CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012425
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase SHPRH 
Protein Synonyms/Alias
 SNF2, histone-linker, PHD and RING finger domain-containing helicase 
Gene Name
 SHPRH 
Gene Synonyms/Alias
 KIAA2023 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1260LFTEYESKLFSNTVKubiquitination[1]
1566FAQISRVKTFQENLSubiquitination[1]
1576QENLSAFKRDPQINIubiquitination[1]
Reference
 [1] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 E3 ubiquitin-protein ligase involved in DNA repair. Upon genotoxic stress, accepts ubiquitin from the UBE2N-UBE2V2 E2 complex and transfers it to 'Lys-164' of PCNA which had been monoubiquitinated by UBE2A/B-RAD18, promoting the formation of non-canonical poly-ubiquitin chains linked through 'Lys-63'. 
Sequence Annotation
 DOMAIN 307 389 Helicase ATP-binding; first part.
 DOMAIN 438 512 H15.
 DOMAIN 710 868 Helicase ATP-binding; second part.
 DOMAIN 1514 1672 Helicase C-terminal.
 NP_BIND 373 380 ATP (By similarity).
 ZN_FING 658 709 PHD-type.
 ZN_FING 1432 1479 RING-type.
 MOTIF 819 822 DEAQ box.
 MOD_RES 266 266 Phosphoserine.  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; DNA damage; DNA repair; Helicase; Hydrolase; Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1683 AA 
Protein Sequence
MSSRRKRAPP VRVDEEKRQQ LHWNMHEDRR NEPIIISDDD EQPCPGSDTS SAHYIILSDS 60
LKEEVAHRDK KRCSKVVSFS KPIEKEETVG IFSPLSVKLN IVISPYHFDN SWKAFLGELT 120
LQLLPAQSLI ENFSERSITL MSSESSNQFL IYVHSKGEDV EKQKKEPMSI CDKGILVESS 180
FSGEMLEDLG WLQKKRRIKL YQKPEGNHII KVGIYLLEAG LAKLDFLSDA NSRMKKFNQL 240
MKKVMEKLHN SIIPDVLEED EDDPESEPEG QDIDELYHFV KQTHQQETQS IQVDVQHPAL 300
IPVLRPYQRE AVNWMLQQEC FRSSPATESA LHFLWREIVT SEGLKLYYNP YTGCIIREYP 360
NSGPQLLGGI LADEMGLGKT VEVLALILTH TRQDVKQDAL TLPEGKVVNY FIPSHYFGGK 420
LKKTEIQNIE FEPKEKVQCP PTRVMILTAV KEMNGKKGVS ILSIYKYVSS IYRYDVQRNR 480
SLLKRMLKCL IFEGLVKQIK GHGFSGTFTL GKNYKEEDIC DKTKKQAVGS PRKIQKETRK 540
SGNKDTDSEY LPSDTSDDDD DPYYYYYKSR RNRSKLRKKL VPSTKKGKSQ PFINPDSQGH 600
CPATSDSGIT DVAMSKSTCI SEFNQEHETE DCAESLNHAD SDVPPSNTMS PFNTSDYRFE 660
CICGELDQID RKPRVQCLKC HLWQHAKCVN YDEKNLKIKP FYCPHCLVAM EPVSTRATLI 720
ISPSSICHQW VDEINRHVRS SSLRVLVYQG VKKDGFLQPH FLAEQDIVII TYDVLRSELN 780
YVDIPHSNSE DGRRLRNQKR YMAIPSPLVA VEWWRICLDE AQMVECPTVK AAEMAQRLSG 840
INRWCISGTP VQRGLEDLFG LVVFLGIEPY CVKHWWVRLL YRPYCKKNPQ HLYSFIAKIL 900
WRSAKKDVID QIQIPPQTEE IHWLHFSPVE RHFYHRQHEV CCQDVVVKLR KISDWALKLS 960
SLDRRTVTSI LYPLLRLRQA CCHPQAVRGE FLPLQKSFEQ STFSFSTMTM EELLTSLQKK 1020
CGTECEEAHR QLVCALNGLA GIHIIKGEYA LAAELYREVL RSSEEHKGKL KTDSLQRLHA 1080
THNLMELLIA RHPGIPPTLR DGRLEEEAKQ LREHYMSKCN TEVAEAQQAL YPVQQTIHEL 1140
QRKIHSNSPW WLNVIHRAIE FTIDEELVQR VRNEITSNYK QQTGKLSMSE KGLQFLLTTQ 1200
MEELNKCQKL VREAVKNLEG PPSRNVIESA TVCHLRPARL PLNCCVFCKA DELFTEYESK 1260
LFSNTVKGQT AIFEEMIEDE EGLVDDRAPT TTRGLWAISE TERSMKAILS FAKSHRFDVE 1320
FVDEGSTSMD LFEAWKKEYK LLHEYWMALR NRVSAVDELA MATERLRVRD PREPKPNPPV 1380
LHIIEPHEVE QNRIKLLNDK AVATSQLQKK LGQLLYLTNL EKSQDKTSGG VNPEPCPICA 1440
RQLGKQWAVL TCGHCFCNEC ISIIIEQYSV GSHRSSIKCA ICRQTTSHKE ISYVFTSEKA 1500
NQEEDIPVKG SHSTKVEAVV RTLMKIQLRD PGAKALVFST WQDVLDIISK ALTDNNMEFA 1560
QISRVKTFQE NLSAFKRDPQ INILLLPLHT GSNGLTIIEA THVLLVEPIL NPAHELQAIG 1620
RVHRIGQTKP TIVHRFLIKA TIEERMQAML KTAERSIYI 1659 
Gene Ontology
 GO:0000786; C:nucleosome; IEA:InterPro.
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006334; P:nucleosome assembly; IEA:InterPro.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. 
Interpro
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR005818; Histone_H1/H5.
 IPR027417; P-loop_NTPase.
 IPR000330; SNF2_N.
 IPR011991; WHTH_DNA-bd_dom.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00271; Helicase_C
 PF00538; Linker_histone
 PF00176; SNF2_N
 PF13639; zf-RING_2 
SMART
 SM00487; DEXDc
 SM00526; H15
 SM00490; HELICc
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS51504; H15
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS