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Protein

E3 ubiquitin-protein ligase SHPRH

Gene

SHPRH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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'.3 Publications

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi373 – 3808ATPPROSITE-ProRule annotation
Zinc fingeri658 – 70952PHD-typeAdd
BLAST
Zinc fingeri1432 – 147948RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • DNA repair Source: UniProtKB-KW
  • nucleosome assembly Source: InterPro
  • protein polyubiquitination Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase SHPRH (EC:3.6.4.-, EC:6.3.2.-)
Alternative name(s):
SNF2, histone-linker, PHD and RING finger domain-containing helicase
Gene namesi
Name:SHPRH
Synonyms:KIAA2023
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:19336. SHPRH.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1432 – 14321C → A: Abolishes E3 activity. 1 Publication

Organism-specific databases

PharmGKBiPA134880315.

Polymorphism and mutation databases

BioMutaiSHPRH.
DMDMi146325723.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16831683E3 ubiquitin-protein ligase SHPRHPRO_0000284918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ149N8.
PaxDbiQ149N8.
PRIDEiQ149N8.

PTM databases

PhosphoSiteiQ149N8.

Expressioni

Tissue specificityi

Broadly expressed.1 Publication

Gene expression databases

BgeeiQ149N8.
ExpressionAtlasiQ149N8. baseline and differential.
GenevisibleiQ149N8. HS.

Organism-specific databases

HPAiHPA034854.

Interactioni

Subunit structurei

Homodimer. Interacts with HLTF, PCNA, UBE2N and RAD18.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C17orf59Q96GS43EBI-714105,EBI-10193358
EDARADDQ8WWZ33EBI-714105,EBI-2949647

Protein-protein interaction databases

BioGridi129208. 16 interactions.
DIPiDIP-46277N.
IntActiQ149N8. 7 interactions.
MINTiMINT-1370426.

Structurei

Secondary structure

1
1683
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni669 – 6713Combined sources
Beta strandi674 – 6774Combined sources
Turni678 – 6814Combined sources
Beta strandi682 – 6854Combined sources
Helixi686 – 6883Combined sources
Turni694 – 6985Combined sources
Helixi704 – 7107Combined sources
Helixi1000 – 103738Combined sources
Helixi1040 – 105617Combined sources
Turni1057 – 10604Combined sources
Helixi1065 – 108016Combined sources
Turni1081 – 10844Combined sources
Turni1090 – 10945Combined sources
Helixi1095 – 111925Combined sources
Helixi1122 – 113312Combined sources
Beta strandi1137 – 11393Combined sources
Helixi1141 – 115111Combined sources
Helixi1155 – 116612Combined sources
Helixi1180 – 11823Combined sources
Helixi1186 – 121227Combined sources
Helixi1220 – 123011Combined sources
Beta strandi1234 – 12363Combined sources
Helixi1242 – 125716Combined sources
Helixi1296 – 131015Combined sources
Helixi1315 – 135945Combined sources
Helixi1385 – 141430Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M85NMR-A652-716[»]
4QN1X-ray2.48A1000-1418[»]
ProteinModelPortaliQ149N8.
SMRiQ149N8. Positions 652-716, 718-989, 1000-1418, 1430-1484, 1523-1642.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini307 – 38983Helicase ATP-binding; first partPROSITE-ProRule annotationAdd
BLAST
Domaini438 – 51275H15PROSITE-ProRule annotationAdd
BLAST
Domaini710 – 868159Helicase ATP-binding; second partPROSITE-ProRule annotationAdd
BLAST
Domaini1514 – 1672159Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi819 – 8224DEAQ box

Domaini

The RING finger mediates E3 ubiquitin ligase activity.

