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Q3LFD5 (UBP41_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative ubiquitin carboxyl-terminal hydrolase 41

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 41
Ubiquitin thioesterase 41
Ubiquitin-specific-processing protease 41
Gene names
Name:USP41
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May recognize and hydrolyze the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins By similarity.

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).

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Putative ubiquitin carboxyl-terminal hydrolase 41
PRO_0000328882

Regions

Domain55 – 358304USP

Sites

Active site641Nucleophile By similarity
Active site3181Proton acceptor By similarity

Natural variations

Natural variant1301Y → C.
Corresponds to variant rs2542134 [ dbSNP | Ensembl ].
VAR_042574
Natural variant3251N → S.
Corresponds to variant rs2277833 [ dbSNP | Ensembl ].
VAR_042575

Experimental info

Sequence conflict1341L → V in CAE47749. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q3LFD5 [UniParc].

Last modified April 8, 2008. Version 2.
Checksum: 6CBF79560927FB11

FASTA35841,394
        10         20         30         40         50         60 
MDGVLFRAHQ CQYVHPCVHV YVTVGLMDPL CERKEKASKQ ERENPLAHLA AWGLVGLHNI 

        70         80         90        100        110        120 
GQTCCLNSLI QVFVMNVDFA RILKRITVPR GADEQRRSVP FQMLLLLEKM QDSRQKAVWP 

       130        140        150        160        170        180 
LELAYCLQKY NVPLFVQHDA AQLYLKLWNL IKDQIADVHL VERLQALYMI RMKDSLICLD 

       190        200        210        220        230        240 
CAMESSRNSS MLTLRLSFFD VDSKPLKTLE DALHCFFQPR ELSSKSKCFC ENCGKKTRGK 

       250        260        270        280        290        300 
QVLKLTHLPQ TLTIHLMRFS IRNSQTRKIC HSLYFPQSLD FSQILPMKRE SCDAEEQSGG 

       310        320        330        340        350 
QYELFAVIAH VGMADSGHYC VYIRNAVDGK WFCFNDSNIC LVSWEDIQCT YGNPNYHW 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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] OF 32-358.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC007731 Genomic DNA. No translation available.
AJ583822 mRNA. Translation: CAE47749.1.
AJ586979 mRNA. Translation: CAE52971.1.
UniGeneHs.38260.

3D structure databases

ProteinModelPortalQ3LFD5.
SMRQ3LFD5. Positions 53-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ3LFD5. 1 interaction.
STRING9606.ENSP00000414922.

Protein family/group databases

MEROPSC19.070.

PTM databases

PhosphoSiteQ3LFD5.

Polymorphism databases

DMDM182702223.

Proteomic databases

PaxDbQ3LFD5.
PRIDEQ3LFD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000454608; ENSP00000414922; ENSG00000161133.
UCSCuc011ahq.1. human.

Organism-specific databases

GeneCardsGC22M020704.
HGNCHGNC:20070. USP41.
neXtProtNX_Q3LFD5.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5077.
HOGENOMHOG000294166.
HOVERGENHBG054189.
InParanoidQ3LFD5.
PhylomeDBQ3LFD5.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeQ3LFD5.
CleanExHS_USP41.
GenevestigatorQ3LFD5.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ3LFD5.

Entry information

Entry nameUBP41_HUMAN
AccessionPrimary (citable) accession number: Q3LFD5
Secondary accession number(s): A8MXD0, Q70BM7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 8, 2008
Last modified: April 16, 2014
This is version 60 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

Peptidase families

Classification of peptidase families and list of entries

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 22

Human chromosome 22: entries, gene names and cross-references to MIM