SHPRH_MOUSE
ID SHPRH_MOUSE Reviewed; 1674 AA.
AC Q7TPQ3; Q7TQ27; Q7TQ28; Q7TQ29; Q8BKE2; Q8BUW0; Q922Q3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
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 STRAIN=C57BL/6J; TISSUE=Cerebellum, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor, and Retina;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-261 AND SER-626, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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'.
CC {ECO:0000250|UniProtKB:Q149N8}.
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:0000250|UniProtKB:Q149N8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7TPQ3-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q7TPQ3-2; Sequence=VSP_024768;
CC Name=3;
CC IsoId=Q7TPQ3-3; Sequence=VSP_024766, VSP_024767;
CC Name=4; Synonyms=C;
CC IsoId=Q7TPQ3-5; Sequence=VSP_024769, VSP_024770;
CC -!- TISSUE SPECIFICITY: Broadly expressed (at protein level).
CC {ECO:0000269|PubMed:12837266}.
CC -!- DOMAIN: The RING finger mediates E3 ubiquitin ligase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO26655.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AY162264; AAO26654.1; -; mRNA.
DR EMBL; AY162265; AAO26655.1; ALT_SEQ; mRNA.
DR EMBL; AY162266; AAO26656.1; -; mRNA.
DR EMBL; AK053448; BAC35389.1; -; mRNA.
DR EMBL; AK082160; BAC38428.1; -; mRNA.
DR EMBL; BC006883; AAH06883.1; -; mRNA.
DR EMBL; BC055003; AAH55003.1; -; mRNA.
DR CCDS; CCDS35838.1; -. [Q7TPQ3-1]
DR CCDS; CCDS35839.1; -. [Q7TPQ3-2]
DR CCDS; CCDS70003.1; -. [Q7TPQ3-5]
DR RefSeq; NP_001071175.1; NM_001077707.1. [Q7TPQ3-1]
DR RefSeq; NP_001271283.1; NM_001284354.1. [Q7TPQ3-5]
DR RefSeq; NP_766525.3; NM_172937.3. [Q7TPQ3-2]
DR RefSeq; XP_006512803.1; XM_006512740.3. [Q7TPQ3-1]
DR AlphaFoldDB; Q7TPQ3; -.
DR SMR; Q7TPQ3; -.
DR BioGRID; 234474; 5.
DR IntAct; Q7TPQ3; 1.
DR STRING; 10090.ENSMUSP00000039422; -.
DR iPTMnet; Q7TPQ3; -.
DR PhosphoSitePlus; Q7TPQ3; -.
DR EPD; Q7TPQ3; -.
DR MaxQB; Q7TPQ3; -.
DR PaxDb; Q7TPQ3; -.
DR PeptideAtlas; Q7TPQ3; -.
DR PRIDE; Q7TPQ3; -.
DR ProteomicsDB; 257156; -. [Q7TPQ3-1]
DR ProteomicsDB; 257157; -. [Q7TPQ3-2]
DR ProteomicsDB; 257158; -. [Q7TPQ3-3]
DR ProteomicsDB; 257159; -. [Q7TPQ3-5]
DR Antibodypedia; 33225; 301 antibodies from 24 providers.
DR DNASU; 268281; -.
DR Ensembl; ENSMUST00000044053; ENSMUSP00000039422; ENSMUSG00000090112. [Q7TPQ3-1]
DR Ensembl; ENSMUST00000054814; ENSMUSP00000125849; ENSMUSG00000090112. [Q7TPQ3-2]
DR Ensembl; ENSMUST00000159541; ENSMUSP00000132870; ENSMUSG00000090112. [Q7TPQ3-5]
DR Ensembl; ENSMUST00000159810; ENSMUSP00000125457; ENSMUSG00000090112. [Q7TPQ3-3]
DR GeneID; 268281; -.
DR KEGG; mmu:268281; -.
DR UCSC; uc007ejp.1; mouse. [Q7TPQ3-1]
DR UCSC; uc033fop.1; mouse. [Q7TPQ3-5]
DR CTD; 257218; -.
DR MGI; MGI:1917581; Shprh.
DR VEuPathDB; HostDB:ENSMUSG00000090112; -.
DR eggNOG; KOG0298; Eukaryota.
DR GeneTree; ENSGT00730000111123; -.
DR HOGENOM; CLU_314715_0_0_1; -.
DR InParanoid; Q7TPQ3; -.
DR OMA; NTADYRF; -.
DR OrthoDB; 357670at2759; -.
DR PhylomeDB; Q7TPQ3; -.
DR TreeFam; TF324273; -.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 268281; 1 hit in 109 CRISPR screens.
DR ChiTaRS; Shprh; mouse.
DR PRO; PR:Q7TPQ3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q7TPQ3; protein.
DR Bgee; ENSMUSG00000090112; Expressed in secondary oocyte and 240 other tissues.
DR ExpressionAtlas; Q7TPQ3; baseline and differential.
DR Genevisible; Q7TPQ3; MM.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO: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; ISO:MGI.
