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Q92995

- UBP13_HUMAN

UniProt

Q92995 - UBP13_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 13

Gene

USP13

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

Functioni

Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data.6 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).

Enzyme regulationi

Specifically inhibited by spautin-1 (specific and potent autophagy inhibitor-1), a derivative of MBCQ that binds to USP13 and inhibits deubiquitinase activity. Regulated by PIK3C3/VPS34-containing complexes. The weak deubiquitinase activity in vitro suggests the existence of some mechanism that activates the enzyme.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei345 – 3451NucleophileCurated
Active sitei823 – 8231Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri209 – 28173UBP-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. omega peptidase activity Source: InterPro
  3. ubiquitin binding Source: UniProtKB
  4. ubiquitin protein ligase binding Source: UniProtKB
  5. ubiquitin-specific protease activity Source: UniProtKB
  6. ubiquitin thiolesterase activity Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. cell proliferation Source: UniProtKB
  3. melanocyte differentiation Source: UniProtKB
  4. protein K63-linked deubiquitination Source: UniProtKB
  5. protein stabilization Source: UniProtKB
  6. regulation of autophagy Source: UniProtKB
  7. regulation of transcription, DNA-templated Source: UniProtKB
  8. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Autophagy, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC19.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 13 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 13
Isopeptidase T-3
Short name:
ISOT-3
Ubiquitin thioesterase 13
Ubiquitin-specific-processing protease 13
Gene namesi
Name:USP13
Synonyms:ISOT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:12611. USP13.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi221 – 2211W → A: Does not abolish ability to stabilize SIAH2. 1 Publication
Mutagenesisi233 – 2331K → A: Does not abolish ability to stabilize SIAH2. 1 Publication
Mutagenesisi273 – 2731F → A: Impairs ability to stabilize SIAH2. 1 Publication
Mutagenesisi345 – 3451C → A: Abolishes deubiquitinating activity. Does not abolish ability to stabilize SIAH2. Does not abolish ability to stabilize SIAH2; when associated with A-814 and A-823. 2 Publications
Mutagenesisi664 – 6641M → E: Impairs ability to stabilize SIAH2. Abolishes ability to stabilize SIAH2; when associated with E-739. 1 Publication
Mutagenesisi739 – 7391M → E: Impairs ability to stabilize SIAH2. Abolishes ability to stabilize SIAH2; when associated with E-664. 1 Publication
Mutagenesisi814 – 8141H → A: Does not abolish ability to stabilize SIAH2; when associated with A-345 and A-823. 1 Publication
Mutagenesisi823 – 8231H → A: Does not abolish ability to stabilize SIAH2; when associated with A-345 and A-814. 1 Publication

Organism-specific databases

PharmGKBiPA37237.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 863863Ubiquitin carboxyl-terminal hydrolase 13PRO_0000080635Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141Phosphoserine1 Publication
Modified residuei122 – 1221Phosphothreonine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92995.
PaxDbiQ92995.
PRIDEiQ92995.

PTM databases

PhosphoSiteiQ92995.

Expressioni

Tissue specificityi

Highly expressed in ovary and testes.

Gene expression databases

BgeeiQ92995.
CleanExiHS_USP13.
ExpressionAtlasiQ92995. baseline and differential.
GenevestigatoriQ92995.

Organism-specific databases

HPAiHPA004827.

Interactioni

Subunit structurei

Interacts with UFD1. Interacts (via UBA domains) with SIAH2 (when ubiquitinated).2 Publications

Protein-protein interaction databases

BioGridi114465. 39 interactions.
IntActiQ92995. 27 interactions.
MINTiMINT-1195142.
STRINGi9606.ENSP00000263966.

Structurei

Secondary structure

1
863
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni191 – 1944Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi217 – 2237Combined sources
Turni224 – 2263Combined sources
Beta strandi229 – 2313Combined sources
Helixi244 – 2518Combined sources
Beta strandi256 – 2605Combined sources
Beta strandi269 – 2724Combined sources
Turni273 – 2753Combined sources
Beta strandi277 – 2793Combined sources
Helixi284 – 2907Combined sources
Helixi296 – 2994Combined sources
Helixi656 – 6627Combined sources
Helixi669 – 67810Combined sources
Helixi683 – 69210Combined sources
Helixi693 – 6953Combined sources
Beta strandi697 – 7004Combined sources
Beta strandi710 – 7145Combined sources
Helixi730 – 73910Combined sources
Helixi743 – 75311Combined sources
Helixi757 – 7659Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L80NMR-A188-301[»]
2LBCNMR-A652-777[»]
ProteinModelPortaliQ92995.
SMRiQ92995. Positions 26-863.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini336 – 861526USPAdd
BLAST
Domaini652 – 69342UBA 1PROSITE-ProRule annotationAdd
BLAST
Domaini727 – 76741UBA 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The UBP-type zinc finger has lost its ability to bind ubiquitin and USP13 is not activated by unanchored ubiquitin. Swapping with the UBP-type zinc finger from USP5 restores ability to bind unanchored ubiquitin and subsequent activation of the protein (PubMed:22216260).1 Publication
The UBA domains mediate binding to ubiquitin.1 Publication

