Q8C2S0 (UBP44_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 44
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 44
Ubiquitin thioesterase 44
Ubiquitin-specific-processing protease 44

Gene names

Name:

Usp44

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	711 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Acts as a negative regulator of histone H2B (H2BK120ub1) ubiquitination. Ref.1
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).
Subcellular location	Nucleus. Note: Peaks in interphase, with relatively low levels maintained throughout mitosis. Ref.1
Tissue specificity	Widely expressed. Highly expressed in lung, pancreas, skin, liver, stomach and intestine. Ref.5
Post-translational modification	Dephosphorylated by CTDP1 By similarity. Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome. Ref.1
Sequence similarities	Belongs to the peptidase C19 family. USP44 subfamily. Contains 1 UBP-type zinc finger.
Sequence caution	The sequence AAI11887.1 differs from that shown. Reason: Intron retention. The sequence BAC40148.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anaphase Inferred from electronic annotation. Source: Compara cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of mitotic anaphase-promoting complex activity Inferred from electronic annotation. Source: Compara proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.1. Source: UniProtKB protein deubiquitination Inferred from electronic annotation. Source: Compara regulation of mitotic cell cycle spindle assembly checkpoint Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	nucleus Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	ubiquitin thiolesterase activity Inferred from electronic annotation. Source: Compara ubiquitin-specific protease activity Inferred from electronic annotation. Source: Compara zinc ion binding 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 – 711	711	Ubiquitin carboxyl-terminal hydrolase 44		PRO_0000395811
Regions
	Zinc finger	24 – 85	62	UBP-type
Sites
	Active site	281	1	Nucleophile By similarity
	Active site	635	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8C2S0 [UniParc]. Last modified November 28, 2012. Version 3. Checksum: F176DB2BA3C658BE	FASTA	711	80,479
	10 20 30 40 50 60 MDRCKHVEQL QLAQGHSILD PQKWYCMVCN TTESIWACLS CSHVACGKYI QEHALKHFQE 70 80 90 100 110 120 SSHPVAFEVN DMYAFCYLCN DYVLNDNAAG DLKSLRSTLS TIKSKKYPCV VPSDSVLHPV 130 140 150 160 170 180 DAQDRVYSLL DGTQSLPGNE DPTCAALWHR RRVLMGKAFR TWFEQSAIGR KGQEPTQERM 190 200 210 220 230 240 VAKREAKRRQ QQELEQQMKA ELESTPPRKS LRLQGSSEEA ATIEIVPVRA PPPPPASPAK 250 260 270 280 290 300 DKAALPTSED RTFKKVSDSL IKRRPMVTPG VTGLRNLGNT CYMNSVLQVL SHLLIFRQCF 310 320 330 340 350 360 LKLDLNQWLA VAASDKARSY KHSAVTEAAA QQMNEGQEKE KGFVCSRHSG LSSGLSGGAS 370 380 390 400 410 420 KGRNMELIQP REPSSPYSSL CHELHILFQV MWSGEWALVS PFAMLHSVWR LIPAFRGYAQ 430 440 450 460 470 480 QDAQEFLCEL LDKIQRELET TGTKLPALIP TSQRRLIEQV LNVVNNIFHG QFLSQVTCLA 490 500 510 520 530 540 CDNKSDTIES FWDLSLEFPE RYQCSGKDAA SQPCLVTDML DKFTETEALE GKIYMCDHCN 550 560 570 580 590 600 SKRRKFSSKS VVFTEAQKQL MICHLPQVLR LHLKRFRWSG RNNREKIGVH VVFEETLNME 610 620 630 640 650 660 PYCCRETLNA LRPECFLYNL SAVVIHHGKG FGSGHYTAYC YNSEGGFWVH CNDSKLSMCT 670 680 690 700 710 MEEVRKAQAY ILFYTQRVTE NGHSKLLPPE LLSNSQHPSK ETDASSNEVL S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Overexpression of ubiquitin specific protease 44 (USP44) induces chromosomal instability and is frequently observed in human T-cell leukemia." Zhang Y., van Deursen J., Galardy P.J. PLoS ONE 6:E23389-E23389(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, PROTEASOMAL DEGRADATION. Tissue: Kidney.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: NOD. Tissue: Thymus.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[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].
[5]	"K48- and K63-linked polyubiquitination of deubiquitinating enzyme USP44." Suresh B., Ramakrishna S., Lee H.J., Choi J.H., Kim J.Y., Ahn W.S., Baek K.H. Cell Biol. Int. 34:799-808(2010) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK088109 mRNA. Translation: BAC40148.1. Sequence problems. CJ236846 mRNA. No translation available. AC124686 Genomic DNA. No translation available. BC111886 mRNA. Translation: AAI11887.1. Sequence problems.
IPI	IPI00224757.
RefSeq	NP_001193780.1. NM_001206851.1.
UniGene	Mm.276331.
3D structure databases
ProteinModelPortal	Q8C2S0.
SMR	Q8C2S0. Positions 26-83, 268-677.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000092975.
PTM databases
PhosphoSite	Q8C2S0.
Proteomic databases
PRIDE	Q8C2S0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	327799.
KEGG	mmu:327799.
UCSC	uc011xlw.1. mouse.
Organism-specific databases
CTD	84101.
MGI	MGI:3045318. Usp44.
Phylogenomic databases
eggNOG	KOG1867.
HOGENOM	HOG000015084.
HOVERGEN	HBG018027.
InParanoid	Q8C2S0.
KO	K11834.
OrthoDB	EOG4XGZZK.
Gene expression databases
Bgee	Q8C2S0.
Genevestigator	Q8C2S0.
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	PS50271. ZF_UBP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	397964.
SOURCE	Search...

Entry information

Entry name

UBP44_MOUSE

Accession

Primary (citable) accession number: Q8C2S0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 13, 2010
Last sequence update:	November 28, 2012
Last modified:	May 1, 2013
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program