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Q149N8 (SHPRH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SHPRH
Synonyms:KIAA2023
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1683 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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'. Ref.8 Ref.9 Ref.10

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer. Interacts with HLTF, PCNA, UBE2N and RAD18. Ref.8 Ref.9 Ref.10

Tissue specificity

Broadly expressed. Ref.1

Domain

The RING finger mediates E3 ubiquitin ligase activity.

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 H15 (linker histone H1/H5 globular) domain.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 PHD-type zinc finger.

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAI13090.1 differs from that shown. Reason: Aberrant splicing.

The sequence AAI17686.1 differs from that shown. Reason: Aberrant splicing.

The sequence BAC04459.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC23119.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

The sequence CAH18145.1 differs from that shown. Reason: Frameshift at positions 762 and 997.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q149N8-1)

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.
Isoform 2 (identifier: Q149N8-2)

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.
Isoform 3 (identifier: Q149N8-4)

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.
Isoform 4 (identifier: Q149N8-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16831683E3 ubiquitin-protein ligase SHPRH
PRO_0000284918

Regions

Domain307 – 38983Helicase ATP-binding; first part
Domain438 – 51275H15
Domain710 – 868159Helicase ATP-binding; second part
Domain1514 – 1672159Helicase C-terminal
Nucleotide binding373 – 3808ATP By similarity
Zinc finger658 – 70952PHD-type
Zinc finger1432 – 147948RING-type
Motif819 – 8224DEAQ box

Amino acid modifications

Modified residue2661Phosphoserine Ref.13

Natural variations

Alternative sequence46 – 156111Missing in isoform 2.
VSP_024753
Alternative sequence442 – 47130TRVMI…YVSSI → YPFTFSYTCDDTDSCERNEW KKRSVHPFHL in isoform 4.
VSP_024760
Alternative sequence472 – 16831212Missing in isoform 4.
VSP_024761
Alternative sequence9961K → KSFEQSTFSF in isoform 3.
VSP_024756
Alternative sequence1039 – 10402EY → RR in isoform 2.
VSP_024757
Alternative sequence1041 – 1683643Missing in isoform 2.
VSP_024758
Alternative sequence1183 – 11875Missing in isoform 3.
VSP_024759
Alternative sequence1653 – 16553HTN → IYI in isoform 3.
VSP_024762
Alternative sequence1656 – 168328Missing in isoform 3.
VSP_024763
Natural variant4381Q → R in an ovarian cancer cell line. Ref.1
VAR_031857
Natural variant4601S → F in a melanoma cell line. Ref.1
VAR_031858
Natural variant10281N → Y in a melanoma cell line. Ref.1
VAR_031859
Natural variant12221V → D Found in a renal cell carcinoma sample; somatic mutation. Ref.14
VAR_064750

Experimental info

Mutagenesis14321C → A: Abolishes E3 activity. Ref.8
Sequence conflict1851M → V in CAH18145. Ref.3
Sequence conflict3791K → E in BAC11544. Ref.6
Sequence conflict4251E → G in BAC11544. Ref.6
Sequence conflict5601D → G in CAH18145. Ref.3
Sequence conflict13981V → F in AAI17687. Ref.5

Secondary structure

............ 1683
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 3EAA1433EF89B232

FASTA1,683193,079
        10         20         30         40         50         60 
MSSRRKRAPP VRVDEEKRQQ LHWNMHEDRR NEPIIISDDD EQPCPGSDTS SAHYIILSDS 

        70         80         90        100        110        120 
LKEEVAHRDK KRCSKVVSFS KPIEKEETVG IFSPLSVKLN IVISPYHFDN SWKAFLGELT 

       130        140        150        160        170        180 
LQLLPAQSLI ENFSERSITL MSSESSNQFL IYVHSKGEDV EKQKKEPMSI CDKGILVESS 