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri658 – 70952PHD-typeAdd
BLAST
Zinc fingeri1432 – 147948RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00730000111123.
HOVERGENiHBG059171.
InParanoidiQ149N8.
KOiK15710.
OrthoDBiEOG7ZD1TJ.
PhylomeDBiQ149N8.
TreeFamiTF324273.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.40.10. 2 hits.
3.40.50.300. 4 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR005818. Histone_H1/H5_H15.
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.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00526. H15. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 6 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51504. H15. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q149N8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSRRKRAPP VRVDEEKRQQ LHWNMHEDRR NEPIIISDDD EQPCPGSDTS
60 70 80 90 100
SAHYIILSDS LKEEVAHRDK KRCSKVVSFS KPIEKEETVG IFSPLSVKLN
110 120 130 140 150
IVISPYHFDN SWKAFLGELT LQLLPAQSLI ENFSERSITL MSSESSNQFL
160 170 180 190 200
IYVHSKGEDV EKQKKEPMSI CDKGILVESS FSGEMLEDLG WLQKKRRIKL
210 220 230 240 250
YQKPEGNHII KVGIYLLEAG LAKLDFLSDA NSRMKKFNQL MKKVMEKLHN
260 270 280 290 300
SIIPDVLEED EDDPESEPEG QDIDELYHFV KQTHQQETQS IQVDVQHPAL
310 320 330 340 350
IPVLRPYQRE AVNWMLQQEC FRSSPATESA LHFLWREIVT SEGLKLYYNP
360 370 380 390 400
YTGCIIREYP NSGPQLLGGI LADEMGLGKT VEVLALILTH TRQDVKQDAL
410 420 430 440 450
TLPEGKVVNY FIPSHYFGGK LKKTEIQNIE FEPKEKVQCP PTRVMILTAV
460 470 480 490 500
KEMNGKKGVS ILSIYKYVSS IYRYDVQRNR SLLKRMLKCL IFEGLVKQIK
510 520 530 540 550
GHGFSGTFTL GKNYKEEDIC DKTKKQAVGS PRKIQKETRK SGNKDTDSEY
560 570 580 590 600
LPSDTSDDDD DPYYYYYKSR RNRSKLRKKL VPSTKKGKSQ PFINPDSQGH
610 620 630 640 650
CPATSDSGIT DVAMSKSTCI SEFNQEHETE DCAESLNHAD SDVPPSNTMS
660 670 680 690 700
PFNTSDYRFE CICGELDQID RKPRVQCLKC HLWQHAKCVN YDEKNLKIKP
710 720 730 740 750
FYCPHCLVAM EPVSTRATLI ISPSSICHQW VDEINRHVRS SSLRVLVYQG
760 770 780 790 800
VKKDGFLQPH FLAEQDIVII TYDVLRSELN YVDIPHSNSE DGRRLRNQKR
810 820 830 840 850
YMAIPSPLVA VEWWRICLDE AQMVECPTVK AAEMAQRLSG INRWCISGTP
860 870 880 890 900
VQRGLEDLFG LVVFLGIEPY CVKHWWVRLL YRPYCKKNPQ HLYSFIAKIL
910 920 930 940 950
WRSAKKDVID QIQIPPQTEE IHWLHFSPVE RHFYHRQHEV CCQDVVVKLR
960 970 980 990 1000
KISDWALKLS SLDRRTVTSI LYPLLRLRQA CCHPQAVRGE FLPLQKSTMT
1010 1020 1030 1040 1050
MEELLTSLQK KCGTECEEAH RQLVCALNGL AGIHIIKGEY ALAAELYREV
1060 1070 1080 1090 1100
LRSSEEHKGK LKTDSLQRLH ATHNLMELLI ARHPGIPPTL RDGRLEEEAK
1110 1120 1130 1140 1150
QLREHYMSKC NTEVAEAQQA LYPVQQTIHE LQRKIHSNSP WWLNVIHRAI
1160 1170 1180 1190 1200
EFTIDEELVQ RVRNEITSNY KQQTGKLSMS EKFRDCRGLQ FLLTTQMEEL
1210 1220 1230 1240 1250
NKCQKLVREA VKNLEGPPSR NVIESATVCH LRPARLPLNC CVFCKADELF
1260 1270 1280 1290 1300
TEYESKLFSN TVKGQTAIFE EMIEDEEGLV DDRAPTTTRG LWAISETERS
1310 1320 1330 1340 1350
MKAILSFAKS HRFDVEFVDE GSTSMDLFEA WKKEYKLLHE YWMALRNRVS
1360 1370 1380 1390 1400
AVDELAMATE RLRVRDPREP KPNPPVLHII EPHEVEQNRI KLLNDKAVAT
1410 1420 1430 1440 1450
SQLQKKLGQL LYLTNLEKSQ DKTSGGVNPE PCPICARQLG KQWAVLTCGH
1460 1470 1480 1490 1500
CFCNECISII IEQYSVGSHR SSIKCAICRQ TTSHKEISYV FTSEKANQEE
1510 1520 1530 1540 1550
DIPVKGSHST KVEAVVRTLM KIQLRDPGAK ALVFSTWQDV LDIISKALTD
1560 1570 1580 1590 1600
NNMEFAQISR VKTFQENLSA FKRDPQINIL LLPLHTGSNG LTIIEATHVL
1610 1620 1630 1640 1650
LVEPILNPAH ELQAIGRVHR IGQTKPTIVH RFLIKATIEE RMQAMLKTAE
1660 1670 1680
RSHTNSSAKH SEASVLTVAD LADLFTKETE ELE
Length:1,683
Mass (Da):193,079
Last modified:May 1, 2007 - v2
Checksum:i3EAA1433EF89B232
GO
Isoform 2 (identifier: Q149N8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-156: Missing.
     1039-1040: EY → RR
     1041-1683: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:929
Mass (Da):107,341
Checksum:i053D4616BE6C508C
GO
Isoform 3 (identifier: Q149N8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     996-996: K → KSFEQSTFSF
     1183-1187: Missing.
     1653-1655: HTN → IYI
     1656-1683: Missing.

