHKKYRCELCNKAFVTPSVLRSHKKTHTGEKEKVCPYCGQKFASSGTLRVHIRSHTGERPYQCPYCEKGFSKNDGLKMHIRTHTREKPYQCSECSKAFSQKRGLDEHKRTHTGEKPFQCDVCDLAFSLKKMLIRHKMTHNPNRPMAECHFCHKKFTRNDYLKVHMDNIHGVADS
Protein: HTH-type transcriptional regulator (Q8LE56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 6,7-dimethyl-8-ribityllumazine synthase
- At3g03280
- 6,7-dimethyl-8-ribityllumazine synthase
- Emb|CAB85509.1
- At3g10120
- Uncharacterized protein At5g17350
- D-ribose-binding periplasmic protein
- At1g64700
- At3g61920
- Basic-leucine zipper transcription factor K
Sequence:
MGICSSSESTQVATAKLILQDGRMMEFANPVKVGYVLLKYPMCFICNSDDMDFDDAVAAISADEELQLGQIYFALPLCWLRQPLKAEEMAALAVKASSALMRGGGGGCRRKCVEPIVSDKLRMRVGSGDDTVGSGSGRRKVRNGDGGGSVSSSRRRKCYAAELSTIDE
Protein: Aquaporin PIP2-3 (Plasma membrane intrinsic protein 2-3) (ZmPIP2-3) (ZmPIP2;3) (Q9ATM7)
Organism: Zea mays (Maize)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAKQDIEASGPEAGEFSAKDYTDPPPAPLIDADELTKWSLYRAVIAEFIATLLFLYITVATVIGYKHQTDAAASGPDAACGGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLVRALLYIIAQCLGAICGVGLVKGFQSAYYVRYGGGANELSDGYSKGTGLAAEIIGTFVLVYTVFSATDPKRSARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSLGAAVIYNKDKAWDDQWIFWVGPLIGAAIAAAYHQYVLRASATKLGSYRSNA
Protein: Protein HEAT INTOLERANT 4 (A2RVJ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein required for basal thermotolerance, especially during heat-induced chromocentre decondensation, thus regulating transcriptional gene silencing (TGS).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:23408827, ECO:0000269|PubMed:25329561}. Nucleus, nucleolus {ECO:0000269|PubMed:25329561}. Note=Localizes to the chromocentre at 23 degrees Celsius, a condensed heterochromatin domain that harbors repetitive elements for which transcription is normally suppressed by transcriptional gene silencing (TGS) (PubMed:23408827, PubMed:25329561). Relocates from the chromocenter to the nucleolus in response to heat (30 hours at 37 degrees Celsius or 30 minutes at 44 degrees Celsius), before heat-induced decondensation of chromocenters occurs (PubMed:25329561). {ECO:0000269|PubMed:23408827, ECO:0000269|PubMed:25329561}.
Interaction partners:
- Helicase protein MOM1
Sequence:
MKKGAKRKGVSKAGRKAAVAETQNDEVIEETTKTTQEESQQHEEEVVDEVKENGEEEEAKGDQEEEEDAKPDSLEEDEENQEDEVKAEEVKEEVEKKPVARRGGKRKRATKKDTEIKDEKKPVPKAKKPRAAKVKEEPVYFEEKRSLEDLWKVAFPVGTEWDQLDALYEFNWDFQNLEEALEEGGKLYGKKVYVFGCTEPQLVPYKGANKIVHVPAVVVIESPFPPSDKIGITSVQREVEEIIPMKKMKMDWLPYIPIEKRDRQVDKMNSQIFTLGCTQRRSALRHMKEDQLKKFEYCLPYFYQPFKEDELEQSTEVQIMFPSEPPVVCEFDWEFDELQEFVDKLVEEEALPAEQADEFKEYVKEQVRAAKKANREAKDARKKAIEEMSEDTKQAFQKMKFYKFYPQPSPDTPDVSGVQSPFINRYYGKAHEVL
Protein: Apoptin (Q99152)
Organism: Chicken anemia virus (isolate Germany Cuxhaven-1) (CAV)
Function: May act as transcriptional regulator. Induces apoptosis in infected cells. Element of infectious replication cycle.
