Q70EL2 (UBP45_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 45
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 45
Ubiquitin thioesterase 45
Ubiquitin-specific-processing protease 45

Gene names

Name:

USP45

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	814 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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
Tissue specificity	Broadly expressed, with highest levels in ovary, skeletal muscle and spleen. Ref.1
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 UBP-type zinc finger.
Sequence caution	The sequence CAI17192.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI19761.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
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 zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q70EL2-1)

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: Q70EL2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     283-289: APRFKDF → RVHLHLI
     290-814: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q70EL2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-262: Missing.
     263-282: KETEKGPLSPKVLFNQLCQK → MRSKKVVQNSRFFLPQTLSW
     312-369: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 814	814	Ubiquitin carboxyl-terminal hydrolase 45		PRO_0000280561
Regions
	Zinc finger	60 – 136	77	UBP-type
Sites
	Active site	199	1	Nucleophile By similarity
	Active site	746	1	Proton acceptor By similarity
Natural variations
	Alternative sequence	1 – 262	262	Missing in isoform 3.		VSP_023789
	Alternative sequence	263 – 282	20	KETEK…QLCQK → MRSKKVVQNSRFFLPQTLSW in isoform 3.		VSP_023790
	Alternative sequence	283 – 289	7	APRFKDF → RVHLHLI in isoform 2.		VSP_023791
	Alternative sequence	290 – 814	525	Missing in isoform 2.		VSP_023792
	Alternative sequence	312 – 369	58	Missing in isoform 3.		VSP_023793
	Natural variant	67	1	K → E. Ref.4 Corresponds to variant rs7744845 [ dbSNP | Ensembl ].		VAR_031167
	Natural variant	521	1	R → T. Ref.4 Corresponds to variant rs41288947 [ dbSNP | Ensembl ].		VAR_060663
	Natural variant	778	1	N → S. Ref.2 Ref.4 Corresponds to variant rs6570065 [ dbSNP | Ensembl ].		VAR_031168
Experimental info
	Sequence conflict	603	1	A → V in CAD91148. Ref.2
	Sequence conflict	691	1	Q → K in CAE47746. Ref.1
	Sequence conflict	726	1	D → G in CAD89915. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: DE4FCC0AD7AD6499	FASTA	814	91,733
	10 20 30 40 50 60 MRVKDPTKAL PEKAKRSKRP TVPHDEDSSD DIAVGLTCQH VSHAISVNHV KRAIAENLWS 70 80 90 100 110 120 VCSECLKERR FYDGQLVLTS DIWLCLKCGF QGCGKNSESQ HSLKHFKSSR TEPHCIIINL 130 140 150 160 170 180 STWIIWCYEC DEKLSTHCNK KVLAQIVDFL QKHASKTQTS AFSRIMKLCE EKCETDEIQK 190 200 210 220 230 240 GGKCRNLSVR GITNLGNTCF FNAVMQNLAQ TYTLTDLMNE IKESSTKLKI FPSSDSQLDP 250 260 270 280 290 300 LVVELSRPGP LTSALFLFLH SMKETEKGPL SPKVLFNQLC QKAPRFKDFQ QQDSQELLHY 310 320 330 340 350 360 LLDAVRTEET KRIQASILKA FNNPTTKTAD DETRKKVKAY GKEGVKMNFI DRIFIGELTS 370 380 390 400 410 420 TVMCEECANI STVKDPFIDI SLPIIEERVS KPLLWGRMNK YRSLRETDHD RYSGNVTIEN 430 440 450 460 470 480 IHQPRAAKKH SSSKDKSQLI HDRKCIRKLS SGETVTYQKN ENLEMNGDSL MFASLMNSES 490 500 510 520 530 540 RLNESPTDDS EKEASHSESN VDADSEPSES ESASKQTGLF RSSSGSGVQP DGPLYPLSAG 550 560 570 580 590 600 KLLYTKETDS GDKEMAEAIS ELRLSSTVTG DQDFDRENQP LNISNNLCFL EGKHLRSYSP 610 620 630 640 650 660 QNAFQTLSQS YITTSKECSI QSCLYQFTSM ELLMGNNKLL CENCTKNKQK YQEETSFAEK 670 680 690 700 710 720 KVEGVYTNAR KQLLISAVPA VLILHLKRFH QAGLSLRKVN RHVDFPLMLD LAPFCSATCK 730 740 750 760 770 780 NASVGDKVLY GLYGIVEHSG SMREGHYTAY VKVRTPSRKL SEHNTKKKNV PGLKAADNES 790 800 810 AGQWVHVSDT YLQVVPESRA LSAQAYLLFY ERVL
	Isoform 2 [UniParc]. Checksum: B961DAA98F82939B	FASTA	289	32,735
	10 20 30 40 50 60 MRVKDPTKAL PEKAKRSKRP TVPHDEDSSD DIAVGLTCQH VSHAISVNHV KRAIAENLWS 70 80 90 100 110 120 VCSECLKERR FYDGQLVLTS DIWLCLKCGF QGCGKNSESQ HSLKHFKSSR TEPHCIIINL 130 140 150 160 170 180 STWIIWCYEC DEKLSTHCNK KVLAQIVDFL QKHASKTQTS AFSRIMKLCE EKCETDEIQK 190 200 210 220 230 240 GGKCRNLSVR GITNLGNTCF FNAVMQNLAQ TYTLTDLMNE IKESSTKLKI FPSSDSQLDP 250 260 270 280 LVVELSRPGP LTSALFLFLH SMKETEKGPL SPKVLFNQLC QKRVHLHLI
	Isoform 3 [UniParc]. Checksum: E66E1435C4CAFA37	FASTA	494	55,812
	10 20 30 40 50 60 MRSKKVVQNS RFFLPQTLSW APRFKDFQQQ DSQELLHYLL DAVRTEETKI STVKDPFIDI 70 80 90 100 110 120 SLPIIEERVS KPLLWGRMNK YRSLRETDHD RYSGNVTIEN IHQPRAAKKH SSSKDKSQLI 130 140 150 160 170 180 HDRKCIRKLS SGETVTYQKN ENLEMNGDSL MFASLMNSES RLNESPTDDS EKEASHSESN 190 200 210 220 230 240 VDADSEPSES ESASKQTGLF RSSSGSGVQP DGPLYPLSAG KLLYTKETDS GDKEMAEAIS 250 260 270 280 290 300 ELRLSSTVTG DQDFDRENQP LNISNNLCFL EGKHLRSYSP QNAFQTLSQS YITTSKECSI 310 320 330 340 350 360 QSCLYQFTSM ELLMGNNKLL CENCTKNKQK YQEETSFAEK KVEGVYTNAR KQLLISAVPA 370 380 390 400 410 420 VLILHLKRFH QAGLSLRKVN RHVDFPLMLD LAPFCSATCK NASVGDKVLY GLYGIVEHSG 430 440 450 460 470 480 SMREGHYTAY VKVRTPSRKL SEHNTKKKNV PGLKAADNES AGQWVHVSDT YLQVVPESRA 490 LSAQAYLLFY ERVL

