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O94966 (UBP19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 19

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 19
Ubiquitin thioesterase 19
Ubiquitin-specific-processing protease 19
Zinc finger MYND domain-containing protein 9
Gene names
Name:USP19
Synonyms:KIAA0891, ZMYND9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1318 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains. Ref.6 Ref.9 Ref.10 Ref.11

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).

Subunit structure

Interacts with RNF123 By similarity. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with HIF1A (via N-terminus). Ref.9 Ref.11

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Ref.6.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 2 CS domains.

Contains 1 MYND-type zinc finger.

Contains 1 USP domain.

Sequence caution

The sequence AAI06030.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAI06030.1 differs from that shown. Reason: Frameshift at position 572.

The sequence AAI42661.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA74914.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Transmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.6. Source: UniProtKB

negative regulation of skeletal muscle tissue development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell cycle process

Inferred from sequence or structural similarity. Source: UniProtKB

protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cellular response to hypoxia

Inferred from mutant phenotype Ref.11. Source: UniProtKB

regulation of protein stability

Inferred from sequence or structural similarity. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from expression pattern Ref.6. Source: UniProtKB

skeletal muscle atrophy

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from direct assay Ref.6. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.9Ref.11. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O94966-1)

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: O94966-2)

The sequence of this isoform differs from the canonical sequence as follows:
     100-114: Missing.
     202-202: L → LKKPLGTQEL...PPFVADPATQ
     573-574: IV → RL
     575-1318: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O94966-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1244-1298: ASRIWQELEA...LRYFVLGTVA → GLGPGQAPEV...PTYSNMEEVD
     1299-1318: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: O94966-4)

The sequence of this isoform differs from the canonical sequence as follows:
     100-114: Missing.
     389-389: R → RGA
     1244-1298: ASRIWQELEA...LRYFVLGTVA → GLGPGQAPEV...PTYSNMEEVD
     1299-1318: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: O94966-5)

The sequence of this isoform differs from the canonical sequence as follows:
     202-202: L → LKKPLGTQEL...PPFVADPATQ
Note: No experimental confirmation available.
Isoform 6 (identifier: O94966-6)

The sequence of this isoform differs from the canonical sequence as follows:
     202-202: L → LKKPLGTQEL...PPFVADPATQ
     389-389: R → RGA
     1244-1298: ASRIWQELEA...LRYFVLGTVA → GLGPGQAPEV...PTYSNMEEVD
     1299-1318: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: O94966-7)

The sequence of this isoform differs from the canonical sequence as follows:
     193-202: VPMLTWPSLL → KKPLGTQELV...PPFVADPATQ
     1244-1298: ASRIWQELEA...LRYFVLGTVA → GLGPGQAPEV...PTYSNMEEVD
     1299-1318: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13181318Ubiquitin carboxyl-terminal hydrolase 19
PRO_0000080646

Regions

Topological domain1 – 12911291Cytoplasmic Potential
Transmembrane1292 – 131221Helical; Potential
Topological domain1313 – 13186Lumenal Potential
Domain113 – 20290CS 1
Domain282 – 384103CS 2
Domain497 – 1214718USP
Zinc finger791 – 83343MYND-type

Sites

Active site5061Nucleophile By similarity
Active site11651Proton acceptor By similarity

Natural variations

Alternative sequence100 – 11415Missing in isoform 2 and isoform 4.
VSP_026708
Alternative sequence193 – 20210VPMLTWPSLL → KKPLGTQELVPGLRCQENGQ ELSPIALEPGPEPHRAKQEA RNQKRAQGRGEVGAGAGPGA QAGPSAKRAVHLCRGPEGDG SRDDPGPRGDAPPFVADPAT Q in isoform 7.
VSP_047057
Alternative sequence2021L → LKKPLGTQELVPGLRCQENG QELSPIALEPGPEPHRAKQE ARNQKRAQGRGEVGAGAGPG AQAGPSAKRAVHLCRGPEGD GSRDDPGPRGDAPPFVADPA TQ in isoform 2, isoform 5 and isoform 6.
VSP_026709
Alternative sequence3891R → RGA in isoform 4 and isoform 6.
VSP_045891
Alternative sequence573 – 5742IV → RL in isoform 2.
VSP_026710
Alternative sequence575 – 1318744Missing in isoform 2.
VSP_026711
Alternative sequence1244 – 129855ASRIW…LGTVA → GLGPGQAPEVAPTRTAPERF APPVDRPAPTYSNMEEVD in isoform 3, isoform 4, isoform 6 and isoform 7.
VSP_026712
Alternative sequence1299 – 131820Missing in isoform 3, isoform 4, isoform 6 and isoform 7.
VSP_026713
Natural variant361D → H.
Corresponds to variant rs11552724 [ dbSNP | Ensembl ].
VAR_051528

Experimental info

Sequence conflict9421S → C in BAG57894. Ref.2
Sequence conflict10411E → G in BAG62152. Ref.2
Isoform 4:
Sequence conflict12511A → T in AAH82241. Ref.4

Secondary structure

...................... 1318
Helix Strand Turn

Details...

