Q9Y5T5 (UBP16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 16
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 16
Ubiquitin thioesterase 16
Ubiquitin-processing protease UBP-M
Ubiquitin-specific-processing protease 16

Gene names

Name:	USP16
ORF Names:	MSTP039

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	823 AA.
Sequence status	Complete.
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.9 Ref.10
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.10
Subunit structure	Homotetramer. Ref.10
Subcellular location	Nucleus Probable Ref.10.
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
Involvement in disease	A chromosomal aberration involving USP16 is a cause of Chronic myelomonocytic leukemia. Inversion inv21 (q21;q22) with RUNX1/AML1.
Sequence similarities	Belongs to the peptidase C19 family. USP16 subfamily. Contains 1 UBP-type zinc finger.
Sequence caution	The sequence AAG39290.1 differs from that shown. Reason: Erroneous initiation. The sequence BAG51175.1 differs from that shown. Reason: Erroneous initiation.

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 Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW histone H2A K63-linked deubiquitination Inferred from mutant phenotype PubMed 20550933. Source: UniProtKB mitosis Inferred from direct assay Ref.10. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of translational elongation Inferred from mutant phenotype PubMed 20550933. Source: UniProtKB protein homotetramerization Inferred from physical interaction Ref.10. Source: UniProtKB response to DNA damage stimulus Inferred from direct assay PubMed 20550933. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Traceable author statement Ref.1. Source: ProtInc nucleus Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	cysteine-type endopeptidase activity Inferred from mutant phenotype Ref.10. Source: UniProtKB histone binding Inferred from direct assay Ref.10. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.10. Source: UniProtKB ubiquitin binding Inferred from direct assay Ref.17. Source: UniProtKB ubiquitin thiolesterase activity Inferred from direct assay Ref.10. Source: UniProtKB ubiquitin-specific protease activity Inferred from direct assay Ref.10. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.17. 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

Nucleophile

Active site

758

1

Proton acceptor 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.12 Ref.16

Modified residue

552

1

Phosphoserine Ref.12 Ref.13 Ref.14

Modified residue

554

1

Phosphothreonine Ref.14

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. Ref.3 Ref.7
Corresponds to variant rs2274802 [ dbSNP | Ensembl ].

VAR_020388

Experimental info

Mutagenesis

205

1

C → S: Loss of enzyme activity. Ref.1 Ref.9 Ref.10

Sequence conflict

141

1

Q → E in AAG39290. Ref.8

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.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

823

Helix Strand Turn

Details...

Helix

27 – 30

4

Helix

33 – 40

8

Beta strand

45 – 47

3

Helix

49 – 52

4

Turn

63 – 65

3

Beta strand

71 – 74

4

Turn

75 – 77

3

Beta strand

80 – 82

3

Beta strand

86 – 88

3

Helix

90 – 96

7

Beta strand

105 – 108

4

Turn

109 – 111

3

Beta strand

114 – 116

3

Turn

117 – 120

4

Beta strand

121 – 123

3

Helix

130 – 142

13

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 [UniParc]. 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 [UniParc]. 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 [UniParc]. 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 [UniParc]. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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), VARIANT HIS-141. Tissue: Testis.
[8]	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.
[9]	"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] [Europe PMC] [Abstract] Cited for: PRELIMINARY FUNCTION, MUTAGENESIS OF CYS-205.
[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] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-205.
[11]	"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] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL REARRANGEMENT.
[12]	"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-415 AND SER-552, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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-552, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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-552 AND THR-554, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"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-415, MASS SPECTROMETRY.
[17]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 22-143, ZINC-BINDING.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
CH471079 Genomic DNA. Translation: EAX09927.1.
CH471079 Genomic DNA. Translation: EAX09929.1.
BC030777 mRNA. Translation: AAH30777.1.
AF113219 mRNA. Translation: AAG39290.1. Different initiation.

IPI

IPI00001780.
IPI00428464.
IPI00792644.
IPI00923398.
IPI00923450.

RefSeq

NP_001001992.1. NM_001001992.1.
NP_001027582.1. NM_001032410.1.
NP_006438.1. NM_006447.2.

UniGene

Hs.99819.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q9Y5T5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y5T5. 4 interactions.

Protein family/group databases

MEROPS

C19.021.

PTM databases

PhosphoSite

Q9Y5T5.

Polymorphism databases

DMDM

6686071.

Proteomic databases

PaxDb

Q9Y5T5.

PRIDE

Q9Y5T5.

Protocols and materials databases

DNASU

10600.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000334352; ENSP00000334808; ENSG00000156256.
ENST00000399975; ENSP00000382857; ENSG00000156256.
ENST00000399976; ENSP00000382858; ENSG00000156256.

GeneID

10600.

KEGG

hsa:10600.

UCSC

uc002ymw.3. human.
uc002ymx.3. human.
uc011acm.2. human.

Organism-specific databases

CTD

10600.

GeneCards

GC21P030396.

H-InvDB

HIX0023011.

HGNC

HGNC:12614. USP16.

HPA

HPA021140.

MIM

604735. gene.

neXtProt

NX_Q9Y5T5.

PharmGKB

PA37240.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5560.

HOVERGEN

HBG062704.

InParanoid

Q9Y5T5.

KO

K11844.

OMA

CKNVAEE.

PhylomeDB

Q9Y5T5.

Gene expression databases

ArrayExpress

Q9Y5T5.

Bgee

Q9Y5T5.

CleanEx

HS_USP16.

Genevestigator

Q9Y5T5.

GermOnline

ENSG00000156256. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR013083. Znf_RING/FYVE/PHD.
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

Search...

Other

ChiTaRS

USP16. human.

EvolutionaryTrace

Q9Y5T5.

GenomeRNAi

10600.

NextBio

40254.

SOURCE

Search...

Entry information

Entry name

UBP16_HUMAN

Accession

Primary (citable) accession number: Q9Y5T5
Secondary accession number(s): A8MU43 , B3KN13, B4DFV8, B4DY37, D3DSD9, Q53GP7, Q53HA0, Q5VKN8, Q8NEL3, Q9H3E6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 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.