References

	« Hide 'large scale' referencesShow '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), CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[2]	"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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-814 (ISOFORM 1), VARIANT SER-778. Tissue: Skeletal muscle.
[3]	"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].
[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] (ISOFORMS 1 AND 2), VARIANTS GLU-67; THR-521 AND SER-778. Tissue: Bone marrow and Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ583819 mRNA. Translation: CAE47746.2. AL713747 mRNA. Translation: CAD89915.1. AL832030 mRNA. Translation: CAD91148.1. AL513550, AL137784 Genomic DNA. Translation: CAI17192.1. Sequence problems. AL137784, AL513550 Genomic DNA. Translation: CAI19761.1. Sequence problems. BC005991 mRNA. Translation: AAH05991.1. BC150648 mRNA. Translation: AAI50649.1. BC157838 mRNA. Translation: AAI57839.1.
IPI	IPI00736634. IPI00738106. IPI00967505.
RefSeq	NP_001073950.1. NM_001080481.1.
UniGene	Hs.143410.
3D structure databases
HSSP	HSSP built from PDB template 2GFO based on UniProtKB P40818.
ProteinModelPortal	Q70EL2.
SMR	Q70EL2. Positions 38-388, 603-810.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q70EL2. 21 interactions.
STRING	9606.ENSP00000333376.
Protein family/group databases
MEROPS	C19.064.
PTM databases
PhosphoSite	Q70EL2.
Polymorphism databases
DMDM	296453002.
Proteomic databases
PaxDb	Q70EL2.
PRIDE	Q70EL2.
Protocols and materials databases
DNASU	85015.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000327681; ENSP00000333376; ENSG00000123552. ENST00000392738; ENSP00000376495; ENSG00000123552. ENST00000500704; ENSP00000424372; ENSG00000123552.
GeneID	85015.
KEGG	hsa:85015.
UCSC	uc003ppw.2. human. uc003ppx.2. human.
Organism-specific databases
CTD	85015.
GeneCards	GC06M099925.
H-InvDB	HIX0006090.
HGNC	HGNC:20080. USP45.
HPA	HPA029602. HPA029604.
neXtProt	NX_Q70EL2.
PharmGKB	PA134889604.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5207.
HOGENOM	HOG000154755.
HOVERGEN	HBG062704.
InParanoid	Q70EL2.
KO	K11844.
OMA	CEEKCET.
Gene expression databases
ArrayExpress	Q70EL2.
Bgee	Q70EL2.
CleanEx	HS_USP45.
Genevestigator	Q70EL2.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR013083. Znf_RING/FYVE/PHD. IPR001607. Znf_UBP. [Graphical view]
Pfam	PF00443. UCH. 1 hit. PF02148. zf-UBP. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. PS50271. ZF_UBP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	USP45. human.
GenomeRNAi	85015.
NextBio	75631.

Entry information

Entry name

UBP45_HUMAN

Accession

Primary (citable) accession number: Q70EL2
Secondary accession number(s): B2RXG0 , Q5T062, Q86T44, Q86TC0, Q9BRU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 78 of the entry and version 3 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.