Subcellular location: Host nucleus. Note=Host nucleus of infected cells.
Interaction partners:
Sequence:
MNALQEDTPPGPSTVFRPPTSSRPLETPHCREIRIGIAGITITLSLCGCANARAPTLRSATADNSESTGFKNVPDLRTDQPKPPSKKRSCDPSEYRVSELKESLITTTPSRPRTAKRRIRL
Protein: Elongation factor 1-alpha (EF-1-alpha) (EC 3.6.5.-) (50 kDa actin-binding protein) (ABP-50) (P0CT31)
Organism: Dictyostelium discoideum (Social amoeba)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. It is also an abundant actin filament bundling protein.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase domain-containing protein
- GTP-binding nuclear protein Ran
- Elongation factor 1-beta
- Small ribosomal subunit protein eS30
- Eukaryotic peptide chain release factor subunit 1
- Sulfate adenylyltransferase
- Heat shock factor-type DNA-binding domain-containing protein
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL10
Sequence:
MGKEKTHINIVVIGHVDAGKSTTTGHLIYKCGGIDKRVIEKYEKEASEMGKQSFKYAWVMDKLKAERERGITIDIALWKFETSKYYFTIIDAPGHRDFIKNMITGTSQADCAVLVIASPTGEFEAGIAKNGQTREHALLAYTLGVKQMIVAINKMDEKSTNYSQARYDEIVKEVSSFIKKIGYNPEKVAFVPISGWNGDNMLERSDKMEWYKGPTLLEALDAIVEPKRPHDKPLRIPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPAGLSTEVKSVEMHHEQLPEARPGDNVGFNVKNVSVKEIKRGMVAGDSKNDPPQETEKFVAQVIVLNHPGQIHAGYSPVLDCHTAHIACKFTEIVDKVDRRTGAVVAKEGTAAVVLKNGDAAMVELTPSRPMCVESFTEYPPLGRFAVRDMRQTVAVGVIKSTVKKAPGKAGDKKGAAAPSKKK
Protein: Atlastin-1 (EC 3.6.5.-) (Spastic paraplegia 3A homolog) (Q6PST4)
Organism: Rattus norvegicus (Rat)
Function: GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate Golgi biogenesis. May regulate axonal development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14506257}; Multi-pass membrane protein {ECO:0000269|PubMed:14506257}. Golgi apparatus membrane {ECO:0000269|PubMed:14506257}; Multi-pass membrane protein {ECO:0000269|PubMed:14506257}. Cell projection, axon {ECO:0000269|PubMed:16537571}. Note=Localizes to endoplasmic reticulum tubular network. {ECO:0000250|UniProtKB:Q8BH66}.
Interaction partners:
- Receptor expression-enhancing protein
- Spastin
- NIPA magnesium transporter 1
- Spartin
- Reticulon-2
- Receptor expression-enhancing protein.
- Reticulon-3
- ADP-ribosylation factor like GTPase 6 interacting protein 1
- Protrudin
- SPG11 vesicle trafficking associated, spatacsin
Sequence:
MAKSRRDRNSWGGFSEKSSDWSSEEEEPVRKAGPVQVLIVKDDHSFELDEAALNRILLSEAVRDKEVVAVSVAGAFRKGKSFLMDFMLRYMYNQESVDWVGDYNEPLTGFSWRGGSERETTGIQIWSEVFLINKLDGKKVAVLLMDTQGTFDSQSTLRDSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTEYGRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLEKRLKVSGNQHEELQNVRKHIHSCFTNISCFLLPHPGLKVATNPNFDGKLKEIDDEFIKNLKILIPWLLSPESLDIKEINGNKITCRGLLEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVATAKDTYNKKMEEICGGDKPFLAPNDLQTKHLQLKEDSVKLFRGVKKMGGEEFSRRYLQQLESEIDELYIQYIKHNDSKNIFHAARTPATLFVVIFITYVIAGVTGFIGLDIIASLCNMIMGLTLITLCTWAYIRYSGEYRELGAVIDQVAAALWDQGSTNEALYKLYSAAATHRHLYQQAFPAPKSEPTEQPEKKKI
Protein: Multifunctional non-homologous end joining protein LigD (NHEJ DNA polymerase) [Includes: 3'-phosphoesterase (3'-ribonuclease/3'-phosphatase); DNA ligase D (LigD) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]); DNA repair polymerase (Pol) (Polymerase/primase)] (Q9I1X7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: With Ku probably forms a non-homologous end joining (NHEJ) repair enzyme, which repairs dsDNA breaks (DSB) with reduced fidelity. Acts as a DNA ligase on singly nicked dsDNA, fills dsDNA gaps (3- or 4- nucleotide gaps, prefers a 5'-phosphate at the gap distal end, prefers dNTPs over rNTPs), has DNA-directed DNA polymerase activity (templated primer extension) and DNA-directed RNA polymerase activity, adds 1 or 2 non-templated rNTP (or less well dNTP) to ssDNA or blunt-end dsDNA (primer extension). Has 3' resection activity, removing 3'-rNMPs from DNA using its 3'-ribonuclease and 3'-phosphatase activities sequentially. Resection requires a 2'-OH in the penultimate nucleoside position (i.e. a ribo- not deoxyribonucleoside), although the 3'-phosphatase activity does not, and its specific activity is 16-fold higher on a DNA substrate. On appropriate substrates will extend a DNA primer to the end of the template strand and then incorporate a non-templated nucleotide.
Interaction partners:
- Non-homologous end joining protein Ku
- Beta sliding clamp
- DNA polymerase I
- Phosphoesterase
- DNA ligase])
- DNA polymerase III subunit delta'
- DNA polymerase
- DNA topoisomerase
- DUF72 domain-containing protein
- D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
Sequence:
MPSSKPLAEYARKRDFRQTPEPSGRKPRKDSTGLLRYCVQKHDASRLHYDFRLELDGTLKSWAVPKGPCLDPAVKRLAVQVEDHPLDYADFEGSIPQGHYGAGDVIVWDRGAWTPLDDPREGLEKGHLSFALDGEKLSGRWHLIRTNLRGKQSQWFLVKAKDGEARSLDRFDVLKERPDSVLSERTLLPRHGEAATPAARPARRGKSGGKTPMPEWIAPELASLVEQPPRGEWAYELKLDGYRLMSRIEDGHVRLLTRNGHDWTERLPHLEKALAGLGLQRSWLDGELVVLDEEGRPDFQALQNAFEEGRGENILYVLFDLPYHEGEDLRDVALEERRARLEALLEGRDEDPLRFSATLAEDPRDLLASACKLGLEGVIGKRLGSAYRSRRSNDWIKLKCQLRQEFVIVGYTEPKGSRRHIGALLLGLYSPDEERRLRYAGKVGSGFTAASLKKVRERLEPLAVRSSPLAKVPPARETGSVQWVRPQQLCEVSYAQMTRGGIIRQAVFHGLREDKPAREVTGERPAGPPPLRGARKASAGASRAATAGVRISHPQRLIDPSIQASKLELAEFHARYADLLLRDLRERPVSLVRGPDGIGGELFFQKHAARLKIPGIVQLDPALDPGHPPLLQIRSAEALVGAVQMGSIEFHTWNASLANLERPDRFVLDLDPDPALPWKRMLEATQLSLTLLDELGLRAFLKTSGGKGMHLLVPLERRHGWDEVKDFAQAISQHLARLMPERFSAVSGPRNRVGKIFVDYLRNSRGASTVAAYSVRAREGLPVSVPVFREELDSLQGANQWNLRSLPQRLDELAGDDPWADYAGTRQRISAAMRRQLGRG
