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Q70CQ1 (UBP49_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Ubiquitin carboxyl-terminal hydrolase 49

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 49
Ubiquitin thioesterase 49
Ubiquitin-specific-processing protease 49
Gene names
Name:USP49
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length688 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically deubiquitinates histone H2B at 'Lys-120' (H2BK120Ub). H2BK120Ub is a specific tag for epigenetic transcriptional activation and acts as a regulator of mRNA splicing. Deubiquitination is required for efficient cotranscriptional splicing of a large set of exons. Ref.5

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Ref.1 Ref.5

Subunit structure

Component of a complex with RUVBL1 and PSMC5. Ref.5

Subcellular location

Nucleus Probable Ref.5.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q70CQ1-1)

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: Q70CQ1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     627-688: FWVHCNDSKL...NDEGRPQTFS → ACALLCGVGDTERG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 688688Ubiquitin carboxyl-terminal hydrolase 49
PRO_0000080678

Regions

Domain253 – 657405USP
Zinc finger24 – 8562UBP-type

Sites

Active site2621Nucleophile Probable
Active site6151Proton acceptor By similarity

Natural variations

Alternative sequence627 – 68862FWVHC…PQTFS → ACALLCGVGDTERG in isoform 2.
VSP_011556

Experimental info

Mutagenesis2621C → A: Loss of deubiquitinase activity. Ref.5

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: 1DE97A430A636B0B

FASTA68879,198
        10         20         30         40         50         60 
MDRCKHVGRL RLAQDHSILN PQKWCCLECA TTESVWACLK CSHVACGRYI EDHALKHFEE 

        70         80         90        100        110        120 
TGHPLAMEVR DLYVFCYLCK DYVLNDNPEG DLKLLRSSLL AVRGQKQDTP VRRGRTLRSM 

       130        140        150        160        170        180 
ASGEDVVLPQ RAPQGQPQML TALWYRRQRL LARTLRLWFE KSSRGQAKLE QRRQEEALER 

       190        200        210        220        230        240 
KKEEARRRRR EVKRRLLEEL ASTPPRKSAR LLLHTPRDAG PAASRPAALP TSRRVPAATL 

       250        260        270        280        290        300 
KLRRQPAMAP GVTGLRNLGN TCYMNSILQV LSHLQKFREC FLNLDPSKTE HLFPKATNGK 

       310        320        330        340        350        360 
TQLSGKPTNS SATELSLRND RAEACEREGF CWNGRASISR SLELIQNKEP SSKHISLCRE 

       370        380        390        400        410        420 
LHTLFRVMWS GKWALVSPFA MLHSVWSLIP AFRGYDQQDA QEFLCELLHK VQQELESEGT 

       430        440        450        460        470        480 
TRRILIPFSQ RKLTKQVLKV VNTIFHGQLL SQVTCISCNY KSNTIEPFWD LSLEFPERYH 

       490        500        510        520        530        540 
CIEKGFVPLN QTECLLTEML AKFTETEALE GRIYACDQCN SKRRKSNPKP LVLSEARKQL 

       550        560        570        580        590        600 
MIYRLPQVLR LHLKRFRWSG RNHREKIGVH VVFDQVLTME PYCCRDMLSS LDKETFAYDL 

       610        620        630        640        650        660 
SAVVMHHGKG FGSGHYTAYC YNTEGGFWVH CNDSKLNVCS VEEVCKTQAY ILFYTQRTVQ 

       670        680 
GNARISETHL QAQVQSSNND EGRPQTFS 

« Hide

Isoform 2 [UniParc].

Checksum: 2476376554DA939E
Show »

FASTA64073,455

References

« Hide 'large scale' references
[1]"Cloning and enzymatic analysis of 22 novel human ubiquitin-specific proteases."
Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S., Lopez-Otin C.
Biochem. Biophys. Res. Commun. 314:54-62(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY.
[2]"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].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 2).
Tissue: Eye.
[5]"USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing."
Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S., Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M., Giles K.E., Ma L., Wang H.
Genes Dev. 27:1581-1595(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH RUVBL1 AND PSMC5, MUTAGENESIS OF CYS-262.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ586139 mRNA. Translation: CAE51939.1.
AL365205 Genomic DNA. Translation: CAI13187.1.
AL365205 Genomic DNA. Translation: CAI13188.1.
CH471081 Genomic DNA. Translation: EAX04065.1.
BC014176 mRNA. Translation: AAH14176.1.
RefSeqNP_001273483.1. NM_001286554.1.
NP_061031.2. NM_018561.4.
UniGeneHs.593575.
Hs.665742.

3D structure databases

ProteinModelPortalQ70CQ1.
SMRQ70CQ1. Positions 26-83, 246-655.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117382. 38 interactions.
IntActQ70CQ1. 33 interactions.
STRING9606.ENSP00000297229.

Protein family/group databases

MEROPSC19.073.

PTM databases

PhosphoSiteQ70CQ1.

Polymorphism databases

DMDM52000871.

Proteomic databases

PaxDbQ70CQ1.
PRIDEQ70CQ1.

Protocols and materials databases

DNASU25862.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297229; ENSP00000297229; ENSG00000164663. [Q70CQ1-2]
ENST00000373006; ENSP00000362097; ENSG00000164663. [Q70CQ1-2]
ENST00000373009; ENSP00000362100; ENSG00000164663. [Q70CQ1-1]
ENST00000394253; ENSP00000377797; ENSG00000164663. [Q70CQ1-1]
GeneID25862.
KEGGhsa:25862.
UCSCuc003ori.3. human. [Q70CQ1-2]

Organism-specific databases

CTD25862.
GeneCardsGC06M041787.
H-InvDBHIX0164985.
HGNCHGNC:20078. USP49.
HPAHPA030254.
HPA030255.
neXtProtNX_Q70CQ1.
PharmGKBPA134954570.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5077.
HOGENOMHOG000015084.
HOVERGENHBG018027.
InParanoidQ70CQ1.
KOK11834.
OMACLECATT.
OrthoDBEOG7JX33S.
PhylomeDBQ70CQ1.
TreeFamTF315281.

Gene expression databases

ArrayExpressQ70CQ1.
BgeeQ70CQ1.
CleanExHS_USP49.
GenevestigatorQ70CQ1.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
SMARTSM00290. ZnF_UBP. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi25862.
NextBio47231.
PROQ70CQ1.

Entry information

Entry nameUBP49_HUMAN
AccessionPrimary (citable) accession number: Q70CQ1
Secondary accession number(s): Q5T3D9, Q5T3E0, Q96CK4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 92 of the entry and version 1 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

Peptidase families

Classification of peptidase families and list of entries

Human chromosome 6

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