       190        200        210        220        230        240 
FSGEMLEDLG WLQKKRRIKL YQKPEGNHII KVGIYLLEAG LAKLDFLSDA NSRMKKFNQL 

       250        260        270        280        290        300 
MKKVMEKLHN SIIPDVLEED EDDPESEPEG QDIDELYHFV KQTHQQETQS IQVDVQHPAL 

       310        320        330        340        350        360 
IPVLRPYQRE AVNWMLQQEC FRSSPATESA LHFLWREIVT SEGLKLYYNP YTGCIIREYP 

       370        380        390        400        410        420 
NSGPQLLGGI LADEMGLGKT VEVLALILTH TRQDVKQDAL TLPEGKVVNY FIPSHYFGGK 

       430        440        450        460        470        480 
LKKTEIQNIE FEPKEKVQCP PTRVMILTAV KEMNGKKGVS ILSIYKYVSS IYRYDVQRNR 

       490        500        510        520        530        540 
SLLKRMLKCL IFEGLVKQIK GHGFSGTFTL GKNYKEEDIC DKTKKQAVGS PRKIQKETRK 

       550        560        570        580        590        600 
SGNKDTDSEY LPSDTSDDDD DPYYYYYKSR RNRSKLRKKL VPSTKKGKSQ PFINPDSQGH 

       610        620        630        640        650        660 
CPATSDSGIT DVAMSKSTCI SEFNQEHETE DCAESLNHAD SDVPPSNTMS PFNTSDYRFE 

       670        680        690        700        710        720 
CICGELDQID RKPRVQCLKC HLWQHAKCVN YDEKNLKIKP FYCPHCLVAM EPVSTRATLI 

       730        740        750        760        770        780 
ISPSSICHQW VDEINRHVRS SSLRVLVYQG VKKDGFLQPH FLAEQDIVII TYDVLRSELN 

       790        800        810        820        830        840 
YVDIPHSNSE DGRRLRNQKR YMAIPSPLVA VEWWRICLDE AQMVECPTVK AAEMAQRLSG 

       850        860        870        880        890        900 
INRWCISGTP VQRGLEDLFG LVVFLGIEPY CVKHWWVRLL YRPYCKKNPQ HLYSFIAKIL 

       910        920        930        940        950        960 
WRSAKKDVID QIQIPPQTEE IHWLHFSPVE RHFYHRQHEV CCQDVVVKLR KISDWALKLS 

       970        980        990       1000       1010       1020 
SLDRRTVTSI LYPLLRLRQA CCHPQAVRGE FLPLQKSTMT MEELLTSLQK KCGTECEEAH 

      1030       1040       1050       1060       1070       1080 
RQLVCALNGL AGIHIIKGEY ALAAELYREV LRSSEEHKGK LKTDSLQRLH ATHNLMELLI 

      1090       1100       1110       1120       1130       1140 
ARHPGIPPTL RDGRLEEEAK QLREHYMSKC NTEVAEAQQA LYPVQQTIHE LQRKIHSNSP 

      1150       1160       1170       1180       1190       1200 
WWLNVIHRAI EFTIDEELVQ RVRNEITSNY KQQTGKLSMS EKFRDCRGLQ FLLTTQMEEL 

      1210       1220       1230       1240       1250       1260 
NKCQKLVREA VKNLEGPPSR NVIESATVCH LRPARLPLNC CVFCKADELF TEYESKLFSN 

      1270       1280       1290       1300       1310       1320 
TVKGQTAIFE EMIEDEEGLV DDRAPTTTRG LWAISETERS MKAILSFAKS HRFDVEFVDE 

      1330       1340       1350       1360       1370       1380 
GSTSMDLFEA WKKEYKLLHE YWMALRNRVS AVDELAMATE RLRVRDPREP KPNPPVLHII 

      1390       1400       1410       1420       1430       1440 
EPHEVEQNRI KLLNDKAVAT SQLQKKLGQL LYLTNLEKSQ DKTSGGVNPE PCPICARQLG 