Sequences

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

Last modified July 10, 2007. Version 2.
Checksum: EA9F318D03304AA1

FASTA1,318145,651
        10         20         30         40         50         60 
MSGGASATGP RRGPPGLEDT TSKKKQKDRA NQESKDGDPR KETGSRYVAQ AGLEPLASGD 

        70         80         90        100        110        120 
PSASASHAAG ITGSRHRTRL FFPSSSGSAS TPQEEQTKEG ACEDPHDLLA TPTPELLLDW 

       130        140        150        160        170        180 
RQSAEEVIVK LRVGVGPLQL EDVDAAFTDT DCVVRFAGGQ QWGGVFYAEI KSSCAKVQTR 

       190        200        210        220        230        240 
KGSLLHLTLP KKVPMLTWPS LLVEADEQLC IPPLNSQTCL LGSEENLAPL AGEKAVPPGN 

       250        260        270        280        290        300 
DPVSPAMVRS RNPGKDDCAK EEMAVAADAA TLVDEPESMV NLAFVKNDSY EKGPDSVVVH 

       310        320        330        340        350        360 
VYVKEICRDT SRVLFREQDF TLIFQTRDGN FLRLHPGCGP HTTFRWQVKL RNLIEPEQCT 

       370        380        390        400        410        420 
FCFTASRIDI CLRKRQSQRW GGLEAPAARV GGAKVAVPTG PTPLDSTPPG GAPHPLTGQE 

       430        440        450        460        470        480 
EARAVEKDKS KARSEDTGLD SVATRTPMEH VTPKPETHLA SPKPTCMVPP MPHSPVSGDS 

       490        500        510        520        530        540 
VEEEEEEEKK VCLPGFTGLV NLGNTCFMNS VIQSLSNTRE LRDFFHDRSF EAEINYNNPL 

       550        560        570        580        590        600 
GTGGRLAIGF AVLLRALWKG THHAFQPSKL KAIVASKASQ FTGYAQHDAQ EFMAFLLDGL 

       610        620        630        640        650        660 
HEDLNRIQNK PYTETVDSDG RPDEVVAEEA WQRHKMRNDS FIVDLFQGQY KSKLVCPVCA 

       670        680        690        700        710        720 
KVSITFDPFL YLPVPLPQKQ KVLPVFYFAR EPHSKPIKFL VSVSKENSTA SEVLDSLSQS 

       730        740        750        760        770        780 
VHVKPENLRL AEVIKNRFHR VFLPSHSLDT VSPSDTLLCF ELLSSELAKE RVVVLEVQQR 

       790        800        810        820        830        840 
PQVPSVPISK CAACQRKQQS EDEKLKRCTR CYRVGYCNQL CQKTHWPDHK GLCRPENIGY 

       850        860        870        880        890        900 
PFLVSVPASR LTYARLAQLL EGYARYSVSV FQPPFQPGRM ALESQSPGCT TLLSTGSLEA 

       910        920        930        940        950        960 
GDSERDPIQP PELQLVTPMA EGDTGLPRVW AAPDRGPVPS TSGISSEMLA SGPIEVGSLP 

       970        980        990       1000       1010       1020 
AGERVSRPEA AVPGYQHPSE AMNAHTPQFF IYKIDSSNRE QRLEDKGDTP LELGDDCSLA 

      1030       1040       1050       1060       1070       1080 
LVWRNNERLQ EFVLVASKEL ECAEDPGSAG EAARAGHFTL DQCLNLFTRP EVLAPEEAWY 

      1090       1100       1110       1120       1130       1140 
CPQCKQHREA SKQLLLWRLP NVLIVQLKRF SFRSFIWRDK INDLVEFPVR NLDLSKFCIG 

      1150       1160       1170       1180       1190       1200 
QKEEQLPSYD LYAVINHYGG MIGGHYTACA RLPNDRSSQR SDVGWRLFDD STVTTVDESQ 

      1210       1220       1230       1240       1250       1260 
VVTRYAYVLF YRRRNSPVER PPRAGHSEHH PDLGPAAEAA ASQASRIWQE LEAEEEPVPE 

      1270       1280       1290       1300       1310 
GSGPLGPWGP QDWVGPLPRG PTTPDEGCLR YFVLGTVAAL VALVLNVFYP LVSQSRWR 

« Hide

Isoform 2 [UniParc].

Checksum: 3DEF7C14294E7E92
Show »

FASTA66071,090
Isoform 3 [UniParc].

Checksum: 442FF7C6DE59AE94
Show »

FASTA1,281141,413
Isoform 4 [UniParc].

Checksum: CD9BFE22C20EB03E
Show »

FASTA1,268140,022
Isoform 5 [UniParc].

Checksum: 0FCD06C7B0C80C4E
Show »

FASTA1,419156,035
Isoform 6 [UniParc].

Checksum: CC8F00B6C0033058
Show »

FASTA1,384151,925
Isoform 7 [UniParc].

