SHPRH_HUMAN
ID SHPRH_HUMAN Reviewed; 1683 AA.
AC Q149N8; Q149N9; Q5VV79; Q68DS5; Q7Z5J5; Q8IVE8; Q8IWQ9; Q8N1S8; Q8NBR7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=E3 ubiquitin-protein ligase SHPRH;
DE EC=2.3.2.27;
DE EC=3.6.4.-;
DE AltName: Full=RING-type E3 ubiquitin transferase SHPRH {ECO:0000305};
DE AltName: Full=SNF2, histone-linker, PHD and RING finger domain-containing helicase;
GN Name=SHPRH; Synonyms=KIAA2023;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP ARG-438; PHE-460 AND TYR-1028.
RX PubMed=12837266; DOI=10.1016/s0888-7543(03)00121-6;
RA Sood R., Makalowska I., Galdzicki M., Hu P., Eddings E., Robbins C.M.,
RA Moses T., Namkoong J., Chen S., Trent J.M.;
RT "Cloning and characterization of a novel gene, SHPRH, encoding a conserved
RT putative protein with SNF2/helicase and PHD-finger domains from the 6q24
RT region.";
RL Genomics 82:153-161(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Chen S., Yu L., Guo J.H.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Salivary gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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 MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-584 AND 1532-1683 (ISOFORM 1).
RC TISSUE=Corpus callosum;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-1683 (ISOFORM 4).
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH PCNA; UBE2N AND RAD18, AND
RP MUTAGENESIS OF CYS-1432.
RX PubMed=17130289; DOI=10.1083/jcb.200606145;
RA Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.;
RT "Human SHPRH suppresses genomic instability through proliferating cell
RT nuclear antigen polyubiquitination.";
RL J. Cell Biol. 175:703-708(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH UBE2N AND RAD18.
RX PubMed=17108083; DOI=10.1073/pnas.0608595103;
RA Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V.,
RA Hurwitz J., Prakash L., Prakash S., Haracska L.;
RT "Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
RT polyubiquitylation of proliferating cell nuclear antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH HLTF.
RX PubMed=18719106; DOI=10.1073/pnas.0805685105;
RA Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H.,
RA Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH
RT prevents genomic instability from stalled replication forks.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
RN [11]
RP IDENTIFICATION BY 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP VARIANT ASP-1222.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in DNA repair. Upon
CC genotoxic stress, accepts ubiquitin from the UBE2N-UBE2V2 E2 complex
CC and transfers it to 'Lys-164' of PCNA which had been monoubiquitinated
CC by UBE2A/B-RAD18, promoting the formation of non-canonical poly-
CC ubiquitin chains linked through 'Lys-63'. {ECO:0000269|PubMed:17108083,
CC ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:18719106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Interacts with HLTF, PCNA, UBE2N and RAD18.
CC {ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289,
CC ECO:0000269|PubMed:18719106}.
CC -!- INTERACTION:
CC Q149N8; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-714105, EBI-10193358;
CC Q149N8; Q8WWZ3: EDARADD; NbExp=3; IntAct=EBI-714105, EBI-2949647;
CC Q149N8-1; P61088: UBE2N; NbExp=2; IntAct=EBI-15612386, EBI-1052908;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q149N8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q149N8-2; Sequence=VSP_024753, VSP_024757, VSP_024758;
CC Name=3;
CC IsoId=Q149N8-4; Sequence=VSP_024756, VSP_024759, VSP_024762,
CC VSP_024763;
CC Name=4;
CC IsoId=Q149N8-5; Sequence=VSP_024760, VSP_024761;
CC -!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:12837266}.
CC -!- DOMAIN: The RING finger mediates E3 ubiquitin ligase activity.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI13090.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=AAI17686.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAC04459.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC23119.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=CAH18145.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY161136; AAO26201.1; -; mRNA.
DR EMBL; AY163808; AAO06907.1; -; mRNA.
DR EMBL; CR749290; CAH18145.1; ALT_FRAME; mRNA.
DR EMBL; AL356599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113089; AAI13090.1; ALT_SEQ; mRNA.
DR EMBL; BC117685; AAI17686.1; ALT_SEQ; mRNA.
DR EMBL; BC117686; AAI17687.1; -; mRNA.
