Reviewed, UniProtKB/Swiss-Prot Q9Y5T5 (UBP16_HUMAN)

Names and origin

Protein names

Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 16
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 16
    Ubiquitin-specific-processing protease 16
    Deubiquitinating enzyme 16
    Ubiquitin-processing protease UBP-M

Gene names

Name:	USP16
ORF Names:	MSTP039

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	823 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Specifically deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-10' of histone H3, and is required for chromosome segregation when cells enter into mitosis. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. Ref.1 Ref.8 Ref.10
Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol. Ref.10
Subunit structure	Homotetramer. Ref.10
Subcellular location	Nucleus Probable.
Tissue specificity	Present in all the tissues examined including fetal brain, lung, liver, kidney, and adult heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.1
Domain	The UBP-type zinc finger binds 3 zinc ions that form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. It recognizes the C-terminal tail of free ubiquitin.
Post-translational modification	Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. The phosphorylated form of the protein is also enzymatically active. Ref.1 Ref.9 Ref.11
Involvement in disease	A chromosomal aberration involving USP16 is a cause of Chronic myelomonocytic leukemia. Inversion inv(21) (q21;q22) with RUNX1/AML1.
Sequence similarities	Belongs to the peptidase C19 family. USP16 subfamily. Contains 1 UBP-type zinc finger.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Chromatin regulator Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW histone deubiquitination Ref.10 Inferred from direct assay. Source: UniProtKB mitosis Ref.10 Inferred from direct assay. Source: UniProtKB positive regulation of transcription, DNA-dependent Ref.10 Inferred from mutant phenotype. Source: UniProtKB protein homotetramerization Ref.10 Inferred from physical interaction. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Ref.1 Traceable author statement. Source: ProtInc nucleus Ref.10 Inferred from direct assay. Source: UniProtKB
Molecular function	cysteine-type endopeptidase activity Ref.10 Inferred from mutant phenotype. Source: UniProtKB histone binding Ref.10 Inferred from direct assay. Source: UniProtKB transcription coactivator activity Ref.10 Inferred from direct assay. Source: UniProtKB ubiquitin binding Ref.14 Inferred from direct assay. Source: UniProtKB ubiquitin thiolesterase activity Ref.10 Inferred from direct assay. Source: UniProtKB ubiquitin-specific protease activity Ref.1 Ref.10 Inferred from direct assay. Source: UniProtKB zinc ion binding Ref.14 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y5T5-1)

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: Q9Y5T5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     150-150: Missing.

