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Q9H9J4 (UBP42_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 42

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 42
Ubiquitin thioesterase 42
Ubiquitin-specific-processing protease 42
Gene names
Name:USP42
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1324 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deubiquitinating enzyme which may play an important role during spermatogenesis By similarity.

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). Ref.1

Tissue specificity

Broadly expressed. Ref.1

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TP53P046372EBI-9118105,EBI-366083

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H9J4-1)

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: Q9H9J4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1316-1324: KRRYLELGR → D

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13241324Ubiquitin carboxyl-terminal hydrolase 42
PRO_0000080672

Regions

Domain111 – 412302USP
Compositional bias742 – 937196Pro-rich
Compositional bias946 – 1118173Arg-rich
Compositional bias1176 – 124671Lys-rich

Sites

Active site1201Nucleophile By similarity
Active site3711Proton acceptor By similarity

Amino acid modifications

Modified residue8561Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11
Modified residue12261Phosphoserine Ref.6

Natural variations

Alternative sequence1316 – 13249KRRYLELGR → D in isoform 2.
VSP_040529
Natural variant10301L → P.
Corresponds to variant rs6463529 [ dbSNP | Ensembl ].
VAR_059754

Experimental info

Sequence conflict6551M → T in CAE53097. Ref.1
Sequence conflict6551M → T in BAB14232. Ref.5
Sequence conflict12141R → RR in CAE53097. Ref.1
Sequence conflict12171Q → R in AAT67238. Ref.4
Sequence conflict12941K → E in AAT67238. Ref.4

Sequences

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

Last modified February 8, 2011. Version 3.
Checksum: 6EB4975521ABF516

FASTA1,324145,392
        10         20         30         40         50         60 
MTIVDKASES SDPSAYQNQP GSSEAVSPGD MDAGSASWGA VSSLNDVSNH TLSLGPVPGA 

        70         80         90        100        110        120 
VVYSSSSVPD KSKPSPQKDQ ALGDGIAPPQ KVLFPSEKIC LKWQQTHRVG AGLQNLGNTC 

       130        140        150        160        170        180 
FANAALQCLT YTPPLANYML SHEHSKTCHA EGFCMMCTMQ AHITQALSNP GDVIKPMFVI 

       190        200        210        220        230        240 
NEMRRIARHF RFGNQEDAHE FLQYTVDAMQ KACLNGSNKL DRHTQATTLV CQIFGGYLRS 

       250        260        270        280        290        300 
RVKCLNCKGV SDTFDPYLDI TLEIKAAQSV NKALEQFVKP EQLDGENSYK CSKCKKMVPA 

       310        320        330        340        350        360 
SKRFTIHRSS NVLTLSLKRF ANFTGGKIAK DVKYPEYLDI RPYMSQPNGE PIVYVLYAVL 

       370        380        390        400        410        420 
VHTGFNCHAG HYFCYIKASN GLWYQMNDSI VSTSDIRSVL SQQAYVLFYI RSHDVKNGGE 

       430        440        450        460        470        480 
LTHPTHSPGQ SSPRPVISQR VVTNKQAAPG FIGPQLPSHM IKNPPHLNGT GPLKDTPSSS 

       490        500        510        520        530        540 
MSSPNGNSSV NRASPVNASA SVQNWSVNRS SVIPEHPKKQ KITISIHNKL PVRQCQSQPN 

       550        560        570        580        590        600 
LHSNSLENPT KPVPSSTITN SAVQSTSNAS TMSVSSKVTK PIPRSESCSQ PVMNGKSKLN 

       610        620        630        640        650        660 
SSVLVPYGAE SSEDSDEESK GLGKENGIGT IVSSHSPGQD AEDEEATPHE LQEPMTLNGA 

       670        680        690        700        710        720 
NSADSDSDPK ENGLAPDGAS CQGQPALHSE NPFAKANGLP GKLMPAPLLS LPEDKILETF 

       730        740        750        760        770        780 
RLSNKLKGST DEMSAPGAER GPPEDRDAEP QPGSPAAESL EEPDAAAGLS STKKAPPPRD 

       790        800        810        820        830        840 
PGTPATKEGA WEAMAVAPEE PPPSAGEDIV GDTAPPDLCD PGSLTGDASP LSQDAKGMIA 

       850        860        870        880        890        900 
EGPRDSALAE APEGLSPAPP ARSEEPCEQP LLVHPSGDHA RDAQDPSQSL GAPEAAERPP 