Protein: BZIP domain-containing protein (A7SB15)
Organism: Nematostella vectensis (Starlet sea anemone)
Interaction partners:
- BZIP domain-containing protein
- BZIP domain-containing protein
- Stress-activated protein kinase JNK
- Stress-activated protein kinase JNK
- Signal transducer and activator of transcription
- BZIP domain-containing protein
- BZIP domain-containing protein
- Neural retina-specific leucine zipper protein
- BZIP domain-containing protein
- Neural retina-specific leucine zipper protein
Sequence:
LTPEEETRRKVRRQRNKVAASKCRLKRREHVKNLLKASEELESANSKLESDIACLNAEKEQLERMLDAHK
Protein: Cyclin O (D3ZHT5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Multicilin
- Cyclin-dependent kinase 2
- Deuterosome assembly protein 1
- Cyclin-A1
- Fizzy-related protein homolog
- Cyclin-A2
- Cell division cycle protein 20 homolog
Sequence:
MVTPCPASPASPASGAGRQDNHQNLRAPVKKSRRPRLRRKEPLRPLNACSLPGDSGVCDLFESPSSSSDGADSPAVSAVRDCSSLLSSAQPLTALDLQTFREYGQSCYDFRKAQENLFHPRESLARQPQVTAESRCKLLSWLLQVHRQFGLSFESLCLTVNTLDRFLLTTPVAADCFQLLGVTCLLIACKQVEVHPPRMKQLLALCGGAFSRQQLCNLECIVLHKLHFSLGAPTINFFLEHFTHSRVEAGQVEVTEALAAQTLARGVAELSLTDYAFTTYTPSLLAICCLALADRMLRHQRLMDLRLGEHPEATLLDCLGKLQKLVSINSSSLTHMLPAHIWEKCSLPQSWK
Protein: WD repeat domain-containing protein 83 (Mitogen-activated protein kinase organizer 1) (MAPK organizer 1) (Q9BRX9)
Organism: Homo sapiens (Human)
Function: Molecular scaffold protein for various multimeric protein complexes. Acts as a module in the assembly of a multicomponent scaffold for the ERK pathway, linking ERK responses to specific agonists. At low concentrations it enhances ERK activation, whereas high concentrations lead to the inhibition of ERK activation. Also involved in response to hypoxia by acting as a negative regulator of HIF1A/HIF-1-alpha via its interaction with EGLN3/PHD3. May promote degradation of HIF1A. May act by recruiting signaling complexes to a specific upstream activator (By similarity). May also be involved in pre-mRNA splicing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:38103557}. Lysosome {ECO:0000269|PubMed:38103557}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000250}.
Interaction partners:
- Splicing factor 3B subunit 4
- Pre-mRNA-processing-splicing factor 8
- Ragulator complex protein LAMTOR3
- Prolyl hydroxylase EGLN3
- G patch domain-containing protein 1
- Peptidyl-prolyl cis-trans isomerase-like 1
- Dual specificity mitogen-activated protein kinase kinase 1
- Ragulator complex protein LAMTOR2
- RNA helicase aquarius
- Mitogen-activated protein kinase 3
