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Q149N8

- SHPRH_HUMAN

UniProt

Q149N8 - SHPRH_HUMAN

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Protein
E3 ubiquitin-protein ligase SHPRH
Gene
SHPRH, KIAA2023
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi373 – 3808ATP By similarity
Zinc fingeri658 – 70952PHD-type
Add
BLAST
Zinc fingeri1432 – 147948RING-type
Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: InterPro
  3. helicase activity Source: UniProtKB-KW
  4. ligase activity Source: UniProtKB-KW
  5. ubiquitin-protein transferase activity Source: FlyBase
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. nucleosome assembly Source: InterPro
  3. 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: Chromosome 6

Organism-specific databases

HGNCiHGNC:19336. SHPRH.

Subcellular locationi

GO - Cellular componenti

  1. nucleosome Source: InterPro
  2. nucleus Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

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

Organism-specific databases

PharmGKBiPA134880315.

PTM / Processingi

Molecule processing

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

ArrayExpressiQ149N8.
BgeeiQ149N8.
GenevestigatoriQ149N8.

Organism-specific databases

HPAiHPA034854.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi129208. 14 interactions.
DIPiDIP-46277N.
IntActiQ149N8. 5 interactions.
MINTiMINT-1370426.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni669 – 6713
Beta strandi674 – 6774
Turni678 – 6814
Beta strandi682 – 6854
Helixi686 – 6883
Turni694 – 6985
Helixi704 – 7107

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M85NMR-A652-716[»]
ProteinModelPortaliQ149N8.
SMRiQ149N8. Positions 652-716, 718-989, 1428-1485, 1523-1642.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini307 – 38983Helicase ATP-binding; first part
Add
BLAST
Domaini438 – 51275H15
Add
BLAST
Domaini710 – 868159Helicase ATP-binding; second part
Add
BLAST
Domaini1514 – 1672159Helicase C-terminal
Add
BLAST

Motif

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

Domaini

The RING finger mediates E3 ubiquitin ligase activity.

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0553.
HOVERGENiHBG059171.
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. Align

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

MSSRRKRAPP VRVDEEKRQQ LHWNMHEDRR NEPIIISDDD EQPCPGSDTS     50
SAHYIILSDS LKEEVAHRDK KRCSKVVSFS KPIEKEETVG IFSPLSVKLN 100
IVISPYHFDN SWKAFLGELT LQLLPAQSLI ENFSERSITL MSSESSNQFL 150
IYVHSKGEDV EKQKKEPMSI CDKGILVESS FSGEMLEDLG WLQKKRRIKL 200
YQKPEGNHII KVGIYLLEAG LAKLDFLSDA NSRMKKFNQL MKKVMEKLHN 250
SIIPDVLEED EDDPESEPEG QDIDELYHFV KQTHQQETQS IQVDVQHPAL 300
IPVLRPYQRE AVNWMLQQEC FRSSPATESA LHFLWREIVT SEGLKLYYNP 350
YTGCIIREYP NSGPQLLGGI LADEMGLGKT VEVLALILTH TRQDVKQDAL 400
TLPEGKVVNY FIPSHYFGGK LKKTEIQNIE FEPKEKVQCP PTRVMILTAV 450
KEMNGKKGVS ILSIYKYVSS IYRYDVQRNR SLLKRMLKCL IFEGLVKQIK 500
GHGFSGTFTL GKNYKEEDIC DKTKKQAVGS PRKIQKETRK SGNKDTDSEY 550
LPSDTSDDDD DPYYYYYKSR RNRSKLRKKL VPSTKKGKSQ PFINPDSQGH 600
CPATSDSGIT DVAMSKSTCI SEFNQEHETE DCAESLNHAD SDVPPSNTMS 650
PFNTSDYRFE CICGELDQID RKPRVQCLKC HLWQHAKCVN YDEKNLKIKP 700
FYCPHCLVAM EPVSTRATLI ISPSSICHQW VDEINRHVRS SSLRVLVYQG 750
VKKDGFLQPH FLAEQDIVII TYDVLRSELN YVDIPHSNSE DGRRLRNQKR 800
YMAIPSPLVA VEWWRICLDE AQMVECPTVK AAEMAQRLSG INRWCISGTP 850
VQRGLEDLFG LVVFLGIEPY CVKHWWVRLL YRPYCKKNPQ HLYSFIAKIL 900
WRSAKKDVID QIQIPPQTEE IHWLHFSPVE RHFYHRQHEV CCQDVVVKLR 950
KISDWALKLS SLDRRTVTSI LYPLLRLRQA CCHPQAVRGE FLPLQKSTMT 1000
MEELLTSLQK KCGTECEEAH RQLVCALNGL AGIHIIKGEY ALAAELYREV 1050
LRSSEEHKGK LKTDSLQRLH ATHNLMELLI ARHPGIPPTL RDGRLEEEAK 1100
QLREHYMSKC NTEVAEAQQA LYPVQQTIHE LQRKIHSNSP WWLNVIHRAI 1150
EFTIDEELVQ RVRNEITSNY KQQTGKLSMS EKFRDCRGLQ FLLTTQMEEL 1200
NKCQKLVREA VKNLEGPPSR NVIESATVCH LRPARLPLNC CVFCKADELF 1250
TEYESKLFSN TVKGQTAIFE EMIEDEEGLV DDRAPTTTRG LWAISETERS 1300
MKAILSFAKS HRFDVEFVDE GSTSMDLFEA WKKEYKLLHE YWMALRNRVS 1350
AVDELAMATE RLRVRDPREP KPNPPVLHII EPHEVEQNRI KLLNDKAVAT 1400
SQLQKKLGQL LYLTNLEKSQ DKTSGGVNPE PCPICARQLG KQWAVLTCGH 1450
CFCNECISII IEQYSVGSHR SSIKCAICRQ TTSHKEISYV FTSEKANQEE 1500
DIPVKGSHST KVEAVVRTLM KIQLRDPGAK ALVFSTWQDV LDIISKALTD 1550
NNMEFAQISR VKTFQENLSA FKRDPQINIL LLPLHTGSNG LTIIEATHVL 1600
LVEPILNPAH ELQAIGRVHR IGQTKPTIVH RFLIKATIEE RMQAMLKTAE 1650
RSHTNSSAKH SEASVLTVAD LADLFTKETE ELE 1683
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. Reason: Aberrant splicing.
The sequence AAI17686.1 differs from that shown. Reason: Aberrant splicing.
The sequence CAH18145.1 differs from that shown. Reason: Frameshift at positions 762 and 997.
The sequence BAC04459.1 differs from that shown. Reason: Erroneous initiation.