Checksum: 982B811383529FEE
Show »

FASTA1,372150,659

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"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 5 AND 7).
Tissue: Brain.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [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; 2 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 846-1318 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-1318 (ISOFORM 4).
Tissue: Skin and Testis.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"The ER-resident ubiquitin-specific protease 19 participates in the UPR and rescues ERAD substrates."
Hassink G.C., Zhao B., Sompallae R., Altun M., Gastaldello S., Zinin N.V., Masucci M.G., Lindsten K.
EMBO Rep. 10:755-761(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION.
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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].
[9]"The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2."
Mei Y., Hahn A.A., Hu S., Yang X.
J. Biol. Chem. 286:35380-35387(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BIRC2/C-IAP1; BIRC3/C-IAP2 AND XIAP/BIRC4.
[10]"Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes."
Iphofer A., Kummer A., Nimtz M., Ritter A., Arnold T., Frank R., van den Heuvel J., Kessler B.M., Jansch L., Franke R.
ChemBioChem 13:1416-1420(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, LINKAGE SPECIFICITY.
[11]"Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor 1alpha (HIF-1alpha) during hypoxia."
Altun M., Zhao B., Velasco K., Liu H., Hassink G., Paschke J., Pereira T., Lindsten K.
J. Biol. Chem. 287:1962-1969(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HIF1A.
[12]"Solution structure of the CS domain of human USP19."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 273-393.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB020698 mRNA. Translation: BAA74914.1. Different initiation.
AK294756 mRNA. Translation: BAG57894.1.
AK300425 mRNA. Translation: BAG62152.1.
AC135506 Genomic DNA. No translation available.
BC048269 mRNA. Translation: AAH48269.1.
BC065909 mRNA. Translation: AAH65909.1.
BC082241 mRNA. Translation: AAH82241.1.
BC106029 mRNA. Translation: AAI06030.1. Sequence problems.
BC142660 mRNA. Translation: AAI42661.1. Different initiation.
BC146752 mRNA. Translation: AAI46753.1.
CCDSCCDS43090.1. [O94966-1]
CCDS56254.1. [O94966-5]
CCDS56255.1. [O94966-6]
CCDS56256.1. [O94966-7]
RefSeqNP_001186089.1. NM_001199160.1. [O94966-5]
NP_001186090.1. NM_001199161.1. [O94966-6]
NP_001186091.1. NM_001199162.1. [O94966-7]
NP_006668.1. NM_006677.2. [O94966-1]
XP_005264888.1. XM_005264831.1. [O94966-4]
UniGeneHs.255596.
Hs.734003.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WH0NMR-A273-393[»]
ProteinModelPortalO94966.
SMRO94966. Positions 273-402, 494-677, 996-1215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116078. 53 interactions.
IntActO94966. 36 interactions.
MINTMINT-4658026.
STRING9606.ENSP00000381863.

Protein family/group databases

MEROPSC19.024.

PTM databases

PhosphoSiteO94966.

Proteomic databases

MaxQBO94966.
PaxDbO94966.
PRIDEO94966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398888; ENSP00000381863; ENSG00000172046. [O94966-1]
ENST00000417901; ENSP00000395260; ENSG00000172046. [O94966-6]
ENST00000434032; ENSP00000401197; ENSG00000172046. [O94966-5]
ENST00000453664; ENSP00000400090; ENSG00000172046. [O94966-7]
GeneID10869.
KEGGhsa:10869.
UCSCuc003cwb.3. human. [O94966-2]
uc003cwd.2. human. [O94966-1]

Organism-specific databases

CTD10869.
GeneCardsGC03M049120.
HGNCHGNC:12617. USP19.
MIM614471. gene.
neXtProtNX_O94966.
PharmGKBPA37243.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5560.
HOGENOMHOG000074206.
HOVERGENHBG061889.
KOK11847.
OMAPQCKQHR.
PhylomeDBO94966.
TreeFamTF106276.

Gene expression databases

ArrayExpressO94966.
BgeeO94966.
CleanExHS_USP19.
GenevestigatorO94966.

Family and domain databases

Gene3D2.60.40.790. 2 hits.
InterProIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR002893. Znf_MYND.
[Graphical view]
PfamPF04969. CS. 2 hits.
PF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SUPFAMSSF49764. SSF49764. 2 hits.
PROSITEPS51203. CS. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP19. human.
EvolutionaryTraceO94966.
GenomeRNAi10869.
NextBio41271.
PROO94966.
SOURCESearch...

Entry information

Entry nameUBP19_HUMAN
AccessionPrimary (citable) accession number: O94966
Secondary accession number(s): A5PKX8 expand/collapse secondary AC list , A6H8U2, B4DGT3, B4DTZ0, E7EN22, E7ETS0, E9PEG8, Q3KQW4, Q641Q9, Q6NZY8, Q86XV9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: July 10, 2007
Last modified: July 9, 2014
This is version 131 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 3

Human chromosome 3: entries, gene names and cross-references to MIM