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O94966

- UBP19_HUMAN

UniProt

O94966 - UBP19_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 19

Gene
USP19, KIAA0891, ZMYND9
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei506 – 5061Nucleophile By similarity
Active sitei1165 – 11651Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri791 – 83343MYND-typeAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. negative regulation of skeletal muscle tissue development Source: UniProtKB
  3. positive regulation of cell cycle process Source: UniProtKB
  4. protein deubiquitination Source: UniProtKB
  5. regulation of cellular response to hypoxia Source: UniProtKB
  6. regulation of protein stability Source: UniProtKB
  7. response to endoplasmic reticulum stress Source: UniProtKB
  8. skeletal muscle atrophy Source: UniProtKB
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

MEROPSiC19.024.

Names & Taxonomyi

Protein namesi
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 namesi
Name:USP19
Synonyms:KIAA0891, ZMYND9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:12617. USP19.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 12911291Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei1292 – 131221Helical; Reviewed predictionAdd
BLAST
Topological domaini1313 – 13186Lumenal Reviewed prediction

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. endoplasmic reticulum membrane Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37243.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13181318Ubiquitin carboxyl-terminal hydrolase 19PRO_0000080646Add
BLAST

Proteomic databases

MaxQBiO94966.
PaxDbiO94966.
PRIDEiO94966.

PTM databases

PhosphoSiteiO94966.

Expressioni

Gene expression databases

ArrayExpressiO94966.
BgeeiO94966.
CleanExiHS_USP19.
GenevestigatoriO94966.

Interactioni

Subunit structurei

Interacts with RNF123 By similarity. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with HIF1A (via N-terminus).2 Publications

Protein-protein interaction databases

BioGridi116078. 58 interactions.
IntActiO94966. 36 interactions.
MINTiMINT-4658026.
STRINGi9606.ENSP00000381863.

Structurei

Secondary structure

1
1318
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi276 – 2783
Beta strandi279 – 2835
Beta strandi287 – 2926
Turni293 – 2953
Beta strandi296 – 3027
Beta strandi312 – 3154
Beta strandi317 – 3248
Helixi329 – 3346
Beta strandi344 – 3529
Turni356 – 3583
Beta strandi360 – 3634
Beta strandi365 – 37713

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WH0NMR-A273-393[»]
ProteinModelPortaliO94966.
SMRiO94966. Positions 273-402, 494-677, 996-1215.

Miscellaneous databases

EvolutionaryTraceiO94966.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini113 – 20290CS 1Add
BLAST
Domaini282 – 384103CS 2Add
BLAST
Domaini497 – 1214718USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 2 CS domains.
Contains 1 USP domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri791 – 83343MYND-typeAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiCOG5560.
HOGENOMiHOG000074206.
HOVERGENiHBG061889.
KOiK11847.
OMAiPQCKQHR.
PhylomeDBiO94966.
TreeFamiTF106276.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF04969. CS. 2 hits.
PF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 2 hits.
PROSITEiPS51203. 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]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O94966-1) [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

MSGGASATGP RRGPPGLEDT TSKKKQKDRA NQESKDGDPR KETGSRYVAQ     50
AGLEPLASGD PSASASHAAG ITGSRHRTRL FFPSSSGSAS TPQEEQTKEG 100
ACEDPHDLLA TPTPELLLDW RQSAEEVIVK LRVGVGPLQL EDVDAAFTDT 150
DCVVRFAGGQ QWGGVFYAEI KSSCAKVQTR KGSLLHLTLP KKVPMLTWPS 200
LLVEADEQLC IPPLNSQTCL LGSEENLAPL AGEKAVPPGN DPVSPAMVRS 250
RNPGKDDCAK EEMAVAADAA TLVDEPESMV NLAFVKNDSY EKGPDSVVVH 300
VYVKEICRDT SRVLFREQDF TLIFQTRDGN FLRLHPGCGP HTTFRWQVKL 350
RNLIEPEQCT FCFTASRIDI CLRKRQSQRW GGLEAPAARV GGAKVAVPTG 400
PTPLDSTPPG GAPHPLTGQE EARAVEKDKS KARSEDTGLD SVATRTPMEH 450
VTPKPETHLA SPKPTCMVPP MPHSPVSGDS VEEEEEEEKK VCLPGFTGLV 500
NLGNTCFMNS VIQSLSNTRE LRDFFHDRSF EAEINYNNPL GTGGRLAIGF 550
AVLLRALWKG THHAFQPSKL KAIVASKASQ FTGYAQHDAQ EFMAFLLDGL 600
HEDLNRIQNK PYTETVDSDG RPDEVVAEEA WQRHKMRNDS FIVDLFQGQY 650
KSKLVCPVCA KVSITFDPFL YLPVPLPQKQ KVLPVFYFAR EPHSKPIKFL 700
VSVSKENSTA SEVLDSLSQS VHVKPENLRL AEVIKNRFHR VFLPSHSLDT 750
VSPSDTLLCF ELLSSELAKE RVVVLEVQQR PQVPSVPISK CAACQRKQQS 800
EDEKLKRCTR CYRVGYCNQL CQKTHWPDHK GLCRPENIGY PFLVSVPASR 850
LTYARLAQLL EGYARYSVSV FQPPFQPGRM ALESQSPGCT TLLSTGSLEA 900
GDSERDPIQP PELQLVTPMA EGDTGLPRVW AAPDRGPVPS TSGISSEMLA 950
SGPIEVGSLP AGERVSRPEA AVPGYQHPSE AMNAHTPQFF IYKIDSSNRE 1000
QRLEDKGDTP LELGDDCSLA LVWRNNERLQ EFVLVASKEL ECAEDPGSAG 1050
EAARAGHFTL DQCLNLFTRP EVLAPEEAWY CPQCKQHREA SKQLLLWRLP 1100
NVLIVQLKRF SFRSFIWRDK INDLVEFPVR NLDLSKFCIG QKEEQLPSYD 1150
LYAVINHYGG MIGGHYTACA RLPNDRSSQR SDVGWRLFDD STVTTVDESQ 1200
VVTRYAYVLF YRRRNSPVER PPRAGHSEHH PDLGPAAEAA ASQASRIWQE 1250
LEAEEEPVPE GSGPLGPWGP QDWVGPLPRG PTTPDEGCLR YFVLGTVAAL 1300
VALVLNVFYP LVSQSRWR 1318
Length:1,318
Mass (Da):145,651
Last modified:July 10, 2007 - v2
Checksum:iEA9F318D03304AA1
GO
Isoform 2 (identifier: O94966-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:660
Mass (Da):71,090
Checksum:i3DEF7C14294E7E92
GO
Isoform 3 (identifier: O94966-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,281
Mass (Da):141,413
Checksum:i442FF7C6DE59AE94
GO
Isoform 4 (identifier: O94966-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,268
Mass (Da):140,022
Checksum:iCD9BFE22C20EB03E
GO
Isoform 5 (identifier: O94966-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     202-202: L → LKKPLGTQEL...PPFVADPATQ

Note: No experimental confirmation available.

Show »
Length:1,419
Mass (Da):156,035
Checksum:i0FCD06C7B0C80C4E
GO
Isoform 6 (identifier: O94966-6) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,384
Mass (Da):151,925
Checksum:iCC8F00B6C0033058
GO
Isoform 7 (identifier: O94966-7) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,372
Mass (Da):150,659
Checksum:i982B811383529FEE
GO

Sequence cautioni

The sequence AAI06030.1 differs from that shown. Reason: Frameshift at position 572.
The sequence AAI06030.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361D → H.
Corresponds to variant rs11552724 [ dbSNP | Ensembl ].
VAR_051528

