Q3LFD5 (UBP41_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 358	358	Putative ubiquitin carboxyl-terminal hydrolase 41		PRO_0000328882
Sites
	Active site	64	1	Nucleophile By similarity
	Active site	318	1	Proton acceptor By similarity
Natural variations
	Natural variant	130	1	Y → C. Corresponds to variant rs2542134 [ dbSNP | Ensembl ].		VAR_042574
	Natural variant	325	1	N → S. Corresponds to variant rs2277833 [ dbSNP | Ensembl ].		VAR_042575
Experimental info
	Sequence conflict	134	1	L → V in CAE47749. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q3LFD5 [UniParc]. Last modified April 8, 2008. Version 2. Checksum: 6CBF79560927FB11	FASTA	358	41,394
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00908904.
UniGene	Hs.38260.
3D structure databases
HSSP	HSSP built from PDB template 2AYN based on UniProtKB P54578.
ProteinModelPortal	Q3LFD5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q3LFD5. 1 interaction.
STRING	9606.ENSP00000414922.
Protein family/group databases
MEROPS	C19.070.
PTM databases
PhosphoSite	Q3LFD5.
Polymorphism databases
DMDM	182702223.
Proteomic databases
PaxDb	Q3LFD5.
PRIDE	Q3LFD5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000454608; ENSP00000414922; ENSG00000161133.
UCSC	uc011ahq.1. human.
Organism-specific databases
GeneCards	GC22M020704.
HGNC	HGNC:20070. USP41.
neXtProt	NX_Q3LFD5.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5077.
HOGENOM	HOG000294166.
HOVERGEN	HBG054189.
InParanoid	Q3LFD5.
Gene expression databases
Bgee	Q3LFD5.
CleanEx	HS_USP41.
Genevestigator	Q3LFD5.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBP41_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.