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Q86UV5 (UBP48_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 48

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 48
Ubiquitin thioesterase 48
Ubiquitin-specific-processing protease 48
Gene names
Name:USP48
Synonyms:USP31
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1035 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Recognizes and hydrolyzes 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. May be involved in the regulation of NF-kappa-B activation by TNF receptor superfamily via its interactions with RELA and TRAF2. May also play a regulatory role at postsynaptic sites. Ref.8

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.8

Subunit structure

Interacts with TRAF2 and RELA. Ref.8

Subcellular location

Cytoplasm. Nucleus Ref.8.

Tissue specificity

Widely expressed. Ref.1 Ref.6 Ref.8

Sequence similarities

Belongs to the peptidase C19 family.

Contains 3 DUSP domains.

Contains 1 ubiquitin-like domain.

Contains 1 USP domain.

Caution

Was termed (Ref.1 and Ref.7) USP31.

Sequence caution

The sequence AAH13567.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH67261.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAI03725.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAA92128.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI12124.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16260.1 differs from that shown. Reason: Erroneous gene model prediction.

Isoform 5: The sequence BAB15533.1 differs from that shown. Reason: Frameshift at position 109.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionubiquitin-specific protease activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86UV5-1)

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: Q86UV5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     909-960: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q86UV5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     704-1035: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q86UV5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     369-392: FNDEDIEKMEGKKLQLGIEEDLAE → LILNTNYHLPPSPKPIKIKNYNKP
     393-1035: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q86UV5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-469: Missing.
     470-483: EEVKELYQRLPAGA → MNLSLSQKTVKIHRLFPMLAFS
     589-589: Missing.
     909-960: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q86UV5-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-875: Missing.
     1020-1035: VCMPEEGFKGTGLLGH → GKDEFVLGIC
Note: No experimental confirmation available.
Isoform 7 (identifier: Q86UV5-7)

Also known as: USP31S1;

The sequence of this isoform differs from the canonical sequence as follows:
     484-485: EP → GL
     486-1035: Missing.
Isoform 8 (identifier: Q86UV5-8)

The sequence of this isoform differs from the canonical sequence as follows:
     391-391: Missing.
     654-654: H → HAVFFFSKYIFLNS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10351035Ubiquitin carboxyl-terminal hydrolase 48
PRO_0000249523

Regions

Domain89 – 421333USP
Domain460 – 55495DUSP 1
Domain569 – 691123DUSP 2
Domain711 – 824114DUSP 3
Domain929 – 100981Ubiquitin-like

Sites

Active site981Nucleophile By similarity
Active site3531Proton acceptor By similarity

Amino acid modifications

Modified residue8861Phosphoserine Ref.11 Ref.13
Modified residue8871Phosphoserine Ref.11
Modified residue8881Phosphoserine Ref.11 Ref.13
Modified residue9561N6-acetyllysine Ref.10

Natural variations

Alternative sequence1 – 875875Missing in isoform 6.
VSP_020471
Alternative sequence1 – 469469Missing in isoform 5.
VSP_020472
Alternative sequence369 – 39224FNDED…EDLAE → LILNTNYHLPPSPKPIKIKN YNKP in isoform 4.
VSP_020473
Alternative sequence3911Missing in isoform 8.
VSP_054487
Alternative sequence393 – 1035643Missing in isoform 4.
VSP_020474
Alternative sequence470 – 48314EEVKE…LPAGA → MNLSLSQKTVKIHRLFPMLA FS in isoform 5.
VSP_020475
Alternative sequence484 – 4852EP → GL in isoform 7.
VSP_020476
Alternative sequence486 – 1035550Missing in isoform 7.
VSP_020477
Alternative sequence5891Missing in isoform 5.
VSP_020478
Alternative sequence6541H → HAVFFFSKYIFLNS in isoform 8.
VSP_054488
Alternative sequence704 – 1035332Missing in isoform 3.
VSP_020479
Alternative sequence909 – 96052Missing in isoform 2 and isoform 5.
VSP_020480
Alternative sequence1020 – 103516VCMPE…GLLGH → GKDEFVLGIC in isoform 6.
VSP_020481
Natural variant1251S → C.
Corresponds to variant rs4253886 [ dbSNP | Ensembl ].
VAR_027427
Natural variant1351E → K.
Corresponds to variant rs12097805 [ dbSNP | Ensembl ].
VAR_027428

Sequences

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

Last modified June 1, 2003. Version 1.
Checksum: 6F7DAF88527E2627

FASTA1,035119,032
        10         20         30         40         50         60 
MAPRLQLEKA AWRWAETVRP EEVSQEHIET AYRIWLEPCI RGVCRRNCKG NPNCLVGIGE 

        70         80         90        100        110        120 
HIWLGEIDEN SFHNIDDPNC ERRKKNSFVG LTNLGATCYV NTFLQVWFLN LELRQALYLC 

       130        140        150        160        170        180 
PSTCSDYMLG DGIQEEKDYE PQTICEHLQY LFALLQNSNR RYIDPSGFVK ALGLDTGQQQ 

       190        200        210        220        230        240 
DAQEFSKLFM SLLEDTLSKQ KNPDVRNIVQ QQFCGEYAYV TVCNQCGRES KLLSKFYELE 

       250        260        270        280        290        300 
LNIQGHKQLT DCISEFLKEE KLEGDNRYFC ENCQSKQNAT RKIRLLSLPC TLNLQLMRFV 

       310        320        330        340        350        360 
FDRQTGHKKK LNTYIGFSEI LDMEPYVEHK GGSYVYELSA VLIHRGVSAY SGHYIAHVKD 

       370        380        390        400        410        420 
PQSGEWYKFN DEDIEKMEGK KLQLGIEEDL AEPSKSQTRK PKCGKGTHCS RNAYMLVYRL 

       430        440        450        460        470        480 
QTQEKPNTTV QVPAFLQELV DRDNSKFEEW CIEMAEMRKQ SVDKGKAKHE EVKELYQRLP 

       490        500        510        520        530        540 
AGAEPYEFVS LEWLQKWLDE STPTKPIDNH ACLCSHDKLH PDKISIMKRI SEYAADIFYS 

       550        560        570        580        590        600 
RYGGGPRLTV KALCKECVVE RCRILRLKNQ LNEDYKTVNN LLKAAVKGSD GFWVGKSSLR 

       610        620        630        640        650        660 
SWRQLALEQL DEQDGDAEQS NGKMNGSTLN KDESKEERKE EEELNFNEDI LCPHGELCIS 

       670        680        690        700        710        720 
ENERRLVSKE AWSKLQQYFP KAPEFPSYKE CCSQCKILER EGEENEALHK MIANEQKTSL 

       730        740        750        760        770        780 
PNLFQDKNRP CLSNWPEDTD VLYIVSQFFV EEWRKFVRKP TRCSPVSSVG NSALLCPHGG 

       790        800        810        820        830        840 
LMFTFASMTK EDSKLIALIW PSEWQMIQKL FVVDHVIKIT RIEVGDVNPS ETQYISEPKL 

       850        860        870        880        890        900 
CPECREGLLC QQQRDLREYT QATIYVHKVV DNKKVMKDSA PELNVSSSET EEDKEEAKPD 

       910        920        930        940        950        960 
GEKDPDFNQS NGGTKRQKIS HQNYIAYQKQ VIRRSMRHRK VRGEKALLVS ANQTLKELKI 

       970        980        990       1000       1010       1020 
QIMHAFSVAP FDQNLSIDGK ILSDDCATLG TLGVIPESVI LLKADEPIAD YAAMDDVMQV 

      1030 
CMPEEGFKGT GLLGH 

« Hide

Isoform 2 [UniParc].

Checksum: B19F5EC40029858F
Show »

FASTA983112,959
Isoform 3 [UniParc].

Checksum: A7608F78005CF98D
Show »

FASTA70381,449
Isoform 4 [UniParc].

Checksum: 675B208E4EFA5350
Show »

FASTA39245,481
Isoform 5 [UniParc].

Checksum: 20D3FA1221CF6383
Show »

FASTA52159,454
Isoform 6 [UniParc].

Checksum: C8309D66B49A9AF6
Show »

FASTA15417,094
Isoform 7 (USP31S1) [UniParc].

Checksum: E519B70ABF229820
Show »

FASTA48556,151
Isoform 8 [UniParc].