      1450       1460       1470       1480       1490       1500 
KQWAVLTCGH CFCNECISII IEQYSVGSHR SSIKCAICRQ TTSHKEISYV FTSEKANQEE 

      1510       1520       1530       1540       1550       1560 
DIPVKGSHST KVEAVVRTLM KIQLRDPGAK ALVFSTWQDV LDIISKALTD NNMEFAQISR 

      1570       1580       1590       1600       1610       1620 
VKTFQENLSA FKRDPQINIL LLPLHTGSNG LTIIEATHVL LVEPILNPAH ELQAIGRVHR 

      1630       1640       1650       1660       1670       1680 
IGQTKPTIVH RFLIKATIEE RMQAMLKTAE RSHTNSSAKH SEASVLTVAD LADLFTKETE 


ELE 

« Hide

Isoform 2 [UniParc].

Checksum: 053D4616BE6C508C
Show »

FASTA929107,341
Isoform 3 [UniParc].

Checksum: A97C8EC77CBABFD7
Show »

FASTA1,659190,497
Isoform 4 [UniParc].

Checksum: C602569D075A3DC0
Show »

FASTA47154,339

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-1222.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS43513.2. [Q149N8-1]
CCDS47496.1. [Q149N8-4]
RefSeqNP_001036148.2. NM_001042683.2. [Q149N8-1]
NP_775105.1. NM_173082.3. [Q149N8-4]
XP_006715504.1. XM_006715441.1. [Q149N8-1]
UniGeneHs.723297.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M85NMR-A652-716[»]
ProteinModelPortalQ149N8.
SMRQ149N8. Positions 652-716, 718-989, 1428-1485, 1523-1642.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid129208. 14 interactions.
DIPDIP-46277N.
IntActQ149N8. 5 interactions.
MINTMINT-1370426.

PTM databases

PhosphoSiteQ149N8.

Polymorphism databases

DMDM146325723.

Proteomic databases

MaxQBQ149N8.
PaxDbQ149N8.
PRIDEQ149N8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275233; ENSP00000275233; ENSG00000146414. [Q149N8-1]
ENST00000367505; ENSP00000356475; ENSG00000146414. [Q149N8-1]
ENST00000438092; ENSP00000412797; ENSG00000146414. [Q149N8-4]
ENST00000519632; ENSP00000430528; ENSG00000146414. [Q149N8-2]
GeneID257218.
KEGGhsa:257218.
UCSCuc003qle.3. human. [Q149N8-4]
uc003qlf.3. human. [Q149N8-1]
uc003qlj.1. human. [Q149N8-2]

Organism-specific databases

CTD257218.
GeneCardsGC06M146185.
HGNCHGNC:19336. SHPRH.
HPAHPA034854.
MIM608048. gene.
neXtProtNX_Q149N8.
PharmGKBPA134880315.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOVERGENHBG059171.
KOK15710.
OrthoDBEOG7ZD1TJ.
PhylomeDBQ149N8.
TreeFamTF324273.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ149N8.
BgeeQ149N8.
GenevestigatorQ149N8.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.30.40.10. 2 hits.
3.40.50.300. 4 hits.
InterProIPR014001. 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]
PfamPF00538. Linker_histone. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00526. H15. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 6 hits.
SSF57903. SSF57903. 1 hit.
PROSITEPS51504. 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]
ProtoNetSearch...

Other

GeneWikiSHPRH.
GenomeRNAi257218.
NextBio92973.
PROQ149N8.
SOURCESearch...

Entry information

Entry nameSHPRH_HUMAN
AccessionPrimary (citable) accession number: Q149N8
Secondary accession number(s): Q149N9 expand/collapse secondary AC list , Q5VV79, Q68DS5, Q7Z5J5, Q8IVE8, Q8IWQ9, Q8N1S8, Q8NBR7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM