Q92995 (UBP13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	USP13
Synonyms:	ISOT3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	863 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15
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).
Enzyme regulation	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. Ref.10
Subunit structure	Interacts with UFD1. Interacts (via UBA domains) with SIAH2 (when ubiquitinated). Ref.11 Ref.13
Tissue specificity	Highly expressed in ovary and testes.
Domain	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 (Ref.15). Ref.15 The UBA domains mediate binding to ubiquitin (Ref.15). Ref.15
Sequence similarities	Belongs to the peptidase C19 family. Contains 2 UBA domains. Contains 1 UBP-type zinc finger.

Ontologies

Keywords
Biological process	Autophagy Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	autophagy Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Inferred from mutant phenotype Ref.12. Source: UniProtKB melanocyte differentiation Traceable author statement Ref.12. Source: UniProtKB protein K63-linked deubiquitination Inferred from direct assay Ref.15. Source: UniProtKB protein stabilization Inferred from direct assay Ref.11. Source: UniProtKB regulation of autophagy Inferred from direct assay Ref.10. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.12. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	cysteine-type endopeptidase activity Inferred from mutant phenotype Ref.12. Source: UniProtKB omega peptidase activity Inferred from electronic annotation. Source: InterPro ubiquitin binding Inferred from direct assay Ref.11Ref.12Ref.15. Source: UniProtKB ubiquitin thiolesterase activity Inferred from direct assay Ref.12Ref.10Ref.15. Source: UniProtKB ubiquitin-specific protease activity Inferred from direct assay Ref.12Ref.10Ref.15. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92995-1)

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: Q92995-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 863

863

Ubiquitin carboxyl-terminal hydrolase 13

PRO_0000080635

Regions

Domain

652 – 693

42

UBA 1

Domain

727 – 767

41

UBA 2

Zinc finger

209 – 281

73

UBP-type

Sites

Active site

345

1

Nucleophile Probable

Active site

823

1

Proton acceptor By similarity

Amino acid modifications

Modified residue

114

1

Phosphoserine Ref.8

Modified residue

122

1

Phosphothreonine Ref.7 Ref.8 Ref.14

Natural variations

Alternative sequence

1 – 65

65

Missing in isoform 2.

VSP_043954

Experimental info

Mutagenesis

221

1

W → A: Does not abolish ability to stabilize SIAH2. Ref.11

Mutagenesis

233

1

K → A: Does not abolish ability to stabilize SIAH2. Ref.11

Mutagenesis

273

1

F → A: Impairs ability to stabilize SIAH2. Ref.11

Mutagenesis

345

1

C → 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. Ref.11 Ref.12

Mutagenesis

664

1

M → E: Impairs ability to stabilize SIAH2. Abolishes ability to stabilize SIAH2; when associated with E-739. Ref.11

Mutagenesis

739

1

M → E: Impairs ability to stabilize SIAH2. Abolishes ability to stabilize SIAH2; when associated with E-664. Ref.11

Mutagenesis

814

1

H → A: Does not abolish ability to stabilize SIAH2; when associated with A-345 and A-823. Ref.11 Ref.12

Mutagenesis

823

1

H → A: Does not abolish ability to stabilize SIAH2; when associated with A-345 and A-814. Ref.11 Ref.12

Sequence conflict

96

1

V → A in AAC63405. Ref.1

Sequence conflict

293

1

I → V in BAF83027. Ref.2

Sequence conflict

305

1

L → F in BAF83027. Ref.2

Sequence conflict

325

1

T → A in BAF83027. Ref.2

Sequence conflict

338

1

L → P in BAF83027. Ref.2

Secondary structure

1

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863

Helix Strand Turn

Details...

Turn

191 – 194

4

Beta strand

212 – 214

3

Beta strand

217 – 223

7

Turn

224 – 226

3

Beta strand

229 – 231

3

Helix

244 – 251

8

Beta strand

256 – 260

5

Beta strand

269 – 272

4

Turn

273 – 275

3

Beta strand

277 – 279

3

Helix

284 – 290

7

Helix

296 – 299

4

Helix

656 – 662

7

Helix

669 – 678

10

Helix

683 – 692

10

Helix

693 – 695

3

Beta strand

697 – 700

4

Beta strand

710 – 714

5

Helix

730 – 739

10

Helix

743 – 753

11

Helix

757 – 765

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 14, 2008. Version 2. Checksum: 988713ADF8C0B938	FASTA	863	97,327
	10 20 30 40 50 60 MQRRGALFGM PGGSGGRKMA AGDIGELLVP HMPTIRVPRS GDRVYKNECA FSYDSPNSEG 70 80 90 100 110 120 GLYVCMNTFL AFGREHVERH FRKTGQSVYM HLKRHVREKV RGASGGALPK RRNSKIFLDL 130 140 150 160 170 180 DTDDDLNSDD YEYEDEAKLV IFPDHYEIAL PNIEELPALV TIACDAVLSS KSPYRKQDPD 190 200 210 220 230 240 TWENELPVSK YANNLTQLDN GVRIPPSGWK CARCDLRENL WLNLTDGSVL CGKWFFDSSG 250 260 270 280 290 300 GNGHALEHYR DMGYPLAVKL GTITPDGADV YSFQEEEPVL DPHLAKHLAH FGIDMLHMHG 310 320 330 340 350 360 TENGLQDNDI KLRVSEWEVI QESGTKLKPM YGPGYTGLKN LGNSCYLSSV MQAIFSIPEF 370 380 390 400 410 420 QRAYVGNLPR IFDYSPLDPT QDFNTQMTKL GHGLLSGQYS KPPVKSELIE QVMKEEHKPQ 430 440 450 460 470 480 QNGISPRMFK AFVSKSHPEF SSNRQQDAQE FFLHLVNLVE RNRIGSENPS DVFRFLVEER 490 500 510 520 530 540 IQCCQTRKVR YTERVDYLMQ LPVAMEAATN KDELIAYELT RREAEANRRP LPELVRAKIP 550 560 570 580 590 600 FSACLQAFSE PENVDDFWSS ALQAKSAGVK TSRFASFPEY LVVQIKKFTF GLDWVPKKFD 610 620 630 640 650 660 VSIDMPDLLD INHLRARGLQ PGEEELPDIS PPIVIPDDSK DRLMNQLIDP SDIDESSVMQ 670 680 690 700 710 720 LAEMGFPLEA CRKAVYFTGN MGAEVAFNWI IVHMEEPDFA EPLTMPGYGG AASAGASVFG 730 740 750 760 770 780 ASGLDNQPPE EIVAIITSMG FQRNQAIQAL RATNNNLERA LDWIFSHPEF EEDSDFVIEM 790 800 810 820 830 840 ENNANANIIS EAKPEGPRVK DGSGTYELFA FISHMGTSTM SGHYICHIKK EGRWVIYNDH 850 860 KVCASERPPK DLGYMYFYRR IPS
	Isoform 2 [UniParc]. Checksum: 5F9943C19D16FE4F	FASTA	798	90,383
	10 20 30 40 50 60 MNTFLAFGRE HVERHFRKTG QSVYMHLKRH VREKVRGASG GALPKRRNSK IFLDLDTDDD 70 80 90 100 110 120 LNSDDYEYED EAKLVIFPDH YEIALPNIEE LPALVTIACD AVLSSKSPYR KQDPDTWENE 130 140 150 160 170 180 LPVSKYANNL TQLDNGVRIP PSGWKCARCD LRENLWLNLT DGSVLCGKWF FDSSGGNGHA 190 200 210 220 230 240 LEHYRDMGYP LAVKLGTITP DGADVYSFQE EEPVLDPHLA KHLAHFGIDM LHMHGTENGL 250 260 270 280 290 300 QDNDIKLRVS EWEVIQESGT KLKPMYGPGY TGLKNLGNSC YLSSVMQAIF SIPEFQRAYV 310 320 330 340 350 360 GNLPRIFDYS PLDPTQDFNT QMTKLGHGLL SGQYSKPPVK SELIEQVMKE EHKPQQNGIS 370 380 390 400 410 420 PRMFKAFVSK SHPEFSSNRQ QDAQEFFLHL VNLVERNRIG SENPSDVFRF LVEERIQCCQ 430 440 450 460 470 480 TRKVRYTERV DYLMQLPVAM EAATNKDELI AYELTRREAE ANRRPLPELV RAKIPFSACL 490 500 510 520 530 540 QAFSEPENVD DFWSSALQAK SAGVKTSRFA SFPEYLVVQI KKFTFGLDWV PKKFDVSIDM 550 560 570 580 590 600 PDLLDINHLR ARGLQPGEEE LPDISPPIVI PDDSKDRLMN QLIDPSDIDE SSVMQLAEMG 610 620 630 640 650 660 FPLEACRKAV YFTGNMGAEV AFNWIIVHME EPDFAEPLTM PGYGGAASAG ASVFGASGLD 670 680 690 700 710 720 NQPPEEIVAI ITSMGFQRNQ AIQALRATNN NLERALDWIF SHPEFEEDSD FVIEMENNAN 730 740 750 760 770 780 ANIISEAKPE GPRVKDGSGT YELFAFISHM GTSTMSGHYI CHIKKEGRWV IYNDHKVCAS 790 ERPPKDLGYM YFYRRIPS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"Screen for ISG15-crossreactive deubiquitinases." Catic A., Fiebiger E., Korbel G.A., Blom D., Galardy P.J., Ploegh H.L. PLoS ONE 2:E679-E679(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"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].
[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, MASS SPECTROMETRY.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00024401.
IPI00947195.

RefSeq

NP_003931.2. NM_003940.2.

UniGene

Hs.175322.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L80	NMR	-	A	188-301	[»]
2LBC	NMR	-	A	652-777	[»]

ProteinModelPortal

Q92995.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92995. 26 interactions.

MINT

MINT-1195142.

STRING

9606.ENSP00000263966.

Protein family/group databases

MEROPS

C19.012.

PTM databases

PhosphoSite

Q92995.

Polymorphism databases

DMDM

209572692.

Proteomic databases

PaxDb

Q92995.

PRIDE

Q92995.

Protocols and materials databases

DNASU

8975.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263966; ENSP00000263966; ENSG00000058056.
ENST00000496897; ENSP00000417146; ENSG00000058056.

GeneID

8975.

KEGG

hsa:8975.

UCSC

uc003fkh.3. human.

Organism-specific databases

CTD

8975.

GeneCards

GC03P179370.

H-InvDB

HIX0003883.

HGNC

HGNC:12611. USP13.

HPA

HPA004827.

MIM

603591. gene.

neXtProt

NX_Q92995.

PharmGKB

PA37237.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5207.

HOGENOM

HOG000162311.

HOVERGEN

HBG002833.

InParanoid

Q92995.

KO

K11836.

OMA

PQQNGIS.

OrthoDB

EOG46DM24.

PhylomeDB

Q92995.

Gene expression databases

ArrayExpress

Q92995.

Bgee

Q92995.

CleanEx

HS_USP13.

Genevestigator

Q92995.

GermOnline

ENSG00000058056. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR016652. Ubiquitinyl_hydrolase.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]

Pfam

PF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]

PIRSF

PIRSF016308. UBP. 1 hit.

SMART

SM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.

PROSITE

PS50030. UBA. 2 hits.
PS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

ProtoNet

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Other

GenomeRNAi

8975.

NextBio

33685.

SOURCE

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Entry information

Entry name

UBP13_HUMAN

Accession

Primary (citable) accession number: Q92995
Secondary accession number(s): A8K2S3 , B4DYF3, D3DNS2, Q96B25

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 14, 2008
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

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.