Isoform 3 (identifier: Q9Y5T5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MGKKRTKGKTVPIDDSSETL → MGSVAV
     150-150: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9Y5T5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-310: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q9Y5T5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     394-823: SGKKSVNDKN...AYLLFYERIL → VRLLNLFYSSRFFFL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 823	823	Ubiquitin carboxyl-terminal hydrolase 16		PRO_0000080643
Regions
	Zinc finger	60 – 125	66	UBP-type
Sites
	Active site	205	1	Probable
	Active site	750	1	By similarity
	Active site	758	1	By similarity
	Metal binding	24	1	Zinc 1
	Metal binding	26	1	Zinc 1
	Metal binding	48	1	Zinc 2
	Metal binding	51	1	Zinc 2
	Metal binding	74	1	Zinc 3
	Metal binding	77	1	Zinc 3
	Metal binding	82	1	Zinc 2
	Metal binding	88	1	Zinc 2
	Metal binding	90	1	Zinc 2
	Metal binding	94	1	Zinc 3
	Metal binding	103	1	Zinc 3
	Metal binding	116	1	Zinc 1
	Metal binding	119	1	Zinc 1
Amino acid modifications
	Modified residue	415	1	Phosphoserine Ref.11
	Modified residue	552	1	Phosphoserine Ref.9 Ref.11
Natural variations
	Alternative sequence	1 – 310	310	Missing in isoform 4.		VSP_036713
	Alternative sequence	1 – 20	20	MGKKR…SSETL → MGSVAV in isoform 3.		VSP_036714
	Alternative sequence	150	1	Missing in isoform 2 and isoform 3.		VSP_036715
	Alternative sequence	394 – 823	430	SGKKS…YERIL → VRLLNLFYSSRFFFL in isoform 5.		VSP_036716
	Natural variant	141	1	Q → H: dbSNP rs2274802. Ref.3 Ref.6		VAR_020388
Experimental info
	Mutagenesis	205	1	C → S: Loss of enzyme activity. Ref.1 Ref.8 Ref.10
	Sequence conflict	141	1	Q → E in AAG39290. Ref.7
	Sequence conflict	297	1	Q → R in BAG51175. Ref.3
	Sequence conflict	348	1	K → E in BAD96604. Ref.4
	Sequence conflict	350	1	S → P in BAD96401. Ref.4
	Sequence conflict	480 – 481	2	EY → DN in AAH30777. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: C7D4175649BA3E31	FASTA	823	93,570
	10 20 30 40 50 60 MGKKRTKGKT VPIDDSSETL EPVCRHIRKG LEQGNLKKAL VNVEWNICQD CKTDNKVKDK 70 80 90 100 110 120 AEEETEEKPS VWLCLKCGHQ GCGRNSQEQH ALKHYLTPRS EPHCLVLSLD NWSVWCYVCD 130 140 150 160 170 180 NEVQYCSSNQ LGQVVDYVRK QASITTPKPA EKDNGNIELE NKKLEKESKN EQEREKKENM 190 200 210 220 230 240 AKENPPMNSP CQITVKGLSN LGNTCFFNAV MQNLSQTPVL RELLKEVKMS GTIVKIEPPD 250 260 270 280 290 300 LALTEPLEIN LEPPGPLTLA MSQFLNEMQE TKKGVVTPKE LFSQVCKKAV RFKGYQQQDS 310 320 330 340 350 360 QELLRYLLDG MRAEEHQRVS KGILKAFGNS TEKLDEELKN KVKDYEKKKS MPSFVDRIFG 370 380 390 400 410 420 GELTSMIMCD QCRTVSLVHE SFLDLSLPVL DDQSGKKSVN DKNLKKTVED EDQDSEEEKD 430 440 450 460 470 480 NDSYIKERSD IPSGTSKHLQ KKAKKQAKKQ AKNQRRQQKI QGKVLHLNDI CTIDHPEDSE 490 500 510 520 530 540 YEAEMSLQGE VNIKSNHISQ EGVMHKEYCV NQKDLNGQAK MIESVTDNQK STEEVDMKNI 550 560 570 580 590 600 NMDNDLEVLT SSPTRNLNGA YLTEGSNGEV DISNGFKNLN LNAALHPDEI NIEILNDSHT 610 620 630 640 650 660 PGTKVYEVVN EDPETAFCTL ANREVFNTDE CSIQHCLYQF TRNEKLRDAN KLLCEVCTRR 670 680 690 700 710 720 QCNGPKANIK GERKHVYTNA KKQMLISLAP PVLTLHLKRF QQAGFNLRKV NKHIKFPEIL 730 740 750 760 770 780 DLAPFCTLKC KNVAEENTRV LYSLYGVVEH SGTMRSGHYT AYAKARTANS HLSNLVLHGD 790 800 810 820 IPQDFEMESK GQWFHISDTH VQAVPTTKVL NSQAYLLFYE RIL
	Isoform 2. Checksum: 36FD67E22FA078AB	FASTA	822	93,499