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 2 UBA domains.PROSITE-ProRule annotation
Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri209 – 28173UBP-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5207.
GeneTreeiENSGT00390000000874.
HOGENOMiHOG000162311.
HOVERGENiHBG002833.
InParanoidiQ92995.
KOiK11836.
OMAiPRMFKAF.
OrthoDBiEOG7CNZF3.
PhylomeDBiQ92995.
TreeFamiTF300576.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR016652. Ubiquitinyl_hydrolase.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PIRSFiPIRSF016308. UBP. 1 hit.
SMARTiSM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS50030. UBA. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92995-1) [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
MQRRGALFGM PGGSGGRKMA AGDIGELLVP HMPTIRVPRS GDRVYKNECA
60 70 80 90 100
FSYDSPNSEG GLYVCMNTFL AFGREHVERH FRKTGQSVYM HLKRHVREKV
110 120 130 140 150
RGASGGALPK RRNSKIFLDL DTDDDLNSDD YEYEDEAKLV IFPDHYEIAL
160 170 180 190 200
PNIEELPALV TIACDAVLSS KSPYRKQDPD TWENELPVSK YANNLTQLDN
210 220 230 240 250
GVRIPPSGWK CARCDLRENL WLNLTDGSVL CGKWFFDSSG GNGHALEHYR
260 270 280 290 300
DMGYPLAVKL GTITPDGADV YSFQEEEPVL DPHLAKHLAH FGIDMLHMHG
310 320 330 340 350
TENGLQDNDI KLRVSEWEVI QESGTKLKPM YGPGYTGLKN LGNSCYLSSV
360 370 380 390 400
MQAIFSIPEF QRAYVGNLPR IFDYSPLDPT QDFNTQMTKL GHGLLSGQYS
410 420 430 440 450
KPPVKSELIE QVMKEEHKPQ QNGISPRMFK AFVSKSHPEF SSNRQQDAQE
460 470 480 490 500
FFLHLVNLVE RNRIGSENPS DVFRFLVEER IQCCQTRKVR YTERVDYLMQ
510 520 530 540 550
LPVAMEAATN KDELIAYELT RREAEANRRP LPELVRAKIP FSACLQAFSE
560 570 580 590 600
PENVDDFWSS ALQAKSAGVK TSRFASFPEY LVVQIKKFTF GLDWVPKKFD
610 620 630 640 650
VSIDMPDLLD INHLRARGLQ PGEEELPDIS PPIVIPDDSK DRLMNQLIDP
660 670 680 690 700
SDIDESSVMQ LAEMGFPLEA CRKAVYFTGN MGAEVAFNWI IVHMEEPDFA
710 720 730 740 750
EPLTMPGYGG AASAGASVFG ASGLDNQPPE EIVAIITSMG FQRNQAIQAL
760 770 780 790 800
RATNNNLERA LDWIFSHPEF EEDSDFVIEM ENNANANIIS EAKPEGPRVK
810 820 830 840 850
DGSGTYELFA FISHMGTSTM SGHYICHIKK EGRWVIYNDH KVCASERPPK
860
DLGYMYFYRR IPS
Length:863
Mass (Da):97,327
Last modified:October 14, 2008 - v2
Checksum:i988713ADF8C0B938
GO
Isoform 2 (identifier: Q92995-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.

Note: No experimental confirmation available.

Show »
Length:798
Mass (Da):90,383
Checksum:i5F9943C19D16FE4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961V → A in AAC63405. (PubMed:9841226)Curated
Sequence conflicti293 – 2931I → V in BAF83027. (PubMed:14702039)Curated
Sequence conflicti305 – 3051L → F in BAF83027. (PubMed:14702039)Curated
Sequence conflicti325 – 3251T → A in BAF83027. (PubMed:14702039)Curated
Sequence conflicti338 – 3381L → P in BAF83027. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6565Missing in isoform 2. 1 PublicationVSP_043954Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75362 mRNA. Translation: AAC63405.1.
AK290338 mRNA. Translation: BAF83027.1.
AK302404 mRNA. Translation: BAG63715.1.
AC007687 Genomic DNA. No translation available.
AC125604 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78383.1.
CH471052 Genomic DNA. Translation: EAW78384.1.
BC016146 mRNA. Translation: AAH16146.1.
CCDSiCCDS3235.1. [Q92995-1]
RefSeqiNP_003931.2. NM_003940.2. [Q92995-1]
UniGeneiHs.175322.

Genome annotation databases

EnsembliENST00000263966; ENSP00000263966; ENSG00000058056. [Q92995-1]
ENST00000496897; ENSP00000417146; ENSG00000058056. [Q92995-2]
GeneIDi8975.
KEGGihsa:8975.
UCSCiuc003fkh.3. human. [Q92995-1]

Polymorphism databases

DMDMi209572692.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75362 mRNA. Translation: AAC63405.1 .
AK290338 mRNA. Translation: BAF83027.1 .
AK302404 mRNA. Translation: BAG63715.1 .
AC007687 Genomic DNA. No translation available.
AC125604 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78383.1 .
CH471052 Genomic DNA. Translation: EAW78384.1 .
BC016146 mRNA. Translation: AAH16146.1 .
CCDSi CCDS3235.1. [Q92995-1 ]
RefSeqi NP_003931.2. NM_003940.2. [Q92995-1 ]
UniGenei Hs.175322.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2L80 NMR - A 188-301 [» ]
2LBC NMR - A 652-777 [» ]
ProteinModelPortali Q92995.
SMRi Q92995. Positions 26-863.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114465. 39 interactions.
IntActi Q92995. 27 interactions.
MINTi MINT-1195142.
STRINGi 9606.ENSP00000263966.

Protein family/group databases

MEROPSi C19.012.

PTM databases

PhosphoSitei Q92995.

Polymorphism databases

DMDMi 209572692.

Proteomic databases

MaxQBi Q92995.
PaxDbi Q92995.
PRIDEi Q92995.

Protocols and materials databases

DNASUi 8975.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263966 ; ENSP00000263966 ; ENSG00000058056 . [Q92995-1 ]
ENST00000496897 ; ENSP00000417146 ; ENSG00000058056 . [Q92995-2 ]
GeneIDi 8975.
KEGGi hsa:8975.
UCSCi uc003fkh.3. human. [Q92995-1 ]

Organism-specific databases

CTDi 8975.
GeneCardsi GC03P179370.
H-InvDB HIX0003883.
HGNCi HGNC:12611. USP13.
HPAi HPA004827.
MIMi 603591. gene.
neXtProti NX_Q92995.
PharmGKBi PA37237.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5207.
GeneTreei ENSGT00390000000874.
HOGENOMi HOG000162311.
HOVERGENi HBG002833.
InParanoidi Q92995.
KOi K11836.
OMAi PRMFKAF.
OrthoDBi EOG7CNZF3.
PhylomeDBi Q92995.
TreeFami TF300576.

Miscellaneous databases

ChiTaRSi USP13. human.
GeneWikii USP13.
GenomeRNAii 8975.
NextBioi 33685.
PROi Q92995.
SOURCEi Search...

Gene expression databases

Bgeei Q92995.
CleanExi HS_USP13.
ExpressionAtlasi Q92995. baseline and differential.
Genevestigatori Q92995.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR016652. Ubiquitinyl_hydrolase.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view ]
Pfami PF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view ]
PIRSFi PIRSF016308. UBP. 1 hit.
SMARTi SM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
PROSITEi PS50030. UBA. 2 hits.
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. "The genomic organization of Isopeptidase T-3 (ISOT-3), a new member of the ubiquitin specific protease family (UBP)."
    Timms K.M., Ansari-Lari M.A., Morris W., Brown S.N., Gibbs R.A.
    Gene 217:101-106(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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 1 AND 2).
    Tissue: Testis and Tongue.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Uterus.
  6. Cited for: FUNCTION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13."
    Liu J., Xia H., Kim M., Xu L., Li Y., Zhang L., Cai Y., Norberg H.V., Zhang T., Furuya T., Jin M., Zhu Z., Wang H., Yu J., Li Y., Hao Y., Choi A., Ke H., Ma D., Yuan J.
    Cell 147:223-234(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  11. "USP13 enzyme regulates Siah2 ligase stability and activity via noncatalytic ubiquitin-binding domains."
    Scortegagna M., Subtil T., Qi J., Kim H., Zhao W., Gu W., Kluger H., Ronai Z.A.
    J. Biol. Chem. 286:27333-27341(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SIAH2, MUTAGENESIS OF TRP-221; LYS-233; PHE-273; CYS-345; MET-664; MET-739; HIS-814 AND HIS-823.
  12. "Regulation of MITF stability by the USP13 deubiquitinase."
    Zhao X., Fiske B., Kawakami A., Li J., Fisher D.E.
    Nat. Commun. 2:414-414(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-345.
  13. "Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control."
    Chen M., Gutierrez G.J., Ronai Z.A.
    Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UFD1.
  14. "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 THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin."
    Zhang Y.H., Zhou C.J., Zhou Z.R., Song A.X., Hu H.Y.
    PLoS ONE 6:E29362-E29362(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 188-301 AND 652-777, FUNCTION, DOMAIN, UBIQUITIN-BINDING.

Entry informationi

Entry nameiUBP13_HUMAN
AccessioniPrimary (citable) accession number: Q92995
Secondary accession number(s): A8K2S3
, B4DYF3, D3DNS2, Q96B25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2008
Last modified: November 26, 2014
This is version 126 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3