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Q70EL2

- UBP45_HUMAN

UniProt

Q70EL2 - UBP45_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 45

Gene

USP45

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei199 – 1991NucleophilePROSITE-ProRule annotation
Active sitei746 – 7461Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri60 – 13677UBP-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: FlyBase
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein deubiquitination Source: FlyBase
  2. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC19.064.

Names & Taxonomyi

Protein namesi
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 namesi
Name:USP45
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:20080. USP45.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134889604.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 814814Ubiquitin carboxyl-terminal hydrolase 45PRO_0000280561Add
BLAST

Proteomic databases

MaxQBiQ70EL2.
PaxDbiQ70EL2.
PRIDEiQ70EL2.

PTM databases

PhosphoSiteiQ70EL2.

Expressioni

Tissue specificityi

Broadly expressed, with highest levels in ovary, skeletal muscle and spleen.1 Publication

Gene expression databases

BgeeiQ70EL2.
CleanExiHS_USP45.
ExpressionAtlasiQ70EL2. baseline and differential.
GenevestigatoriQ70EL2.

Organism-specific databases

HPAiHPA029602.
HPA029604.

Interactioni

Protein-protein interaction databases

BioGridi124430. 22 interactions.
IntActiQ70EL2. 21 interactions.
STRINGi9606.ENSP00000333376.

Structurei

3D structure databases

ProteinModelPortaliQ70EL2.
SMRiQ70EL2. Positions 38-388, 603-810.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini190 – 813624USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri60 – 13677UBP-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5207.
GeneTreeiENSGT00760000119203.
HOGENOMiHOG000154755.
HOVERGENiHBG062704.
InParanoidiQ70EL2.
KOiK11844.
OMAiRIMKLCE.
OrthoDBiEOG7J9VNZ.
PhylomeDBiQ70EL2.
TreeFamiTF326075.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q70EL2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRVKDPTKAL PEKAKRSKRP TVPHDEDSSD DIAVGLTCQH VSHAISVNHV
60 70 80 90 100
KRAIAENLWS VCSECLKERR FYDGQLVLTS DIWLCLKCGF QGCGKNSESQ
110 120 130 140 150
HSLKHFKSSR TEPHCIIINL STWIIWCYEC DEKLSTHCNK KVLAQIVDFL
160 170 180 190 200
QKHASKTQTS AFSRIMKLCE EKCETDEIQK GGKCRNLSVR GITNLGNTCF
210 220 230 240 250
FNAVMQNLAQ TYTLTDLMNE IKESSTKLKI FPSSDSQLDP LVVELSRPGP
260 270 280 290 300
LTSALFLFLH SMKETEKGPL SPKVLFNQLC QKAPRFKDFQ QQDSQELLHY
310 320 330 340 350
LLDAVRTEET KRIQASILKA FNNPTTKTAD DETRKKVKAY GKEGVKMNFI
360 370 380 390 400
DRIFIGELTS TVMCEECANI STVKDPFIDI SLPIIEERVS KPLLWGRMNK
410 420 430 440 450
YRSLRETDHD RYSGNVTIEN IHQPRAAKKH SSSKDKSQLI HDRKCIRKLS
460 470 480 490 500
SGETVTYQKN ENLEMNGDSL MFASLMNSES RLNESPTDDS EKEASHSESN
510 520 530 540 550
VDADSEPSES ESASKQTGLF RSSSGSGVQP DGPLYPLSAG KLLYTKETDS
560 570 580 590 600
GDKEMAEAIS ELRLSSTVTG DQDFDRENQP LNISNNLCFL EGKHLRSYSP
610 620 630 640 650
QNAFQTLSQS YITTSKECSI QSCLYQFTSM ELLMGNNKLL CENCTKNKQK
660 670 680 690 700
YQEETSFAEK KVEGVYTNAR KQLLISAVPA VLILHLKRFH QAGLSLRKVN
710 720 730 740 750
RHVDFPLMLD LAPFCSATCK NASVGDKVLY GLYGIVEHSG SMREGHYTAY
760 770 780 790 800
VKVRTPSRKL SEHNTKKKNV PGLKAADNES AGQWVHVSDT YLQVVPESRA
810
LSAQAYLLFY ERVL
Length:814
Mass (Da):91,733
Last modified:May 18, 2010 - v3
Checksum:iDE4FCC0AD7AD6499
GO
Isoform 2 (identifier: Q70EL2-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:289
Mass (Da):32,735
Checksum:iB961DAA98F82939B
GO
Isoform 3 (identifier: Q70EL2-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:494
Mass (Da):55,812
Checksum:iE66E1435C4CAFA37
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti603 – 6031A → V in CAD91148. (PubMed:17974005)Curated
Sequence conflicti691 – 6911Q → K in CAE47746. (PubMed:14715245)Curated
Sequence conflicti726 – 7261D → G in CAD89915. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671K → E.1 Publication
Corresponds to variant rs7744845 [ dbSNP | Ensembl ].
VAR_031167
Natural varianti521 – 5211R → T.1 Publication
Corresponds to variant rs41288947 [ dbSNP | Ensembl ].
VAR_060663
Natural varianti778 – 7781N → S.2 Publications
Corresponds to variant rs6570065 [ dbSNP | Ensembl ].
VAR_031168

