Q9H9J4 (UBP42_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	1324 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis Ubl conjugation pathway
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW protein deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB spermatogenesis Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity 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: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1324	1324	Ubiquitin carboxyl-terminal hydrolase 42		PRO_0000080672
Regions
	Compositional bias	742 – 937	196	Pro-rich
	Compositional bias	946 – 1118	173	Arg-rich
	Compositional bias	1176 – 1246	71	Lys-rich
Sites
	Active site	120	1	Nucleophile By similarity
	Active site	371	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	856	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10
	Modified residue	1226	1	Phosphoserine Ref.6
	Modified residue	1247	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	1316 – 1324	9	KRRYLELGR → D in isoform 2.		VSP_040529
	Natural variant	1030	1	L → P. Corresponds to variant rs6463529 [ dbSNP | Ensembl ].		VAR_059754
Experimental info
	Sequence conflict	655	1	M → T in CAE53097. Ref.1
	Sequence conflict	655	1	M → T in BAB14232. Ref.5
	Sequence conflict	1214	1	R → RR in CAE53097. Ref.1
	Sequence conflict	1217	1	Q → R in AAT67238. Ref.4
	Sequence conflict	1294	1	K → E in AAT67238. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 8, 2011. Version 3. Checksum: 6EB4975521ABF516	FASTA	1,324	145,392
	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
	Isoform 2 [UniParc]. Checksum: 28998E673C8EFE3B	FASTA	1,316	144,335
	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 VTSLETVAQF RRAQGGFPLS GGPPLEGVGP FREKTKHLRM ESRDDRCRLF EYGQGD

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, 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-856, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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 AND SER-1247, MASS SPECTROMETRY.
+	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.
IPI	IPI00784612. IPI01009873.
RefSeq	NP_115548.1. NM_032172.2.
UniGene	Hs.31856.
3D structure databases
ProteinModelPortal	Q9H9J4.
SMR	Q9H9J4. Positions 111-409.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H9J4. 24 interactions.
STRING	9606.ENSP00000301962.
Protein family/group databases
MEROPS	C19.048.
PTM databases
PhosphoSite	Q9H9J4.
Polymorphism databases
DMDM	85681903.
Proteomic databases
PaxDb	Q9H9J4.
PRIDE	Q9H9J4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000306177; ENSP00000301962; ENSG00000106346.
GeneID	84132.
KEGG	hsa:84132.
UCSC	uc011jwo.1. human. uc011jwp.2. human.
Organism-specific databases
CTD	84132.
GeneCards	GC07P006144.
H-InvDB	HIX0006462.
HGNC	HGNC:20068. USP42.
HPA	HPA006752.
neXtProt	NX_Q9H9J4.
PharmGKB	PA134902515.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5533.
HOGENOM	HOG000236355.
HOVERGEN	HBG080724.
InParanoid	Q9H9J4.
KO	K11855.
OMA	ALHSENP.
OrthoDB	EOG4RV2RB.
Gene expression databases
ArrayExpress	Q9H9J4.
Bgee	Q9H9J4.
CleanEx	HS_USP42.
Genevestigator	Q9H9J4.
GermOnline	ENSG00000106346. Homo sapiens.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	84132.
NextBio	73425.
PMAP-CutDB	Q9H9J4.

Entry information

Entry name

UBP42_HUMAN

Accession

Primary (citable) accession number: Q9H9J4
Secondary accession number(s): A2RUE3 , B5MDA5, Q0VIN8, Q3C166, Q6P9B4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	February 8, 2011
Last modified:	May 1, 2013
This is version 103 of the entry and version 3 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.