Q8NB14 (UBP38_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 38
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 38
HP43.8KD
Ubiquitin thioesterase 38
Ubiquitin-specific-processing protease 38

Gene names

Name:	USP38
Synonyms:	KIAA1891

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	1042 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Deubiquitinating enzyme exhibiting a preference towards 'Lys-63'-linked Ubiquitin chains. Ref.8
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.7
Tissue specificity	Highly expressed in skeletal muscle. Expressed in adrenal gland. Ref.5 Ref.7
Sequence similarities	Belongs to the peptidase C19 family.
Sequence caution	The sequence AAK26248.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB71627.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC03730.1 differs from that shown. Reason: The absence of the residues from Tyr-840 to Ser-871 is not the result of an alternative splicing.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1042	1042	Ubiquitin carboxyl-terminal hydrolase 38		PRO_0000080668
Sites
	Active site	454	1	Nucleophile By similarity
	Active site	857	1	Proton acceptor By similarity
Experimental info
	Sequence conflict	646	1	M → V in BAC03730. Ref.1
	Sequence conflict	919	1	S → G in BAB71627. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8NB14 [UniParc]. Last modified October 10, 2003. Version 2. Checksum: D888D4F44C6E7251	FASTA	1,042	116,546
	10 20 30 40 50 60 MDKILEGLVS SSHPLPLKRV IVRKVVESAE HWLDEAQCEA MFDLTTRLIL EGQDPFQRQV 70 80 90 100 110 120 GHQVLEAYAR YHRPEFESFF NKTFVLGLLH QGYHSLDRKD VAILDYIHNG LKLIMSCPSV 130 140 150 160 170 180 LDLFSLLQVE VLRMVCERPE PQLCARLSDL LTDFVQCIPK GKLSITFCQQ LVRTIGHFQC 190 200 210 220 230 240 VSTQERELRE YVSQVTKVSN LLQNIWKAEP ATLLPSLQEV FASISSTDAS FEPSVALASL 250 260 270 280 290 300 VQHIPLQMIT VLIRSLTTDP NVKDASMTQA LCRMIDWLSW PLAQHVDTWV IALLKGLAAV 310 320 330 340 350 360 QKFTILIDVT LLKIELVFNR LWFPLVRPGA LAVLSHMLLS FQHSPEAFHL IVPHVVNLVH 370 380 390 400 410 420 SFKNDGLPSS TAFLVQLTEL IHCMMYHYSG FPDLYEPILE AIKDFPKPSE EKIKLILNQS 430 440 450 460 470 480 AWTSQSNSLA SCLSRLSGKS ETGKTGLINL GNTCYMNSVI QALFMATDFR RQVLSLNLNG 490 500 510 520 530 540 CNSLMKKLQH LFAFLAHTQR EAYAPRIFFE ASRPPWFTPR SQQDCSEYLR FLLDRLHEEE 550 560 570 580 590 600 KILKVQASHK PSEILECSET SLQEVASKAA VLTETPRTSD GEKTLIEKMF GGKLRTHIRC 610 620 630 640 650 660 LNCRSTSQKV EAFTDLSLAF CPSSSLENMS VQDPASSPSI QDGGLMQASV PGPSEEPVVY 670 680 690 700 710 720 NPTTAAFICD SLVNEKTIGS PPNEFYCSEN TSVPNESNKI LVNKDVPQKP GGETTPSVTD 730 740 750 760 770 780 LLNYFLAPEI LTGDNQYYCE NCASLQNAEK TMQITEEPEY LILTLLRFSY DQKYHVRRKI 790 800 810 820 830 840 LDNVSLPLVL ELPVKRITSF SSLSESWSVD VDFTDLSENL AKKLKPSGTD EASCTKLVPY 850 860 870 880 890 900 LLSSVVVHSG ISSESGHYYS YARNITSTDS SYQMYHQSEA LALASSQSHL LGRDSPSAVF 910 920 930 940 950 960 EQDLENKEMS KEWFLFNDSR VTFTSFQSVQ KITSRFPKDT AYVLLYKKQH STNGLSGNNP 970 980 990 1000 1010 1020 TSGLWINGDP PLQKELMDAI TKDNKLYLQE QELNARARAL QAASASCSFR PNGFDDNDPP 1030 1040 GSCGPTGGGG GGGFNTVGRL VF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Tissue: Brain, Chondrocyte and Gastric mucosa.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[3]	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].
[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]. Tissue: Testis.
[5]	"Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins." Nagase T., Kikuno R., Ohara O. DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-1042, TISSUE SPECIFICITY. Tissue: Brain.
[6]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 633-1042. Tissue: Adrenal gland.
[7]	"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: TISSUE SPECIFICITY, ENZYME ACTIVITY.
[8]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK057992 mRNA. Translation: BAB71627.1. Different initiation. AK091712 mRNA. Translation: BAC03730.1. Sequence problems. AK126943 mRNA. Translation: BAG54405.1. AL833976 mRNA. Translation: CAD38820.1. CH471056 Genomic DNA. Translation: EAX05075.1. BC068975 mRNA. Translation: AAH68975.1. AB067478 mRNA. Translation: BAB67784.1. AF211481 mRNA. Translation: AAK26248.1. Different initiation.
IPI	IPI00168084.
RefSeq	NP_115946.2. NM_032557.5.
UniGene	Hs.480848.
3D structure databases
ProteinModelPortal	Q8NB14.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NB14. 6 interactions.
STRING	9606.ENSP00000303434.
Protein family/group databases
MEROPS	C19.056.
PTM databases
PhosphoSite	Q8NB14.
Polymorphism databases
DMDM	38372866.
Proteomic databases
PaxDb	Q8NB14.
PRIDE	Q8NB14.
Protocols and materials databases
DNASU	84640.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000307017; ENSP00000303434; ENSG00000170185.
GeneID	84640.
KEGG	hsa:84640.
UCSC	uc003ijb.3. human.
Organism-specific databases
CTD	84640.
GeneCards	GC04P144106.
HGNC	HGNC:20067. USP38.
HPA	HPA047948.
neXtProt	NX_Q8NB14.
PharmGKB	PA134880611.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5560.
HOGENOM	HOG000007432.
HOVERGEN	HBG060424.
InParanoid	Q8NB14.
KO	K11854.
OMA	HYYSYAR.
PhylomeDB	Q8NB14.
Gene expression databases
ArrayExpress	Q8NB14.
Bgee	Q8NB14.
CleanEx	HS_USP38.
Genevestigator	Q8NB14.
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
ChiTaRS	USP38. human.
GenomeRNAi	84640.
NextBio	74575.

Entry information

Entry name

UBP38_HUMAN

Accession

Primary (citable) accession number: Q8NB14
Secondary accession number(s): B3KX93 , Q8NDF5, Q96DK6, Q96PZ6, Q9BY55

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	October 10, 2003
Last modified:	April 3, 2013
This is version 90 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.