DR EMBL; AK075318; BAC11544.1; -; mRNA.
DR EMBL; AK094944; BAC04459.1; ALT_INIT; mRNA.
DR EMBL; AB095943; BAC23119.1; ALT_SEQ; mRNA.
DR CCDS; CCDS43513.2; -. [Q149N8-1]
DR CCDS; CCDS47496.1; -. [Q149N8-4]
DR RefSeq; NP_001036148.2; NM_001042683.2. [Q149N8-1]
DR RefSeq; NP_775105.1; NM_173082.3. [Q149N8-4]
DR RefSeq; XP_006715504.1; XM_006715441.3.
DR PDB; 2M85; NMR; -; A=652-716.
DR PDB; 4QN1; X-ray; 2.48 A; A=1000-1418.
DR PDBsum; 2M85; -.
DR PDBsum; 4QN1; -.
DR AlphaFoldDB; Q149N8; -.
DR SMR; Q149N8; -.
DR BioGRID; 129208; 85.
DR DIP; DIP-46277N; -.
DR IntAct; Q149N8; 25.
DR MINT; Q149N8; -.
DR STRING; 9606.ENSP00000356475; -.
DR GlyGen; Q149N8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q149N8; -.
DR PhosphoSitePlus; Q149N8; -.
DR BioMuta; SHPRH; -.
DR DMDM; 146325723; -.
DR EPD; Q149N8; -.
DR jPOST; Q149N8; -.
DR MassIVE; Q149N8; -.
DR MaxQB; Q149N8; -.
DR PaxDb; Q149N8; -.
DR PeptideAtlas; Q149N8; -.
DR PRIDE; Q149N8; -.
DR ProteomicsDB; 60294; -. [Q149N8-1]
DR ProteomicsDB; 60295; -. [Q149N8-2]
DR ProteomicsDB; 60296; -. [Q149N8-4]
DR ProteomicsDB; 60297; -. [Q149N8-5]
DR Antibodypedia; 33225; 301 antibodies from 24 providers.
DR DNASU; 257218; -.
DR Ensembl; ENST00000275233.12; ENSP00000275233.7; ENSG00000146414.17. [Q149N8-1]
DR Ensembl; ENST00000367505.6; ENSP00000356475.2; ENSG00000146414.17. [Q149N8-1]
DR Ensembl; ENST00000438092.6; ENSP00000412797.2; ENSG00000146414.17. [Q149N8-4]
DR Ensembl; ENST00000519632.5; ENSP00000430528.1; ENSG00000146414.17. [Q149N8-2]
DR GeneID; 257218; -.
DR KEGG; hsa:257218; -.
DR MANE-Select; ENST00000275233.12; ENSP00000275233.7; NM_001042683.3; NP_001036148.2.
DR UCSC; uc003qle.4; human. [Q149N8-1]
DR CTD; 257218; -.
DR DisGeNET; 257218; -.
DR GeneCards; SHPRH; -.
DR HGNC; HGNC:19336; SHPRH.
DR HPA; ENSG00000146414; Low tissue specificity.
DR MIM; 608048; gene.
DR neXtProt; NX_Q149N8; -.
DR OpenTargets; ENSG00000146414; -.
DR PharmGKB; PA134880315; -.
DR VEuPathDB; HostDB:ENSG00000146414; -.
DR eggNOG; KOG0298; Eukaryota.
DR GeneTree; ENSGT00730000111123; -.
DR HOGENOM; CLU_001726_1_1_1; -.
DR InParanoid; Q149N8; -.
DR OrthoDB; 357670at2759; -.
DR PhylomeDB; Q149N8; -.
DR TreeFam; TF324273; -.
DR PathwayCommons; Q149N8; -.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR SignaLink; Q149N8; -.
DR SIGNOR; Q149N8; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 257218; 13 hits in 1133 CRISPR screens.
DR ChiTaRS; SHPRH; human.
DR GeneWiki; SHPRH; -.
DR GenomeRNAi; 257218; -.
DR Pharos; Q149N8; Tbio.
DR PRO; PR:Q149N8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q149N8; protein.
DR Bgee; ENSG00000146414; Expressed in calcaneal tendon and 179 other tissues.
