Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q149N8

- SHPRH_HUMAN

UniProt

Q149N8 - SHPRH_HUMAN

Protein

E3 ubiquitin-protein ligase SHPRH

Gene

SHPRH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 3808ATPPROSITE-ProRule annotation
    Zinc fingeri658 – 70952PHD-typeAdd
    BLAST
    Zinc fingeri1432 – 147948RING-typePROSITE-ProRule annotationAdd
    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

    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

    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 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

    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

    1
    1683
    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.
    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.
    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.

    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:
    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

    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: October 1, 2014
    This is version 89 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