Sequence:
MAFPEPKPRPPELPQKRLKTLDCGQGAVRAVRFNVDGNYCLTCGSDKTLKLWNPLRGTLLRTYSGHGYEVLDAAGSFDNSSLCSGGGDKAVVLWDVASGQVVRKFRGHAGKVNTVQFNEEATVILSGSIDSSIRCWDCRSRRPEPVQTLDEARDGVSSVKVSDHEILAGSVDGRVRRYDLRMGQLFSDYVGSPITCTCFSRDGQCTLVSSLDSTLRLLDKDTGELLGEYKGHKNQEYKLDCCLSERDTHVVSCSEDGKVFFWDLVEGALALALPVGSGVVQSLAYHPTEPCLLTAMGGSVQCWREEAYEAEDGAG
Protein: Quemao, isoform C (EC 2.5.1.29) (M9PEL3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEELNIILQKTKDKSTQKEQDEILLQPFTYIQQIPGKQFRSELALAFNHWLLIPGEKLAQIGDIVQMLHNSSLLGVPVAHSIYGVASTINAANYALFLALEKVQQLDHPEATKVYTEQLLELHRGQGMEIYWRDSFTCPSESDYKLMTVRKTGGLFMLAIRLMQLFSSNKEDYSKLTAILGLYFQIRDDYCNLSLKEYTENKSFAEDLTEGKFGFPVIHAVRTQKQDKQVLHILRQRTHDIEVKKYCITLLEKLGSFQYTRKVLESLDAEARSEVARLGSNPYMDRLLNKLLSWKTSDSASITQSNQINHNNVSRSSPNQNTLNCN
Protein: General transcription and DNA repair factor IIH helicase subunit XPD/RAD3 (TFIIH subunit XPD) (EC 5.6.2.3) (DNA 5'-3' helicase RAD3) (DNA repair helicase RAD3) (RNA polymerase II transcription factor B subunit RAD3) (TFB subunit RAD3) (P06839)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/RAD3 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. XPD/RAD3 acts by forming a bridge between TFIIK and the core-TFIIH complex. Involved in the maintenance of the fidelity of DNA replication.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- General transcription and DNA repair factor IIH subunit TFB2
- General transcription and DNA repair factor IIH subunit SSL1
- DNA repair protein RAD14
- Serine/threonine-protein kinase KIN28
- Transcription initiation factor IIE subunit beta
- Transcription initiation factor IIE subunit alpha
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB/SSL2
- General transcription and DNA repair factor IIH subunit TFB1
- DNA repair protein RAD2
- General transcription and DNA repair factor IIH subunit TFB4
Sequence:
MKFYIDDLPVLFPYPKIYPEQYNYMCDIKKTLDVGGNSILEMPSGTGKTVSLLSLTIAYQMHYPEHRKIIYCSRTMSEIEKALVELENLMDYRTKELGYQEDFRGLGLTSRKNLCLHPEVSKERKGTVVDEKCRRMTNGQAKRKLEEDPEANVELCEYHENLYNIEVEDYLPKGVFSFEKLLKYCEEKTLCPYFIVRRMISLCNIIIYSYHYLLDPKIAERVSNEVSKDSIVIFDEAHNIDNVCIESLSLDLTTDALRRATRGANALDERISEVRKVDSQKLQDEYEKLVQGLHSADILTDQEEPFVETPVLPQDLLTEAIPGNIRRAEHFVSFLKRLIEYLKTRMKVLHVISETPKSFLQHLKQLTFIERKPLRFCSERLSLLVRTLEVTEVEDFTALKDIATFATLISTYEEGFLLIIEPYEIENAAVPNPIMRFTCLDASIAIKPVFERFSSVIITSGTISPLDMYPRMLNFKTVLQKSYAMTLAKKSFLPMIITKGSDQVAISSRFEIRNDPSIVRNYGSMLVEFAKITPDGMVVFFPSYLYMESIVSMWQTMGILDEVWKHKLILVETPDAQETSLALETYRKACSNGRGAILLSVARGKVSEGIDFDHQYGRTVLMIGIPFQYTESRILKARLEFMRENYRIRENDFLSFDAMRHAAQCLGRVLRGKDDYGVMVLADRRFSRKRSQLPKWIAQGLSDADLNLSTDMAISNTKQFLRTMAQPTDPKDQEGVSVWSYEDLIKHQNSRKDQGGFIENENKEGEQDEDEDEDIEMQ
Protein: Sucrase-isomaltase, intestinal [Cleaved into: Sucrase (EC 3.2.1.48); Isomaltase (EC 3.2.1.10)] (P23739)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides.
Subcellular location: Apical cell membrane; Single-pass type II membrane protein. Note=Brush border.