DR ExpressionAtlas; Q149N8; baseline and differential.
DR Genevisible; Q149N8; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; EXP:Reactome.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:FlyBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00538; Linker_histone; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; DNA damage; DNA repair;
KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1683
FT /note="E3 ubiquitin-protein ligase SHPRH"
FT /id="PRO_0000284918"
FT DOMAIN 307..389
FT /note="Helicase ATP-binding; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 438..512
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 710..868
FT /note="Helicase ATP-binding; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1514..1672
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 658..709
FT /note="PHD-type"
FT ZN_FING 1432..1479
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 819..822
FT /note="DEAQ box"
FT COMPBIAS 7..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 373..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPQ3"
FT VAR_SEQ 46..156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_024753"
FT VAR_SEQ 442..471
FT /note="TRVMILTAVKEMNGKKGVSILSIYKYVSSI -> YPFTFSYTCDDTDSCERN
FT EWKKRSVHPFHL (in isoform 4)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_024760"
FT VAR_SEQ 472..1683
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_024761"
FT VAR_SEQ 996
FT /note="K -> KSFEQSTFSF (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024756"
FT VAR_SEQ 1039..1040
FT /note="EY -> RR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_024757"
FT VAR_SEQ 1041..1683
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_024758"
FT VAR_SEQ 1183..1187
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024759"
FT VAR_SEQ 1653..1655
FT /note="HTN -> IYI (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024762"
FT VAR_SEQ 1656..1683
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024763"
FT VARIANT 438
FT /note="Q -> R (in an ovarian cancer cell line;
FT dbSNP:rs1411096648)"
FT /evidence="ECO:0000269|PubMed:12837266"
FT /id="VAR_031857"
FT VARIANT 460
FT /note="S -> F (in a melanoma cell line)"
FT /evidence="ECO:0000269|PubMed:12837266"
FT /id="VAR_031858"
FT VARIANT 1028
FT /note="N -> Y (in a melanoma cell line)"
FT /evidence="ECO:0000269|PubMed:12837266"
FT /id="VAR_031859"
FT VARIANT 1222
FT /note="V -> D (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064750"
FT MUTAGEN 1432
FT /note="C->A: Abolishes E3 activity."
FT /evidence="ECO:0000269|PubMed:17130289"
FT CONFLICT 185
FT /note="M -> V (in Ref. 3; CAH18145)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="K -> E (in Ref. 6; BAC11544)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="E -> G (in Ref. 6; BAC11544)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="D -> G (in Ref. 3; CAH18145)"
FT /evidence="ECO:0000305"
FT CONFLICT 1398
FT /note="V -> F (in Ref. 5; AAI17687)"
FT /evidence="ECO:0000305"
FT TURN 669..671
FT /evidence="ECO:0007829|PDB:2M85"
FT STRAND 674..677
FT /evidence="ECO:0007829|PDB:2M85"
FT TURN 678..681
FT /evidence="ECO:0007829|PDB:2M85"
FT STRAND 682..685
FT /evidence="ECO:0007829|PDB:2M85"
FT HELIX 686..688
