O94966 (UBP19_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 118.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1318 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. |
| 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. |
Ontologies
Alternative products
| This entry describes 6 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 | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1318 | 1318 | Ubiquitin carboxyl-terminal hydrolase 19 | PRO_0000080646 | ||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||
| Topological domain | 1 – 1291 | 1291 | Cytoplasmic Potential | |||||||||||||||||||||||||||
| Transmembrane | 1292 – 1312 | 21 | Helical; Potential | |||||||||||||||||||||||||||
| Topological domain | 1313 – 1318 | 6 | Lumenal Potential | |||||||||||||||||||||||||||
| Domain | 113 – 202 | 90 | CS 1 | |||||||||||||||||||||||||||
| Domain | 282 – 384 | 103 | CS 2 | |||||||||||||||||||||||||||
| Zinc finger | 791 – 833 | 43 | MYND-type | |||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||
| Active site | 506 | 1 | Nucleophile By similarity | |||||||||||||||||||||||||||
| Active site | 1165 | 1 | Proton acceptor By similarity | |||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||
| Alternative sequence | 100 – 114 | 15 | Missing in isoform 2 and isoform 4. | VSP_026708 | ||||||||||||||||||||||||||
| Alternative sequence | 202 | 1 | L → LKKPLGTQELVPGLRCQENG QELSPIALEPGPEPHRAKQE ARNQKRAQGRGEVGAGAGPG AQAGPSAKRAVHLCRGPEGD GSRDDPGPRGDAPPFVADPA TQ in isoform 2, isoform 5 and isoform 6. | VSP_026709 | ||||||||||||||||||||||||||
| Alternative sequence | 389 | 1 | R → RGA in isoform 4 and isoform 6. | VSP_045891 | ||||||||||||||||||||||||||
| Alternative sequence | 573 – 574 | 2 | IV → RL in isoform 2. | VSP_026710 | ||||||||||||||||||||||||||
| Alternative sequence | 575 – 1318 | 744 | Missing in isoform 2. | VSP_026711 | ||||||||||||||||||||||||||
| Alternative sequence | 1244 – 1298 | 55 | ASRIW…LGTVA → GLGPGQAPEVAPTRTAPERF APPVDRPAPTYSNMEEVD in isoform 3, isoform 4 and isoform 6. | VSP_026712 | ||||||||||||||||||||||||||
| Alternative sequence | 1299 – 1318 | 20 | Missing in isoform 3 and isoform 4. | VSP_026713 | ||||||||||||||||||||||||||
| Natural variant | 36 | 1 | D → H. Corresponds to variant rs11552724 [ dbSNP | Ensembl ]. | VAR_051528 | ||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Sequence conflict | 942 | 1 | S → C in BAG57894. Ref.2 | |||||||||||||||||||||||||||
| Isoform 4: | ||||||||||||||||||||||||||||||
| Sequence conflict | 1251 | 1 | A → T in AAH82241. Ref.4 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Helix | 276 – 278 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 279 – 283 | 5 | ||||||||||||||||||||||||||||
| Beta strand | 287 – 292 | 6 | ||||||||||||||||||||||||||||
| Turn | 293 – 295 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 296 – 302 | 7 | ||||||||||||||||||||||||||||
| Beta strand | 312 – 315 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 317 – 324 | 8 | ||||||||||||||||||||||||||||
| Helix | 329 – 334 | 6 | ||||||||||||||||||||||||||||
| Beta strand | 344 – 352 | 9 | ||||||||||||||||||||||||||||
| Turn | 356 – 358 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 360 – 363 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 365 – 377 | 13 | ||||||||||||||||||||||||||||
Sequences
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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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). 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. 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. 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. | ||||||||||||
| IPI | IPI00016589. IPI00654743. IPI00797161. IPI00853489. IPI00927646. | ||||||||||||
| RefSeq | NP_001186089.1. NM_001199160.1. NP_001186090.1. NM_001199161.1. NP_001186091.1. NM_001199162.1. NP_006668.1. NM_006677.2. | ||||||||||||
| UniGene | Hs.255596. Hs.734003. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | O94966. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | O94966. 32 interactions. | ||||||||||||
| MINT | MINT-4658026. | ||||||||||||
| STRING | 9606.ENSP00000381863. | ||||||||||||
Protein family/group databases | |||||||||||||
| MEROPS | C19.024. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | O94966. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | O94966. | ||||||||||||
| PRIDE | O94966. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000398888; ENSP00000381863; ENSG00000172046. ENST00000434032; ENSP00000401197; ENSG00000172046. | ||||||||||||
| GeneID | 10869. | ||||||||||||
| KEGG | hsa:10869. | ||||||||||||
| UCSC | uc003cwb.3. human. uc003cwd.2. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 10869. | ||||||||||||
| GeneCards | GC03M049120. | ||||||||||||
| HGNC | HGNC:12617. USP19. | ||||||||||||
| MIM | 614471. gene. | ||||||||||||
| neXtProt | NX_O94966. | ||||||||||||
| PharmGKB | PA37243. | ||||||||||||
| HUGE | Search... | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG5560. | ||||||||||||
| HOGENOM | HOG000074206. | ||||||||||||
| HOVERGEN | HBG061889. | ||||||||||||
| KO | K11847. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | O94966. | ||||||||||||
| Bgee | O94966. | ||||||||||||
| CleanEx | HS_USP19. | ||||||||||||
| Genevestigator | O94966. | ||||||||||||
| GermOnline | ENSG00000172046. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR007052. CS-like_domain. IPR017447. CS_domain. IPR015054. DUF1872. IPR008978. HSP20-like_chaperone. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR002893. Znf_MYND. [Graphical view] | ||||||||||||
| Pfam | PF04969. CS. 1 hit. PF08959. DUF1872. 1 hit. PF00443. UCH. 1 hit. PF01753. zf-MYND. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF49764. HSP20_chap. 2 hits. | ||||||||||||
| PROSITE | PS51203. CS. 2 hits. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. PS01360. ZF_MYND_1. 1 hit. PS50865. ZF_MYND_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| ChiTaRS | USP19. human. | ||||||||||||
| EvolutionaryTrace | O94966. | ||||||||||||
| GenomeRNAi | 10869. | ||||||||||||
| NextBio | 41271. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | UBP19_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O94966 Secondary accession number(s): A5PKX8 Q86XV9 | ||||||||
| Entry history |
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| 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. | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| Human chromosome 3 Human chromosome 3: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
