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RWDD1_HUMAN
ID   RWDD1_HUMAN             Reviewed;         243 AA.
AC   Q9H446; A8K3W2; A8MT24; Q9Y313; Q9Y6B3;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=RWD domain-containing protein 1;
DE   AltName: Full=DRG family-regulatory protein 2;
GN   Name=RWDD1; Synonyms=DFRP2; ORFNames=CGI-24, PTD013;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pituitary tumor;
RA   Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA   Luo M., Chen J., Hu R.;
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-144, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   STRUCTURE BY NMR OF 1-121.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the RWD domain of human RWD domain containing
RT   protein 1.";
RL   Submitted (AUG-2007) to the PDB data bank.
CC   -!- FUNCTION: Protects DRG2 from proteolytic degradation. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DRG2. Interacts with androgen receptor (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9H446; Q9Y295: DRG1; NbExp=8; IntAct=EBI-748952, EBI-719554;
CC       Q9H446; P55039: DRG2; NbExp=8; IntAct=EBI-748952, EBI-750565;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H446-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H446-2; Sequence=VSP_044500;
CC   -!- SIMILARITY: Belongs to the RWDD1/GIR2 family. {ECO:0000305}.
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DR   EMBL; AF132958; AAD27733.1; -; mRNA.
DR   EMBL; AF092134; AAD40376.1; -; mRNA.
DR   EMBL; AK290727; BAF83416.1; -; mRNA.
DR   EMBL; AK301089; BAG62691.1; -; mRNA.
DR   EMBL; AL121953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48221.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48222.1; -; Genomic_DNA.
DR   EMBL; BC015802; AAH15802.1; -; mRNA.
DR   CCDS; CCDS34520.1; -. [Q9H446-1]
DR   CCDS; CCDS43496.1; -. [Q9H446-2]
DR   RefSeq; NP_001007465.1; NM_001007464.2. [Q9H446-2]
DR   RefSeq; NP_057036.2; NM_015952.3. [Q9H446-1]
DR   RefSeq; NP_057188.2; NM_016104.3. [Q9H446-2]
DR   PDB; 2EBM; NMR; -; A=1-121.
DR   PDBsum; 2EBM; -.
DR   AlphaFoldDB; Q9H446; -.
DR   BMRB; Q9H446; -.
DR   SMR; Q9H446; -.
DR   BioGRID; 119518; 12.
DR   DIP; DIP-34520N; -.
DR   IntAct; Q9H446; 9.
DR   STRING; 9606.ENSP00000420357; -.
DR   iPTMnet; Q9H446; -.
DR   MetOSite; Q9H446; -.
DR   PhosphoSitePlus; Q9H446; -.
DR   BioMuta; RWDD1; -.
DR   DMDM; 34098713; -.
DR   EPD; Q9H446; -.
DR   jPOST; Q9H446; -.
DR   MassIVE; Q9H446; -.
DR   MaxQB; Q9H446; -.
DR   PaxDb; Q9H446; -.
DR   PeptideAtlas; Q9H446; -.
DR   PRIDE; Q9H446; -.
DR   ProteomicsDB; 1990; -.
DR   ProteomicsDB; 80786; -. [Q9H446-1]
DR   Antibodypedia; 32499; 124 antibodies from 24 providers.
DR   DNASU; 51389; -.
DR   Ensembl; ENST00000466444.7; ENSP00000420357.2; ENSG00000111832.13. [Q9H446-1]
DR   Ensembl; ENST00000487832.6; ENSP00000428778.1; ENSG00000111832.13. [Q9H446-2]
DR   GeneID; 51389; -.
DR   KEGG; hsa:51389; -.
DR   MANE-Select; ENST00000466444.7; ENSP00000420357.2; NM_015952.4; NP_057036.2.
DR   UCSC; uc003pxc.5; human. [Q9H446-1]
DR   CTD; 51389; -.
DR   DisGeNET; 51389; -.
DR   GeneCards; RWDD1; -.
DR   HGNC; HGNC:20993; RWDD1.
DR   HPA; ENSG00000111832; Low tissue specificity.
DR   neXtProt; NX_Q9H446; -.
DR   OpenTargets; ENSG00000111832; -.
DR   PharmGKB; PA134967923; -.
DR   VEuPathDB; HostDB:ENSG00000111832; -.
DR   eggNOG; KOG4018; Eukaryota.
DR   GeneTree; ENSGT00390000009168; -.
DR   HOGENOM; CLU_084528_2_0_1; -.
DR   InParanoid; Q9H446; -.
DR   OMA; IYCGELE; -.
DR   OrthoDB; 1269244at2759; -.
DR   PhylomeDB; Q9H446; -.
DR   TreeFam; TF313662; -.
DR   PathwayCommons; Q9H446; -.
DR   SignaLink; Q9H446; -.
DR   BioGRID-ORCS; 51389; 11 hits in 1074 CRISPR screens.
DR   ChiTaRS; RWDD1; human.
DR   EvolutionaryTrace; Q9H446; -.
DR   GenomeRNAi; 51389; -.
DR   Pharos; Q9H446; Tbio.
DR   PRO; PR:Q9H446; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9H446; protein.
DR   Bgee; ENSG00000111832; Expressed in calcaneal tendon and 216 other tissues.
DR   ExpressionAtlas; Q9H446; baseline and differential.
DR   Genevisible; Q9H446; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005844; C:polysome; IBA:GO_Central.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
DR   GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   GO; GO:2000825; P:positive regulation of androgen receptor activity; IEA:Ensembl.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR040213; GIR2-like.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR12292; PTHR12292; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00591; RWD; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50908; RWD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..243
FT                   /note="RWD domain-containing protein 1"
FT                   /id="PRO_0000097540"
FT   DOMAIN          10..114
FT                   /note="RWD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT   REGION          142..197
FT                   /note="Interaction with DRG2"
FT                   /evidence="ECO:0000250"
FT   REGION          198..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..243
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         144
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   VAR_SEQ         1..96
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044500"
FT   CONFLICT        120..130
FT                   /note="TRREEEKKQKE -> LEERRKNKR (in Ref. 1; AAD27733)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139
FT                   /note="Q -> R (in Ref. 2; AAD40376)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..18
FT                   /evidence="ECO:0007829|PDB:2EBM"
FT   STRAND          20..25
FT                   /evidence="ECO:0007829|PDB:2EBM"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:2EBM"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:2EBM"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:2EBM"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:2EBM"
FT   STRAND          66..74
FT                   /evidence="ECO:0007829|PDB:2EBM"
FT   HELIX           77..94
FT                   /evidence="ECO:0007829|PDB:2EBM"
FT   HELIX           100..117
FT                   /evidence="ECO:0007829|PDB:2EBM"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:2EBM"
SQ   SEQUENCE   243 AA;  27940 MW;  A7AABD457136B4DA CRC64;
     MTDYGEEQRN ELEALESIYP DSFTVLSENP PSFTITVTSE AGENDETVQT TLKFTYSEKY
     PDEAPLYEIF SQENLEDNDV SDILKLLALQ AEENLGMVMI FTLVTAVQEK LNEIVDQIKT
     RREEEKKQKE KEAEEAEKQL FHGTPVTIEN FLNWKAKFDA ELLEIKKKRM KEEEQAGKNK
     LSGKQLFETD HNLDTSDIQF LEDAGNNVEV DESLFQEMDD LELEDDEDDP DYNPADPESD
     SAD
 
 
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