FT /evidence="ECO:0007829|PDB:2M85"
FT TURN 694..698
FT /evidence="ECO:0007829|PDB:2M85"
FT HELIX 704..710
FT /evidence="ECO:0007829|PDB:2M85"
FT HELIX 1000..1037
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1040..1056
FT /evidence="ECO:0007829|PDB:4QN1"
FT TURN 1057..1060
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1065..1080
FT /evidence="ECO:0007829|PDB:4QN1"
FT TURN 1081..1084
FT /evidence="ECO:0007829|PDB:4QN1"
FT TURN 1090..1094
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1095..1119
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1122..1133
FT /evidence="ECO:0007829|PDB:4QN1"
FT STRAND 1137..1139
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1141..1151
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1155..1166
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1180..1182
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1186..1212
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1220..1230
FT /evidence="ECO:0007829|PDB:4QN1"
FT STRAND 1234..1236
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1242..1257
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1296..1310
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1315..1359
FT /evidence="ECO:0007829|PDB:4QN1"
FT HELIX 1385..1414
FT /evidence="ECO:0007829|PDB:4QN1"
SQ SEQUENCE 1683 AA; 193079 MW; 3EAA1433EF89B232 CRC64;
MSSRRKRAPP VRVDEEKRQQ LHWNMHEDRR NEPIIISDDD EQPCPGSDTS SAHYIILSDS
LKEEVAHRDK KRCSKVVSFS KPIEKEETVG IFSPLSVKLN IVISPYHFDN SWKAFLGELT
LQLLPAQSLI ENFSERSITL MSSESSNQFL IYVHSKGEDV EKQKKEPMSI CDKGILVESS
FSGEMLEDLG WLQKKRRIKL YQKPEGNHII KVGIYLLEAG LAKLDFLSDA NSRMKKFNQL
MKKVMEKLHN SIIPDVLEED EDDPESEPEG QDIDELYHFV KQTHQQETQS IQVDVQHPAL
IPVLRPYQRE AVNWMLQQEC FRSSPATESA LHFLWREIVT SEGLKLYYNP YTGCIIREYP
NSGPQLLGGI LADEMGLGKT VEVLALILTH TRQDVKQDAL TLPEGKVVNY FIPSHYFGGK
LKKTEIQNIE FEPKEKVQCP PTRVMILTAV KEMNGKKGVS ILSIYKYVSS IYRYDVQRNR
SLLKRMLKCL IFEGLVKQIK GHGFSGTFTL GKNYKEEDIC DKTKKQAVGS PRKIQKETRK
SGNKDTDSEY LPSDTSDDDD DPYYYYYKSR RNRSKLRKKL VPSTKKGKSQ PFINPDSQGH
CPATSDSGIT DVAMSKSTCI SEFNQEHETE DCAESLNHAD SDVPPSNTMS PFNTSDYRFE
CICGELDQID RKPRVQCLKC HLWQHAKCVN YDEKNLKIKP FYCPHCLVAM EPVSTRATLI
ISPSSICHQW VDEINRHVRS SSLRVLVYQG VKKDGFLQPH FLAEQDIVII TYDVLRSELN
YVDIPHSNSE DGRRLRNQKR YMAIPSPLVA VEWWRICLDE AQMVECPTVK AAEMAQRLSG
INRWCISGTP VQRGLEDLFG LVVFLGIEPY CVKHWWVRLL YRPYCKKNPQ HLYSFIAKIL
WRSAKKDVID QIQIPPQTEE IHWLHFSPVE RHFYHRQHEV CCQDVVVKLR KISDWALKLS
SLDRRTVTSI LYPLLRLRQA CCHPQAVRGE FLPLQKSTMT MEELLTSLQK KCGTECEEAH
RQLVCALNGL AGIHIIKGEY ALAAELYREV LRSSEEHKGK LKTDSLQRLH ATHNLMELLI
ARHPGIPPTL RDGRLEEEAK QLREHYMSKC NTEVAEAQQA LYPVQQTIHE LQRKIHSNSP
WWLNVIHRAI EFTIDEELVQ RVRNEITSNY KQQTGKLSMS EKFRDCRGLQ FLLTTQMEEL
NKCQKLVREA VKNLEGPPSR NVIESATVCH LRPARLPLNC CVFCKADELF TEYESKLFSN
TVKGQTAIFE EMIEDEEGLV DDRAPTTTRG LWAISETERS MKAILSFAKS HRFDVEFVDE
GSTSMDLFEA WKKEYKLLHE YWMALRNRVS AVDELAMATE RLRVRDPREP KPNPPVLHII
EPHEVEQNRI KLLNDKAVAT SQLQKKLGQL LYLTNLEKSQ DKTSGGVNPE PCPICARQLG
KQWAVLTCGH CFCNECISII IEQYSVGSHR SSIKCAICRQ TTSHKEISYV FTSEKANQEE
DIPVKGSHST KVEAVVRTLM KIQLRDPGAK ALVFSTWQDV LDIISKALTD NNMEFAQISR
VKTFQENLSA FKRDPQINIL LLPLHTGSNG LTIIEATHVL LVEPILNPAH ELQAIGRVHR
IGQTKPTIVH RFLIKATIEE RMQAMLKTAE RSHTNSSAKH SEASVLTVAD LADLFTKETE
ELE