Checksum: 6DD9F285164E7ADD
Show »

FASTA1,047120,526

References

« Hide 'large scale' references
[1]"Identification of the human ubiquitin specific protease 31 (USP31) gene: structure, sequence and expression analysis."
Lockhart P.J., Hulihan M., Lincoln S., Hussey J., Skipper L., Bisceglio G., Wilkes K., Farrer M.J.
DNA Seq. 15:9-14(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 712-1035 (ISOFORM 1).
Tissue: Colon, Hepatoma and Placenta.
[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 2 AND 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 399-1035 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-636 (ISOFORMS 1/2).
Tissue: Colon, Eye, Pancreas, Skin and Uterus.
[5]"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] OF 691-1035 (ISOFORM 1).
Tissue: Melanoma.
[6]"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: TISSUE SPECIFICITY.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB."
Tzimas C., Michailidou G., Arsenakis M., Kieff E., Mosialos G., Hatzivassiliou E.G.
Cell. Signal. 18:83-92(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 7), ENZYME ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RELA AND TRAF2.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886; SER-887 AND SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886 AND SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF502942 mRNA. Translation: AAP30832.1.
AL590103 Genomic DNA. Translation: CAI12124.1. Sequence problems.
AL590103, AL359815 Genomic DNA. Translation: CAI12127.1.
AL359815, AL590103 Genomic DNA. Translation: CAI16256.1.
AL359815 Genomic DNA. Translation: CAI16260.1. Sequence problems.
AK000110 mRNA. Translation: BAA90950.1.
AK002190 mRNA. Translation: BAA92128.1. Different initiation.
AK026707 mRNA. Translation: BAB15533.1. Frameshift.
AK026930 mRNA. Translation: BAB15591.1.
BC007326 mRNA. Translation: AAH07326.2.
BC013567 mRNA. Translation: AAH13567.1. Different initiation.
BC067261 mRNA. Translation: AAH67261.1. Sequence problems.
BC103724 mRNA. Translation: AAI03725.1. Sequence problems.
BC104896 mRNA. Translation: AAI04897.1.
BC143354 mRNA. Translation: AAI43355.1.
AL834375 mRNA. Translation: CAD39038.1.
CCDSCCDS30623.1. [Q86UV5-1]
CCDS44084.1. [Q86UV5-7]
RefSeqNP_001027902.1. NM_001032730.1. [Q86UV5-7]
NP_115612.4. NM_032236.5. [Q86UV5-1]
XP_005246066.1. XM_005246009.1. [Q86UV5-2]
UniGeneHs.467524.

3D structure databases

ProteinModelPortalQ86UV5.
SMRQ86UV5. Positions 84-442, 945-996.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123941. 13 interactions.
IntActQ86UV5. 3 interactions.
MINTMINT-7944238.

Protein family/group databases

MEROPSC19.068.

PTM databases

PhosphoSiteQ86UV5.

Polymorphism databases

DMDM74750436.

Proteomic databases

MaxQBQ86UV5.
PaxDbQ86UV5.
PRIDEQ86UV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308271; ENSP00000309262; ENSG00000090686. [Q86UV5-1]
ENST00000400301; ENSP00000383157; ENSG00000090686. [Q86UV5-2]
ENST00000421625; ENSP00000406256; ENSG00000090686. [Q86UV5-7]
ENST00000529637; ENSP00000431949; ENSG00000090686.
GeneID84196.
KEGGhsa:84196.
UCSCuc001bfa.3. human. [Q86UV5-5]
uc001bfb.3. human. [Q86UV5-1]
uc001bfc.3. human. [Q86UV5-2]
uc001bfd.1. human. [Q86UV5-6]
uc001bff.3. human. [Q86UV5-7]

Organism-specific databases

CTD84196.
GeneCardsGC01M022004.
HGNCHGNC:18533. USP48.
HPAHPA030045.
HPA030046.
HPA053976.
neXtProtNX_Q86UV5.
PharmGKBPA134947522.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5077.
HOVERGENHBG080368.
InParanoidQ86UV5.
KOK11858.
OrthoDBEOG72G16G.
PhylomeDBQ86UV5.
TreeFamTF106280.

Gene expression databases

ArrayExpressQ86UV5.
BgeeQ86UV5.
CleanExHS_USP31.
HS_USP48.
GenevestigatorQ86UV5.

Family and domain databases

Gene3D3.30.2230.10. 1 hit.
InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
SUPFAMSSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEPS51283. DUSP. 3 hits.
PS50053. UBIQUITIN_2. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
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Other

ChiTaRSUSP48. human.
GeneWikiUSP48.
GenomeRNAi84196.
NextBio35481187.
PROQ86UV5.

Entry information

Entry nameUBP48_HUMAN
AccessionPrimary (citable) accession number: Q86UV5
Secondary accession number(s): B7ZKS7 expand/collapse secondary AC list , Q2M3I4, Q5SZI4, Q5T3T5, Q6NX53, Q8N3F6, Q96F64, Q96IQ3, Q9H5N3, Q9H5T7, Q9NUJ6, Q9NXR0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 109 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 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 1

Human chromosome 1: entries, gene names and cross-references to MIM