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Protein

Ubiquitin carboxyl-terminal hydrolase 44

Gene

Usp44

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei281 – 2811NucleophilePROSITE-ProRule annotation
Active sitei635 – 6351Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri24 – 8562UBP-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: MGI
  2. ubiquitin thiolesterase activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. mitotic nuclear division Source: UniProtKB-KW
  3. negative regulation of mitotic anaphase-promoting complex activity Source: MGI
  4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  5. protein deubiquitination Source: MGI
  6. regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
  7. regulation of spindle checkpoint Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC19.057.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Usp44
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:3045318. Usp44.

Subcellular locationi

Nucleus 1 Publication
Note: Peaks in interphase, with relatively low levels maintained throughout mitosis.

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 711711Ubiquitin carboxyl-terminal hydrolase 44PRO_0000395811Add
BLAST

Post-translational modificationi

Dephosphorylated by CTDP1.By similarity
Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome.

Keywords - PTMi

Ubl conjugation

Proteomic databases

PRIDEiQ8C2S0.

PTM databases

PhosphoSiteiQ8C2S0.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in lung, pancreas, skin, liver, stomach and intestine.1 Publication

Gene expression databases

BgeeiQ8C2S0.
GenevestigatoriQ8C2S0.

Interactioni

Protein-protein interaction databases

BioGridi236490. 1 interaction.
STRINGi10090.ENSMUSP00000092975.

Structurei

3D structure databases

ProteinModelPortaliQ8C2S0.
SMRiQ8C2S0. Positions 26-83, 371-677.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini272 – 677406USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family. USP44 subfamily.Curated
Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri24 – 8562UBP-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1867.
HOGENOMiHOG000015084.
HOVERGENiHBG018027.
InParanoidiQ8C2S0.
KOiK11834.
OrthoDBiEOG7JX33S.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C2S0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDRCKHVEQL QLAQGHSILD PQKWYCMVCN TTESIWACLS CSHVACGKYI
60 70 80 90 100
QEHALKHFQE SSHPVAFEVN DMYAFCYLCN DYVLNDNAAG DLKSLRSTLS
110 120 130 140 150
TIKSKKYPCV VPSDSVLHPV DAQDRVYSLL DGTQSLPGNE DPTCAALWHR
160 170 180 190 200
RRVLMGKAFR TWFEQSAIGR KGQEPTQERM VAKREAKRRQ QQELEQQMKA
210 220 230 240 250
ELESTPPRKS LRLQGSSEEA ATIEIVPVRA PPPPPASPAK DKAALPTSED
260 270 280 290 300
RTFKKVSDSL IKRRPMVTPG VTGLRNLGNT CYMNSVLQVL SHLLIFRQCF
310 320 330 340 350
LKLDLNQWLA VAASDKARSY KHSAVTEAAA QQMNEGQEKE KGFVCSRHSG
360 370 380 390 400
LSSGLSGGAS KGRNMELIQP REPSSPYSSL CHELHILFQV MWSGEWALVS
410 420 430 440 450
PFAMLHSVWR LIPAFRGYAQ QDAQEFLCEL LDKIQRELET TGTKLPALIP
460 470 480 490 500
TSQRRLIEQV LNVVNNIFHG QFLSQVTCLA CDNKSDTIES FWDLSLEFPE
510 520 530 540 550
RYQCSGKDAA SQPCLVTDML DKFTETEALE GKIYMCDHCN SKRRKFSSKS
560 570 580 590 600
VVFTEAQKQL MICHLPQVLR LHLKRFRWSG RNNREKIGVH VVFEETLNME
610 620 630 640 650
PYCCRETLNA LRPECFLYNL SAVVIHHGKG FGSGHYTAYC YNSEGGFWVH
660 670 680 690 700
CNDSKLSMCT MEEVRKAQAY ILFYTQRVTE NGHSKLLPPE LLSNSQHPSK
710
ETDASSNEVL S
Length:711
Mass (Da):80,479
Last modified:November 28, 2012 - v3
Checksum:iF176DB2BA3C658BE
GO

Sequence cautioni

The sequence AAI11887.1 differs from that shown.Intron retention.Curated
The sequence BAC40148.1 differs from that shown.Intron retention.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001193780.1. NM_001206851.1.
UniGeneiMm.491598.

Genome annotation databases

GeneIDi327799.
KEGGimmu:327799.
UCSCiuc011xlw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001193780.1. NM_001206851.1.
UniGeneiMm.491598.

3D structure databases

ProteinModelPortaliQ8C2S0.
SMRiQ8C2S0. Positions 26-83, 371-677.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi236490. 1 interaction.
STRINGi10090.ENSMUSP00000092975.

Protein family/group databases

MEROPSiC19.057.

PTM databases

PhosphoSiteiQ8C2S0.

Proteomic databases

PRIDEiQ8C2S0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi327799.
KEGGimmu:327799.
UCSCiuc011xlw.1. mouse.

Organism-specific databases

CTDi84101.
MGIiMGI:3045318. Usp44.

Phylogenomic databases

eggNOGiKOG1867.
HOGENOMiHOG000015084.
HOVERGENiHBG018027.
InParanoidiQ8C2S0.
KOiK11834.
OrthoDBiEOG7JX33S.

Miscellaneous databases

NextBioi397964.
PROiQ8C2S0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C2S0.
GenevestigatoriQ8C2S0.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiUBP44_MOUSE
AccessioniPrimary (citable) accession number: Q8C2S0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: November 28, 2012
Last modified: February 4, 2015
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.