	10 20 30 40 50 60 MGKKRTKGKT VPIDDSSETL EPVCRHIRKG LEQGNLKKAL VNVEWNICQD CKTDNKVKDK 70 80 90 100 110 120 AEEETEEKPS VWLCLKCGHQ GCGRNSQEQH ALKHYLTPRS EPHCLVLSLD NWSVWCYVCD 130 140 150 160 170 180 NEVQYCSSNQ LGQVVDYVRK QASITTPKPE KDNGNIELEN KKLEKESKNE QEREKKENMA 190 200 210 220 230 240 KENPPMNSPC QITVKGLSNL GNTCFFNAVM QNLSQTPVLR ELLKEVKMSG TIVKIEPPDL 250 260 270 280 290 300 ALTEPLEINL EPPGPLTLAM SQFLNEMQET KKGVVTPKEL FSQVCKKAVR FKGYQQQDSQ 310 320 330 340 350 360 ELLRYLLDGM RAEEHQRVSK GILKAFGNST EKLDEELKNK VKDYEKKKSM PSFVDRIFGG 370 380 390 400 410 420 ELTSMIMCDQ CRTVSLVHES FLDLSLPVLD DQSGKKSVND KNLKKTVEDE DQDSEEEKDN 430 440 450 460 470 480 DSYIKERSDI PSGTSKHLQK KAKKQAKKQA KNQRRQQKIQ GKVLHLNDIC TIDHPEDSEY 490 500 510 520 530 540 EAEMSLQGEV NIKSNHISQE GVMHKEYCVN QKDLNGQAKM IESVTDNQKS TEEVDMKNIN 550 560 570 580 590 600 MDNDLEVLTS SPTRNLNGAY LTEGSNGEVD ISNGFKNLNL NAALHPDEIN IEILNDSHTP 610 620 630 640 650 660 GTKVYEVVNE DPETAFCTLA NREVFNTDEC SIQHCLYQFT RNEKLRDANK LLCEVCTRRQ 670 680 690 700 710 720 CNGPKANIKG ERKHVYTNAK KQMLISLAPP VLTLHLKRFQ QAGFNLRKVN KHIKFPEILD 730 740 750 760 770 780 LAPFCTLKCK NVAEENTRVL YSLYGVVEHS GTMRSGHYTA YAKARTANSH LSNLVLHGDI 790 800 810 820 PQDFEMESKG QWFHISDTHV QAVPTTKVLN SQAYLLFYER IL
	Isoform 3. Checksum: E4528720234CB7B7	FASTA	808	91,870
	10 20 30 40 50 60 MGSVAVEPVC RHIRKGLEQG NLKKALVNVE WNICQDCKTD NKVKDKAEEE TEEKPSVWLC 70 80 90 100 110 120 LKCGHQGCGR NSQEQHALKH YLTPRSEPHC LVLSLDNWSV WCYVCDNEVQ YCSSNQLGQV 130 140 150 160 170 180 VDYVRKQASI TTPKPEKDNG NIELENKKLE KESKNEQERE KKENMAKENP PMNSPCQITV 190 200 210 220 230 240 KGLSNLGNTC FFNAVMQNLS QTPVLRELLK EVKMSGTIVK IEPPDLALTE PLEINLEPPG 250 260 270 280 290 300 PLTLAMSQFL NEMQETKKGV VTPKELFSQV CKKAVRFKGY QQQDSQELLR YLLDGMRAEE 310 320 330 340 350 360 HQRVSKGILK AFGNSTEKLD EELKNKVKDY EKKKSMPSFV DRIFGGELTS MIMCDQCRTV 370 380 390 400 410 420 SLVHESFLDL SLPVLDDQSG KKSVNDKNLK KTVEDEDQDS EEEKDNDSYI KERSDIPSGT 430 440 450 460 470 480 SKHLQKKAKK QAKKQAKNQR RQQKIQGKVL HLNDICTIDH PEDSEYEAEM SLQGEVNIKS 490 500 510 520 530 540 NHISQEGVMH KEYCVNQKDL NGQAKMIESV TDNQKSTEEV DMKNINMDND LEVLTSSPTR 550 560 570 580 590 600 NLNGAYLTEG SNGEVDISNG FKNLNLNAAL HPDEINIEIL NDSHTPGTKV YEVVNEDPET 610 620 630 640 650 660 AFCTLANREV FNTDECSIQH CLYQFTRNEK LRDANKLLCE VCTRRQCNGP KANIKGERKH 670 680 690 700 710 720 VYTNAKKQML ISLAPPVLTL HLKRFQQAGF NLRKVNKHIK FPEILDLAPF CTLKCKNVAE 730 740 750 760 770 780 ENTRVLYSLY GVVEHSGTMR SGHYTAYAKA RTANSHLSNL VLHGDIPQDF EMESKGQWFH 790 800 ISDTHVQAVP TTKVLNSQAY LLFYERIL
	Isoform 4. Checksum: 9AD260CF2FE530A9	FASTA	513	58,397
	10 20 30 40 50 60 MRAEEHQRVS KGILKAFGNS TEKLDEELKN KVKDYEKKKS MPSFVDRIFG GELTSMIMCD 70 80 90 100 110 120 QCRTVSLVHE SFLDLSLPVL DDQSGKKSVN DKNLKKTVED EDQDSEEEKD NDSYIKERSD 130 140 150 160 170 180 IPSGTSKHLQ KKAKKQAKKQ AKNQRRQQKI QGKVLHLNDI CTIDHPEDSE YEAEMSLQGE 190 200 210 220 230 240 VNIKSNHISQ EGVMHKEYCV NQKDLNGQAK MIESVTDNQK STEEVDMKNI NMDNDLEVLT 250 260 270 280 290 300 SSPTRNLNGA YLTEGSNGEV DISNGFKNLN LNAALHPDEI NIEILNDSHT PGTKVYEVVN 310 320 330 340 350 360 EDPETAFCTL ANREVFNTDE CSIQHCLYQF TRNEKLRDAN KLLCEVCTRR QCNGPKANIK 370 380 390 400 410 420 GERKHVYTNA KKQMLISLAP PVLTLHLKRF QQAGFNLRKV NKHIKFPEIL DLAPFCTLKC 430 440 450 460 470 480 KNVAEENTRV LYSLYGVVEH SGTMRSGHYT AYAKARTANS HLSNLVLHGD IPQDFEMESK 490 500 510 GQWFHISDTH VQAVPTTKVL NSQAYLLFYE RIL
	Isoform 5. Checksum: 5B3EB300F72F4E04	FASTA	408	46,599