Note: No experimental confirmation available.
Show »
Length:1,659
Mass (Da):190,497
Checksum:iA97C8EC77CBABFD7
GO
Isoform 4 (identifier: Q149N8-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     442-471: TRVMILTAVKEMNGKKGVSILSIYKYVSSI → YPFTFSYTCDDTDSCERNEWKKRSVHPFHL
     472-1683: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:471
Mass (Da):54,339
Checksum:iC602569D075A3DC0
GO

Sequence cautioni

The sequence AAI13090.1 differs from that shown.Aberrant splicing.Curated
The sequence AAI17686.1 differs from that shown.Aberrant splicing.Curated
The sequence BAC04459.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC23119.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated
The sequence CAH18145.1 differs from that shown. Reason: Frameshift at positions 762 and 997. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851M → V in CAH18145 (PubMed:17974005).Curated
Sequence conflicti379 – 3791K → E in BAC11544 (PubMed:14702039).Curated
Sequence conflicti425 – 4251E → G in BAC11544 (PubMed:14702039).Curated
Sequence conflicti560 – 5601D → G in CAH18145 (PubMed:17974005).Curated
Sequence conflicti1398 – 13981V → F in AAI17687 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti438 – 4381Q → R in an ovarian cancer cell line. 1 Publication
VAR_031857
Natural varianti460 – 4601S → F in a melanoma cell line. 1 Publication
VAR_031858
Natural varianti1028 – 10281N → Y in a melanoma cell line. 1 Publication
VAR_031859
Natural varianti1222 – 12221V → D Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064750

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei46 – 156111Missing in isoform 2. 1 PublicationVSP_024753Add
BLAST
Alternative sequencei442 – 47130TRVMI…YVSSI → YPFTFSYTCDDTDSCERNEW KKRSVHPFHL in isoform 4. 1 PublicationVSP_024760Add
BLAST
Alternative sequencei472 – 16831212Missing in isoform 4. 1 PublicationVSP_024761Add
BLAST
Alternative sequencei996 – 9961K → KSFEQSTFSF in isoform 3. 1 PublicationVSP_024756
Alternative sequencei1039 – 10402EY → RR in isoform 2. 1 PublicationVSP_024757
Alternative sequencei1041 – 1683643Missing in isoform 2. 1 PublicationVSP_024758Add
BLAST
Alternative sequencei1183 – 11875Missing in isoform 3. 1 PublicationVSP_024759
Alternative sequencei1653 – 16553HTN → IYI in isoform 3. 1 PublicationVSP_024762
Alternative sequencei1656 – 168328Missing in isoform 3. 1 PublicationVSP_024763Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY161136 mRNA. Translation: AAO26201.1.
AY163808 mRNA. Translation: AAO06907.1.
CR749290 mRNA. Translation: CAH18145.1. Frameshift.
AL356599, AL451145 Genomic DNA. Translation: CAI41120.1.
AL451145, AL356599 Genomic DNA. Translation: CAH70765.1.
BC113089 mRNA. Translation: AAI13090.1. Sequence problems.
BC117685 mRNA. Translation: AAI17686.1. Sequence problems.
BC117686 mRNA. Translation: AAI17687.1.
AK075318 mRNA. Translation: BAC11544.1.
AK094944 mRNA. Translation: BAC04459.1. Different initiation.
AB095943 mRNA. Translation: BAC23119.1. Sequence problems.
CCDSiCCDS43513.2. [Q149N8-1]
CCDS47496.1. [Q149N8-4]
RefSeqiNP_001036148.2. NM_001042683.2. [Q149N8-1]
NP_775105.1. NM_173082.3. [Q149N8-4]
XP_006715504.1. XM_006715441.2. [Q149N8-1]
UniGeneiHs.723297.