Interaction partners:
- Lactase/phlorizin hydrolase
- Trehalase
- Pancreatic alpha-amylase
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
Sequence:
MAKKKFSALEISLIVLFIIVTAIAIALVTVLATKVPAVEEIKSPTPTSNSTPTSTPTSTSTPTSTSTPSPGKCPPEQGEPINERINCIPEQHPTKAICEERGCCWRPWNNTVIPWCFFADNHGYNAESITNENAGLKATLNRIPSPTLFGEDIKSVILTTQTQTGNRFRFKITDPNNKRYEVPHQFVKEETGIPAADTLYDVQVSENPFSIKVIRKSNNKVLCDTSVGPLLYSNQYLQISTRLPSEYIYGFGGHIHKRFRHDLYWKTWPIFTRDEIPGDNNHNLYGHQTFFMGIGDTSGKSYGVFLMNSNAMEVFIQPTPIITYRVTGGILDFYIFLGDTPEQVVQQYQEVHWRPAMPAYWNLGFQLSRWNYGSLDTVSEVVRRNREAGIPYDAQVTDIDYMEDHKEFTYDRVKFNGLPEFAQDLHNHGKYIIILDPAISINKRANGAEYQTYVRGNEKNVWVNESDGTTPLIGEVWPGLTVYPDFTNPQTIEWWANECNLFHQQVEYDGLWIDMNEVSSFIQGSLNLKGVLLIVLNYPPFTPGILDKVMYSKTLCMDAVQHWGKQYDVHSLYGYSMAIATEQAVERVFPNKRSFILTRSTFGGSGRHANHWLGDNTASWEQMEWSITGMLEFGIFGMPLVGATSCGFLADTTEELCRRWMQLGAFYPFSRNHNAEGYMEQDPAYFGQDSSRHYLTIRYTLLPFLYTLFYRAHMFGETVARPFLYEFYDDTNSWIEDTQFLWGPALLITPVLRPGVENVSAYIPNATWYDYETGIKRPWRKERINMYLPGDKIGLHLRGGYIIPTQEPDVTTTASRKNPLGLIVALDDNQAAKGELFWDDGESKDSIEKKMYILYTFSVSNNELVLNCTHSSYAEGTSLAFKTIKVLGLREDVRSITVGENDQQMATHTNFTFDSANKILSITALNFNLAGSFIVRWCRTFSDNEKFTCYPDVGTATEGTCTQRGCLWQPVSGLSNVPPYYFPPENNPYTLTSIQPLPTGITAELQLNPPNARIKLPSNPISTLRVGVKYHPNDMLQFKIYDAQHKRYEVPVPLNIPDTPTSSNERLYDVEIKENPFGIQVRRRSSGKLIWDSRLPGFGFNDQFIQISTRLPSNYLYGFGEVEHTAFKRDLNWHTWGMFTRDQPPGYKLNSYGFHPYYMALENEGNAHGVLLLNSNGMDVTFQPTPALTYRTIGGILDFYMFLGPTPEIATRQYHEVIGFPVMPPYWALGFQLCRYGYRNTSEIEQLYNDMVAANIPYDVQYTDINYMERQLDFTIGERFKTLPEFVDRIRKDGMKYIVILAPAISGNETQPYPAFERGIQKDVFVKWPNTNDICWPKVWPDLPNVTIDETITEDEAVNASRAHVAFPDFFRNSTLEWWAREIYDFYNEKMKFDGLWIDMNEPSSFGIQMGGKVLNECRRMMTLNYPPVFSPELRVKEGEGASISEAMCMETEHILIDGSSVLQYDVHNLYGWSQVKPTLDALQNTTGLRGIVISRSTYPTTGRWGGHWLGDNYTTWDNLEKSLIGMLELNLFGIPYIGADICGVFHDSGYPSLYFVGIQVGAFYPYPRESPTINFTRSQDPVSWMKLLLQMSKKVLEIRYTLLPYFYTQMHEAHAHGGTVIRPLMHEFFDDKETWEIYKQFLWGPAFMVTPVVEPFRTSVTGYVPKARWFDYHTGADIKLKGILHTFSAPFDTINLHVRGGYILPCQEPARNTHLSRQNYMKLIVAADDNQMAQGTLFGDDGESIDTYERGQYTSIQFNLNQTTLTSTVLANGYKNKQEMRLGSIHIWGKGTLRISNANLVYGGRKHQPPFTQEEAKETLIFDLKNMNVTLDEPIQITWS