	10 20 30 40 50 60 MGKKRTKGKT VPIDDSSETL EPVCRHIRKG LEQGNLKKAL VNVEWNICQD CKTDNKVKDK 70 80 90 100 110 120 AEEETEEKPS VWLCLKCGHQ GCGRNSQEQH ALKHYLTPRS EPHCLVLSLD NWSVWCYVCD 130 140 150 160 170 180 NEVQYCSSNQ LGQVVDYVRK QASITTPKPA EKDNGNIELE NKKLEKESKN EQEREKKENM 190 200 210 220 230 240 AKENPPMNSP CQITVKGLSN LGNTCFFNAV MQNLSQTPVL RELLKEVKMS GTIVKIEPPD 250 260 270 280 290 300 LALTEPLEIN LEPPGPLTLA MSQFLNEMQE TKKGVVTPKE LFSQVCKKAV RFKGYQQQDS 310 320 330 340 350 360 QELLRYLLDG MRAEEHQRVS KGILKAFGNS TEKLDEELKN KVKDYEKKKS MPSFVDRIFG 370 380 390 400 GELTSMIMCD QCRTVSLVHE SFLDLSLPVL DDQVRLLNLF YSSRFFFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division." Cai S.-Y., Babbitt R.W., Marchesi V.T. Proc. Natl. Acad. Sci. U.S.A. 96:2828-2833(1999) [PubMed: 10077596] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF CYS-205.
[2]	Grimbert P., Pawlak A., Sahali D. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), VARIANT HIS-141. Tissue: Amygdala, Teratocarcinoma and Testis.
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain and Liver.
[5]	"The DNA sequence of human chromosome 21." Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L. Nature 405:311-319(2000) [PubMed: 10830953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT HIS-141. Tissue: Testis.
[7]	Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., Liu L.S., Ding J.F. , Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-823. Tissue: Aorta.
[8]	"Caspase-dependent deubiquitination of monoubiquitinated nucleosomal histone H2A induced by diverse apoptogenic stimuli." Mimnaugh E.G., Kayastha G., McGovern N.B., Hwang S.G., Marcu M.G., Trepel J., Cai S.-Y., Marchesi V.T., Neckers L. Cell Death Differ. 8:1182-1196(2001) [PubMed: 11753566] [Abstract] Cited for: PRELIMINARY FUNCTION, MUTAGENESIS OF CYS-205.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Regulation of cell cycle progression and gene expression by H2A deubiquitination." Joo H.-Y., Zhai L., Yang C., Nie S., Erdjument-Bromage H., Tempst P., Chang C., Wang H. Nature 449:1068-1072(2007) [PubMed: 17914355] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-205.
[11]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415 AND SER-552, MASS SPECTROMETRY.
[12]	"Genome profiling of chronic myelomonocytic leukemia: frequent alterations of RAS and RUNX1 genes." Gelsi-Boyer V., Trouplin V., Adelaide J., Aceto N., Remy V., Pinson S., Houdayer C., Arnoulet C., Sainty D., Bentires-Alj M., Olschwang S., Vey N., Mozziconacci M.-J., Birnbaum D., Chaffanet M. BMC Cancer 8:299-299(2008) [PubMed: 18925961] [Abstract] Cited for: CHROMOSOMAL REARRANGEMENT.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin." Pai M.-T., Tzeng S.-R., Kovacs J.J., Keaton M.A., Li S.S.-C., Yao T.-P., Zhou P. J. Mol. Biol. 370:290-302(2007) [PubMed: 17512543] [Abstract] Cited for: STRUCTURE BY NMR OF 22-143, ZINC-BINDING.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF126736 mRNA. Translation: AAD20949.1.
AY333928 mRNA. Translation: AAR13293.1.
AK023247 mRNA. Translation: BAG51175.1. Different initiation.
AK302247 mRNA. Translation: BAG63599.1.
AK294284 mRNA. Translation: BAG57569.1.
AK222681 mRNA. Translation: BAD96401.1.
AK222884 mRNA. Translation: BAD96604.1.
AL163249 Genomic DNA. Translation: CAB90432.1.
AF129075 Genomic DNA. No translation available.
BC030777 mRNA. Translation: AAH30777.1.
AF113219 mRNA. Translation: AAG39290.1. Different initiation.