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.
VSP_024753Add
BLAST
Alternative sequencei442 – 47130TRVMI…YVSSI → YPFTFSYTCDDTDSCERNEW KKRSVHPFHL in isoform 4.
VSP_024760Add
BLAST
Alternative sequencei472 – 16831212Missing in isoform 4.
VSP_024761Add
BLAST
Alternative sequencei996 – 9961K → KSFEQSTFSF in isoform 3.
VSP_024756
Alternative sequencei1039 – 10402EY → RR in isoform 2.
VSP_024757
Alternative sequencei1041 – 1683643Missing in isoform 2.
VSP_024758Add
BLAST
Alternative sequencei1183 – 11875Missing in isoform 3.
VSP_024759
Alternative sequencei1653 – 16553HTN → IYI in isoform 3.
VSP_024762
Alternative sequencei1656 – 168328Missing in isoform 3.
VSP_024763Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851M → V in CAH18145. 1 Publication
Sequence conflicti379 – 3791K → E in BAC11544. 1 Publication
Sequence conflicti425 – 4251E → G in BAC11544. 1 Publication
Sequence conflicti560 – 5601D → G in CAH18145. 1 Publication
Sequence conflicti1398 – 13981V → F in AAI17687. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006715441.1. [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]

Polymorphism databases

DMDMi146325723.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS43513.2. [Q149N8-1 ]
CCDS47496.1. [Q149N8-4 ]
RefSeqi NP_001036148.2. NM_001042683.2. [Q149N8-1 ]
NP_775105.1. NM_173082.3. [Q149N8-4 ]
XP_006715504.1. XM_006715441.1. [Q149N8-1 ]
UniGenei Hs.723297.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2M85 NMR - A 652-716 [» ]
ProteinModelPortali Q149N8.
SMRi Q149N8. Positions 652-716, 718-989, 1428-1485, 1523-1642.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 129208. 14 interactions.
DIPi DIP-46277N.
IntActi Q149N8. 5 interactions.
MINTi MINT-1370426.

PTM databases

PhosphoSitei Q149N8.

Polymorphism databases

DMDMi 146325723.

Proteomic databases

MaxQBi Q149N8.
PaxDbi Q149N8.
PRIDEi Q149N8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000275233 ; ENSP00000275233 ; ENSG00000146414 . [Q149N8-1 ]
ENST00000367505 ; ENSP00000356475 ; ENSG00000146414 . [Q149N8-1 ]
ENST00000438092 ; ENSP00000412797 ; ENSG00000146414 . [Q149N8-4 ]
ENST00000519632 ; ENSP00000430528 ; ENSG00000146414 . [Q149N8-2 ]
GeneIDi 257218.
KEGGi hsa:257218.
UCSCi uc003qle.3. human. [Q149N8-4 ]
uc003qlf.3. human. [Q149N8-1 ]
uc003qlj.1. human. [Q149N8-2 ]

Organism-specific databases

CTDi 257218.
GeneCardsi GC06M146185.
HGNCi HGNC:19336. SHPRH.
HPAi HPA034854.
MIMi 608048. gene.
neXtProti NX_Q149N8.
PharmGKBi PA134880315.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0553.
HOVERGENi HBG059171.
KOi K15710.
OrthoDBi EOG7ZD1TJ.
PhylomeDBi Q149N8.
TreeFami TF324273.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

GeneWikii SHPRH.
GenomeRNAii 257218.
NextBioi 92973.
PROi Q149N8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q149N8.
Bgeei Q149N8.
Genevestigatori Q149N8.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.30.40.10. 2 hits.
3.40.50.300. 4 hits.
InterProi IPR014001. 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 ]
Pfami PF00538. Linker_histone. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00526. H15. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 6 hits.
SSF57903. SSF57903. 1 hit.
PROSITEi PS51504. 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 ]
ProtoNeti Search...

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: September 3, 2014
This is version 88 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

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