Genome annotation databases

EnsembliENST00000275233; ENSP00000275233; ENSG00000146414. [Q149N8-1]
ENST00000367505; ENSP00000356475; ENSG00000146414. [Q149N8-1]
ENST00000438092; ENSP00000412797; ENSG00000146414. [Q149N8-4]
ENST00000519632; ENSP00000430528; ENSG00000146414. [Q149N8-2]
GeneIDi257218.
KEGGihsa:257218.
UCSCiuc003qle.3. human. [Q149N8-4]
uc003qlf.3. human. [Q149N8-1]
uc003qlj.1. human. [Q149N8-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY161136 mRNA. Translation: AAO26201.1.
AY163808 mRNA. Translation: AAO06907.1.
CR749290 mRNA. Translation: CAH18145.1. Frameshift.
AL356599, AL451145 Genomic DNA. Translation: CAI41120.1.
AL451145, AL356599 Genomic DNA. Translation: CAH70765.1.
BC113089 mRNA. Translation: AAI13090.1. Sequence problems.
BC117685 mRNA. Translation: AAI17686.1. Sequence problems.
BC117686 mRNA. Translation: AAI17687.1.
AK075318 mRNA. Translation: BAC11544.1.
AK094944 mRNA. Translation: BAC04459.1. Different initiation.
AB095943 mRNA. Translation: BAC23119.1. Sequence problems.
CCDSiCCDS43513.2. [Q149N8-1]
CCDS47496.1. [Q149N8-4]
RefSeqiNP_001036148.2. NM_001042683.2. [Q149N8-1]
NP_775105.1. NM_173082.3. [Q149N8-4]
XP_006715504.1. XM_006715441.2. [Q149N8-1]
UniGeneiHs.723297.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M85NMR-A652-716[»]
4QN1X-ray2.48A1000-1418[»]
ProteinModelPortaliQ149N8.
SMRiQ149N8. Positions 652-716, 718-989, 1000-1418, 1430-1484, 1523-1642.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129208. 16 interactions.
DIPiDIP-46277N.
IntActiQ149N8. 7 interactions.
MINTiMINT-1370426.

PTM databases

PhosphoSiteiQ149N8.

Polymorphism and mutation databases

BioMutaiSHPRH.
DMDMi146325723.

Proteomic databases

MaxQBiQ149N8.
PaxDbiQ149N8.
PRIDEiQ149N8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000275233; ENSP00000275233; ENSG00000146414. [Q149N8-1]
ENST00000367505; ENSP00000356475; ENSG00000146414. [Q149N8-1]
ENST00000438092; ENSP00000412797; ENSG00000146414. [Q149N8-4]
ENST00000519632; ENSP00000430528; ENSG00000146414. [Q149N8-2]
GeneIDi257218.
KEGGihsa:257218.
UCSCiuc003qle.3. human. [Q149N8-4]
uc003qlf.3. human. [Q149N8-1]
uc003qlj.1. human. [Q149N8-2]

Organism-specific databases

CTDi257218.
GeneCardsiGC06M146185.
HGNCiHGNC:19336. SHPRH.
HPAiHPA034854.
MIMi608048. gene.
neXtProtiNX_Q149N8.
PharmGKBiPA134880315.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00730000111123.
HOVERGENiHBG059171.
InParanoidiQ149N8.
KOiK15710.
OrthoDBiEOG7ZD1TJ.
PhylomeDBiQ149N8.
TreeFamiTF324273.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiSHPRH. human.
GeneWikiiSHPRH.
GenomeRNAii257218.
NextBioi92973.
PROiQ149N8.
SOURCEiSearch...

Gene expression databases

BgeeiQ149N8.
ExpressionAtlasiQ149N8. baseline and differential.
GenevisibleiQ149N8. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.40.10. 2 hits.
3.40.50.300. 4 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR005818. Histone_H1/H5_H15.
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.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00526. H15. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 6 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51504. H15. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel gene, SHPRH, encoding a conserved putative protein with SNF2/helicase and PHD-finger domains from the 6q24 region."
    Sood R., Makalowska I., Galdzicki M., Hu P., Eddings E., Robbins C.M., Moses T., Namkoong J., Chen S., Trent J.M.
    Genomics 82:153-161(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS ARG-438; PHE-460 AND TYR-1028.
  2. Chen S., Yu L., Guo J.H.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Salivary gland.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-584 AND 1532-1683 (ISOFORM 1).
    Tissue: Corpus callosum.
  7. "The nucleotide sequence of a long cDNA clone isolated from human."
    Nagase T., Kikuno R., Ohara O.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-1683 (ISOFORM 4).
    Tissue: Brain.
  8. "Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination."
    Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.
    J. Cell Biol. 175:703-708(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH PCNA; UBE2N AND RAD18, MUTAGENESIS OF CYS-1432.
  9. "Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen."
    Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V., Hurwitz J., Prakash L., Prakash S., Haracska L.
    Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBE2N AND RAD18.
  10. "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks."
    Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.
    Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HLTF.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: VARIANT ASP-1222.

Entry informationi

Entry nameiSHPRH_HUMAN
AccessioniPrimary (citable) accession number: Q149N8
Secondary accession number(s): Q149N9
, Q5VV79, Q68DS5, Q7Z5J5, Q8IVE8, Q8IWQ9, Q8N1S8, Q8NBR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: June 24, 2015
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.