IPI

IPI00001780.
IPI00428464.
IPI00792644.
IPI00923398.
IPI00923450.

RefSeq

NP_001001992.1.
NP_001027582.1.
NP_006438.1.

UniGene

Hs.99819

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I50	NMR	-	A	22-143	[»]

ModBase

Search...

Protein family/group databases

MEROPS

C19.021.

PTM databases

PhosphoSite

Q9Y5T5.

Proteomic databases

PRIDE

Q9Y5T5.

Genome annotation databases

Ensembl

ENSG00000156256. Homo sapiens. [Contig view]

GeneID

10600.

KEGG

hsa:10600.

UCSC

uc002ymw.1. human.

Organism-specific databases

GeneCards

GC21P029318.

H-InvDB

HIX0023011.

HGNC

HGNC:12614. USP16.

MIM

604735. gene.

PharmGKB

PA38475.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9Y5T5.

HOVERGEN

Q9Y5T5.

OMA

Q9Y5T5. CKNVAEE.

Enzyme and pathway databases

BRENDA

3.1.2.15. 247.

Gene expression databases

ArrayExpress

Q9Y5T5.

Bgee

Q9Y5T5.

CleanEx

HS_USP16.

GermOnline

ENSG00000156256. Homo sapiens.

Family and domain databases

InterPro

IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR001607. Znf_UBP.
[Graphical view]

Pfam

PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]

PROSITE

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 Resources

NextBio

40254.

SOURCE

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Entry information

Entry name

UBP16_HUMAN

Accession

Primary (citable) accession number: Q9Y5T5
Secondary accession number(s): A8MU43 , B3KN13, B4DFV8, B4DY37, Q53GP7, Q53HA0, Q5VKN8, Q8NEL3, Q9H3E6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	July 7, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)