       910        920        930        940        950        960 
APVLDMAPAG HPEGDAEPSP GERVEDAAAP KAPGPSPAKE KIGSLRKVDR GHYRSRRERS 

       970        980        990       1000       1010       1020 
SSGEPARESR SKTEGHRHRR RRTCPRERDR QDRHAPEHHP GHGDRLSPGE RRSLGRCSHH 

      1030       1040       1050       1060       1070       1080 
HSRHRSGVEL DWVRHHYTEG ERGWGREKFY PDRPRWDRCR YYHDRYALYA ARDWKPFHGG 

      1090       1100       1110       1120       1130       1140 
REHERAGLHE RPHKDHNRGR RGCEPARERE RHRPSSPRAG APHALAPHPD RFSHDRTALV 

      1150       1160       1170       1180       1190       1200 
AGDNCNLSDR FHEHENGKSR KRRHDSVENS DSHVEKKARR SEQKDPLEEP KAKKHKKSKK 

      1210       1220       1230       1240       1250       1260 
KKKSKDKHRD RDSRHQQDSD LSAACSDADL HRHKKKKKKK KRHSRKSEDF VKDSELHLPR 

      1270       1280       1290       1300       1310       1320 
VTSLETVAQF RRAQGGFPLS GGPPLEGVGP FREKTKHLRM ESRDDRCRLF EYGQGKRRYL 


ELGR 

« Hide

Isoform 2 [UniParc].

Checksum: 28998E673C8EFE3B
Show »

FASTA1,316144,335

References

« Hide 'large scale' references
[1]"Cloning and enzymatic analysis of 22 novel human ubiquitin-specific proteases."
Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S., Lopez-Otin C.
Biochem. Biophys. Res. Commun. 314:54-62(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, ENZYME ACTIVITY.
[2]"A discovery of a novel deubiquitinating enzyme human USP42."
Baek K.-H., Yoo K.-J.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1202 (ISOFORM 1).
Tissue: Placenta.
[5]"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] OF 1-1198.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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 SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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 SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ601395 mRNA. Translation: CAE53097.1.
AY618868 mRNA. Translation: AAT67238.1.
AC004895 Genomic DNA. No translation available.
BC060846 mRNA. Translation: AAH60846.2.
BC132862 mRNA. Translation: AAI32863.1.
AK022759 mRNA. Translation: BAB14232.1.
RefSeqNP_115548.1. NM_032172.2.
XP_005249939.1. XM_005249882.2.
UniGeneHs.31856.

3D structure databases

ProteinModelPortalQ9H9J4.
SMRQ9H9J4. Positions 111-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123904. 30 interactions.
IntActQ9H9J4. 27 interactions.
MINTMINT-7899498.
STRING9606.ENSP00000301962.

Protein family/group databases

MEROPSC19.048.

PTM databases

PhosphoSiteQ9H9J4.

Polymorphism databases

DMDM322510098.

Proteomic databases

PaxDbQ9H9J4.
PRIDEQ9H9J4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306177; ENSP00000301962; ENSG00000106346. [Q9H9J4-2]
GeneID84132.
KEGGhsa:84132.
UCSCuc011jwo.1. human. [Q9H9J4-1]
uc011jwp.2. human. [Q9H9J4-2]

Organism-specific databases

CTD84132.
GeneCardsGC07P006144.
H-InvDBHIX0006462.
HGNCHGNC:20068. USP42.
HPAHPA006752.
neXtProtNX_Q9H9J4.
PharmGKBPA134902515.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000236355.
HOVERGENHBG080724.
InParanoidQ9H9J4.
KOK11855.
OMAGKLMPAP.
OrthoDBEOG72VH5K.
PhylomeDBQ9H9J4.
TreeFamTF315281.

Gene expression databases

ArrayExpressQ9H9J4.
BgeeQ9H9J4.
CleanExHS_USP42.
GenevestigatorQ9H9J4.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiUSP42.
GenomeRNAi84132.
NextBio73425.
PMAP-CutDBQ9H9J4.
PROQ9H9J4.

Entry information

Entry nameUBP42_HUMAN
AccessionPrimary (citable) accession number: Q9H9J4
Secondary accession number(s): A2RUE3 expand/collapse secondary AC list , B5MDA5, Q0VIN8, Q3C166, Q6P9B4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: February 8, 2011
Last modified: April 16, 2014
This is version 113 of the entry and version 3 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

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 7

Human chromosome 7: entries, gene names and cross-references to MIM