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 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 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; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; DNA damage; DNA repair; Helicase;
KW Hydrolase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1674
FT /note="E3 ubiquitin-protein ligase SHPRH"
FT /id="PRO_0000284919"
FT DOMAIN 302..384
FT /note="Helicase ATP-binding; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 433..507
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 701..859
FT /note="Helicase ATP-binding; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1505..1663
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 649..700
FT /note="PHD-type"
FT ZN_FING 1423..1470
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 810..813
FT /note="DEAQ box"
FT COMPBIAS 7..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 368..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1030..1031
FT /note="EY -> RR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024766"
FT VAR_SEQ 1032..1674
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024767"
FT VAR_SEQ 1617..1674
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12837266"
FT /id="VSP_024768"
FT VAR_SEQ 1617..1662
FT /note="PTIVHRFLIKATIEERMQAMLKTAERSHTSSSGKHSEASVLTVAGL -> SI
FT RGLECLKTYRYTSTHDHTLSTYLVLLSI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12837266"
FT /id="VSP_024769"
FT VAR_SEQ 1663..1674
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12837266"
FT /id="VSP_024770"
FT CONFLICT 177
FT /note="S -> G (in Ref. 2; BAC38428)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="Q -> H (in Ref. 2; BAC38428)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="Q -> R (in Ref. 2; BAC38428)"
FT /evidence="ECO:0000305"
FT CONFLICT 1285
FT /note="V -> I (in Ref. 1; AAO26654/AAO26655/AAO26656)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1674 AA; 191490 MW; 2491B2F32F326393 CRC64;
MSSRRKRAPP MKVDEERQQQ LHWNMHEDLR SEPLTMTVGE QACSDADSSS DCIIIDEGPP
ESALHRDKKR RSETVSVLEA TEEETRLSVT LNVTVSPYRV DNSWKAFLGD FALQLLPKES
LVEHFSERTF TLSPSESSSQ FLIYVHSECK NVEKQENVLE GSAGVCSKGI RVESSFSSDM
LQDLAWLQKR RGIKLYQRPD GTHTIKVGIY ILEAGLTRLD FMSDAGSRMK KFNQLMKRVM
EKLHNFIIPD VLEEEEEGSE SEPEGQDIDE LYHFVKQTHQ QETRSVQVDV QHPALIPVLR
PYQREAVNWM LQQEQFRSAP PADNSLHFLW REIVTPDGLK LYYNPYTGCI IRDFPHAGPQ
LLGGILADEM GLGKTVEVLA LILTHTRQDV KQDALTLPEG KVVNYFIPTH CPREKVKNRE
IQDTEYEPKE KVHCPPTRVM ILTAVKEMNG KKGVSILSIY KYVSSIFRYD VQRNRGLLKR
MLKCLIFEGL VKQIKGHGFS GTFTLGKNYK EDVFDKTKKQ AVGSPRKIEK ELRKSVNKDA
DSEYLPSNTS DDDEPYYYYC KAGKSRSKLK KPALLTKKGK GQSVHLDSQG DAPAAGVCAS
TDVHVSENTC VSEDKQTQEA KDCAESPNPA AEELAQSNTS SPCETSDYRF ECICGEFDQI
GHKPRVQCLK CHLWQHAKCV NYEEKNLKVK PFYCPHCLVA MEPVSTRATL IISPSSICHQ
WVDEINRHVR SSSLRVLVYQ GVKKHGFLQP HFLAEQDIVI ITYDVLRSEL NYVNIPHSNS
EDGRRLRNQK RYMAIPSPLV AVEWWRICLD EAQMVECPTV KAAEMAQRLS GINRWCISGT
PVQRGLEDLF GLVVFLGIEP YCVKHWWIRL LYHPYCKKNP QHLYSFIAKI MWRSAKKDVI
DQIQIPPQTE EMHWLHFSPV ERHFYHRQHE VCCQDAIVKL RKISDWALKL SSLDRRTVSS
ILYPLLRLRQ ACCHPQAVRG EFLPLQKSTM TMEELLTSLQ KKCGTECEEA HRQLVCALNG
LAGIHIIKGE YALAAELYRE VLRSSEEHKG KLKTDSLQRL HATHNLMELL GAKHPGIPPT
LRDGRLEEEA KQLREHYMSK CNTEVAEAQQ ALQPVQQSIR ELQRKIHSNS PWWLNVIHRA
MEFSVDEELV QRVRNEISSN YKQQTDKLSM SEKFRDCRGL QFLLTTQMEE LHKFQKLVRE
AVKKLEKPPS REVIESATVC HLRPARLPLN CCVFCKADEL FTEYESKLFF NTVKGQTAIF
EEMIEDEEGL VDDRVPTTTR GLWAVSETER SMKAILSFAR SHRFDVEYVD EGSVSMDLFE
AWKKEYKLLH EYWMTLRNRV SAVDELAMAT ERLRVRHPKE PKPNPPVHHI IEPHEVEQNR
IKLVNDKAVA TSQLQKKLGQ LLYLTNLEKS QDKTSGGINP EPCPICARQL GKQWAVLTCG
HCFCNECTSI IIEQYSVGSH RSSIKCAICR QTTSHKEVSY VFTSEKANQE DDIPVKGSHS
TKVEAVVRTL MKIQLRDPGA KALVFSTWQD VLDIISKALT DNNMEFTQIS RIKTFQENLS
AFKYDPHINI LLLPLHTGSN GLTIIEATHV LLVEPILNPA HELQAIGRVH RIGQTKPTIV
HRFLIKATIE ERMQAMLKTA ERSHTSSSGK HSEASVLTVA GLADLFTKEN EELE