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei100 – 11415Missing in isoform 2 and isoform 4. VSP_026708Add
BLAST
Alternative sequencei193 – 20210VPMLTWPSLL → KKPLGTQELVPGLRCQENGQ ELSPIALEPGPEPHRAKQEA RNQKRAQGRGEVGAGAGPGA QAGPSAKRAVHLCRGPEGDG SRDDPGPRGDAPPFVADPAT Q in isoform 7. VSP_047057
Alternative sequencei202 – 2021L → LKKPLGTQELVPGLRCQENG QELSPIALEPGPEPHRAKQE ARNQKRAQGRGEVGAGAGPG AQAGPSAKRAVHLCRGPEGD GSRDDPGPRGDAPPFVADPA TQ in isoform 2, isoform 5 and isoform 6. VSP_026709
Alternative sequencei389 – 3891R → RGA in isoform 4 and isoform 6. VSP_045891
Alternative sequencei573 – 5742IV → RL in isoform 2. VSP_026710
Alternative sequencei575 – 1318744Missing in isoform 2. VSP_026711Add
BLAST
Alternative sequencei1244 – 129855ASRIW…LGTVA → GLGPGQAPEVAPTRTAPERF APPVDRPAPTYSNMEEVD in isoform 3, isoform 4, isoform 6 and isoform 7. VSP_026712Add
BLAST
Alternative sequencei1299 – 131820Missing in isoform 3, isoform 4, isoform 6 and isoform 7. VSP_026713Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti942 – 9421S → C in BAG57894. 1 Publication
Sequence conflicti1041 – 10411E → G in BAG62152. 1 Publication
Isoform 4 (identifier: O94966-4)
Sequence conflicti1251 – 12511A → T in AAH82241. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43090.1. [O94966-1]
CCDS56254.1. [O94966-5]
CCDS56255.1. [O94966-6]
CCDS56256.1. [O94966-7]
RefSeqiNP_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]
UniGeneiHs.255596.
Hs.734003.

Genome annotation databases

EnsembliENST00000398888; ENSP00000381863; ENSG00000172046. [O94966-1]
ENST00000417901; ENSP00000395260; ENSG00000172046. [O94966-6]
ENST00000434032; ENSP00000401197; ENSG00000172046. [O94966-5]
ENST00000453664; ENSP00000400090; ENSG00000172046. [O94966-7]
GeneIDi10869.
KEGGihsa:10869.
UCSCiuc003cwb.3. human. [O94966-2]
uc003cwd.2. human. [O94966-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS43090.1. [O94966-1 ]
CCDS56254.1. [O94966-5 ]
CCDS56255.1. [O94966-6 ]
CCDS56256.1. [O94966-7 ]
RefSeqi NP_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 ]
UniGenei Hs.255596.
Hs.734003.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WH0 NMR - A 273-393 [» ]
ProteinModelPortali O94966.
SMRi O94966. Positions 273-402, 494-677, 996-1215.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116078. 58 interactions.
IntActi O94966. 36 interactions.
MINTi MINT-4658026.
STRINGi 9606.ENSP00000381863.

Protein family/group databases

MEROPSi C19.024.

PTM databases

PhosphoSitei O94966.

Proteomic databases

MaxQBi O94966.
PaxDbi O94966.
PRIDEi O94966.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398888 ; ENSP00000381863 ; ENSG00000172046 . [O94966-1 ]
ENST00000417901 ; ENSP00000395260 ; ENSG00000172046 . [O94966-6 ]
ENST00000434032 ; ENSP00000401197 ; ENSG00000172046 . [O94966-5 ]
ENST00000453664 ; ENSP00000400090 ; ENSG00000172046 . [O94966-7 ]
GeneIDi 10869.
KEGGi hsa:10869.
UCSCi uc003cwb.3. human. [O94966-2 ]
uc003cwd.2. human. [O94966-1 ]

Organism-specific databases

CTDi 10869.
GeneCardsi GC03M049120.
HGNCi HGNC:12617. USP19.
MIMi 614471. gene.
neXtProti NX_O94966.
PharmGKBi PA37243.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5560.
HOGENOMi HOG000074206.
HOVERGENi HBG061889.
KOi K11847.
OMAi PQCKQHR.
PhylomeDBi O94966.
TreeFami TF106276.

Miscellaneous databases

ChiTaRSi USP19. human.
EvolutionaryTracei O94966.
GenomeRNAii 10869.
NextBioi 41271.
PROi O94966.
SOURCEi Search...

Gene expression databases

ArrayExpressi O94966.
Bgeei O94966.
CleanExi HS_USP19.
Genevestigatori O94966.

Family and domain databases

Gene3Di 2.60.40.790. 2 hits.
InterProi IPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR002893. Znf_MYND.
[Graphical view ]
Pfami PF04969. CS. 2 hits.
PF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view ]
SUPFAMi SSF49764. SSF49764. 2 hits.
PROSITEi PS51203. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiUBP19_HUMAN
AccessioniPrimary (citable) accession number: O94966
Secondary accession number(s): A5PKX8
, A6H8U2, B4DGT3, B4DTZ0, E7EN22, E7ETS0, E9PEG8, Q3KQW4, Q641Q9, Q6NZY8, Q86XV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: July 10, 2007
Last modified: September 3, 2014
This is version 132 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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