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 262262Missing in isoform 3. 1 PublicationVSP_023789Add
BLAST
Alternative sequencei263 – 28220KETEK…QLCQK → MRSKKVVQNSRFFLPQTLSW in isoform 3. 1 PublicationVSP_023790Add
BLAST
Alternative sequencei283 – 2897APRFKDF → RVHLHLI in isoform 2. 1 PublicationVSP_023791
Alternative sequencei290 – 814525Missing in isoform 2. 1 PublicationVSP_023792Add
BLAST
Alternative sequencei312 – 36958Missing in isoform 3. 1 PublicationVSP_023793Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34501.1. [Q70EL2-1]
RefSeqiNP_001073950.1. NM_001080481.1. [Q70EL2-1]
XP_005267226.1. XM_005267169.1. [Q70EL2-1]
XP_005267227.1. XM_005267170.2. [Q70EL2-1]
UniGeneiHs.143410.

Genome annotation databases

EnsembliENST00000327681; ENSP00000333376; ENSG00000123552. [Q70EL2-1]
ENST00000500704; ENSP00000424372; ENSG00000123552. [Q70EL2-1]
GeneIDi85015.
KEGGihsa:85015.
UCSCiuc003ppw.2. human. [Q70EL2-3]
uc003ppx.2. human. [Q70EL2-1]

Polymorphism databases

DMDMi296453002.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34501.1. [Q70EL2-1 ]
RefSeqi NP_001073950.1. NM_001080481.1. [Q70EL2-1 ]
XP_005267226.1. XM_005267169.1. [Q70EL2-1 ]
XP_005267227.1. XM_005267170.2. [Q70EL2-1 ]
UniGenei Hs.143410.

3D structure databases

ProteinModelPortali Q70EL2.
SMRi Q70EL2. Positions 38-388, 603-810.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124430. 22 interactions.
IntActi Q70EL2. 21 interactions.
STRINGi 9606.ENSP00000333376.

Protein family/group databases

MEROPSi C19.064.

PTM databases

PhosphoSitei Q70EL2.

Polymorphism databases

DMDMi 296453002.

Proteomic databases

MaxQBi Q70EL2.
PaxDbi Q70EL2.
PRIDEi Q70EL2.

Protocols and materials databases

DNASUi 85015.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327681 ; ENSP00000333376 ; ENSG00000123552 . [Q70EL2-1 ]
ENST00000500704 ; ENSP00000424372 ; ENSG00000123552 . [Q70EL2-1 ]
GeneIDi 85015.
KEGGi hsa:85015.
UCSCi uc003ppw.2. human. [Q70EL2-3 ]
uc003ppx.2. human. [Q70EL2-1 ]

Organism-specific databases

CTDi 85015.
GeneCardsi GC06M099925.
H-InvDB HIX0006090.
HGNCi HGNC:20080. USP45.
HPAi HPA029602.
HPA029604.
neXtProti NX_Q70EL2.
PharmGKBi PA134889604.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5207.
GeneTreei ENSGT00760000119203.
HOGENOMi HOG000154755.
HOVERGENi HBG062704.
InParanoidi Q70EL2.
KOi K11844.
OMAi RIMKLCE.
OrthoDBi EOG7J9VNZ.
PhylomeDBi Q70EL2.
TreeFami TF326075.

Miscellaneous databases

ChiTaRSi USP45. human.
GenomeRNAii 85015.
NextBioi 75631.
PROi Q70EL2.

Gene expression databases

Bgeei Q70EL2.
CleanExi HS_USP45.
ExpressionAtlasi Q70EL2. baseline and differential.
Genevestigatori Q70EL2.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiUBP45_HUMAN
AccessioniPrimary (citable) accession number: Q70EL2
Secondary accession number(s): B2RXG0
, Q5T062, Q86T44, Q86TC0, Q9BRU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3