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Q9H0E7 (UBP44_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length712 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.6 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.5 Ref.6 Ref.7

Subcellular location

Nucleus. Note: Peaks in interphase, with relatively low levels maintained throughout mitosis By similarity. Ref.7

Tissue specificity

Expressed in testis. Expressed at high levels in T-cell acute lymphoblastic leukemia. Ref.5 Ref.9

Developmental stage

Elevated in mitosis; levels increase in mitotic cells and rapidly decrease once cells have completed chromosome attachment and exit from mitosis. Ref.6

Induction

Transcriptionally regulated by POU5F1/OCT4 in embryonic stem cells and embryonal carcinoma cells. Ref.8

Post-translational modification

Dephosphorylated by CTDP1. Ref.6 Ref.11

Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome. Ref.7

Sequence similarities

Belongs to the peptidase C19 family. USP44 subfamily.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 712712Ubiquitin carboxyl-terminal hydrolase 44
PRO_0000080673

Regions

Domain273 – 678406USP
Zinc finger27 – 8862UBP-type

Sites

Active site2821Nucleophile
Active site6361Proton acceptor By similarity

Amino acid modifications

Modified residue1691Phosphoserine Probable
Modified residue2391Phosphoserine Probable
Modified residue2691Phosphothreonine Probable
Modified residue4011Phosphoserine Probable

Natural variations

Natural variant911T → A. Ref.1 Ref.2 Ref.4
Corresponds to variant rs3812813 [ dbSNP | Ensembl ].
VAR_017125
Natural variant3161E → Q.
Corresponds to variant rs7305024 [ dbSNP | Ensembl ].
VAR_057043
Natural variant3481R → G.
Corresponds to variant rs7135642 [ dbSNP | Ensembl ].
VAR_057044

Experimental info

Mutagenesis2821C → S or A: Abolishes deubiquitinase activity. Ref.6 Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q9H0E7 [UniParc].

Last modified July 13, 2010. Version 2.
Checksum: A8211DFAD78EE731

FASTA71281,185
        10         20         30         40         50         60 
MLAMDTCKHV GQLQLAQDHS SLNPQKWHCV DCNTTESIWA CLSCSHVACG RYIEEHALKH 

        70         80         90        100        110        120 
FQESSHPVAL EVNEMYVFCY LCDDYVLNDN TTGDLKLLRR TLSAIKSQNY HCTTRSGRFL 

       130        140        150        160        170        180 
RSMGTGDDSY FLHDGAQSLL QSEDQLYTAL WHRRRILMGK IFRTWFEQSP IGRKKQEEPF 

       190        200        210        220        230        240 
QEKIVVKREV KKRRQELEYQ VKAELESMPP RKSLRLQGLA QSTIIEIVSV QVPAQTPASP 

       250        260        270        280        290        300 
AKDKVLSTSE NEISQKVSDS SVKRRPIVTP GVTGLRNLGN TCYMNSVLQV LSHLLIFRQC 

       310        320        330        340        350        360 
FLKLDLNQWL AMTASEKTRS CKHPPVTDTV VYQMNECQEK DTGFVCSRQS SLSSGLSGGA 

       370        380        390        400        410        420 
SKGRKMELIQ PKEPTSQYIS LCHELHTLFQ VMWSGKWALV SPFAMLHSVW RLIPAFRGYA 

       430        440        450        460        470        480 
QQDAQEFLCE LLDKIQRELE TTGTSLPALI PTSQRKLIKQ VLNVVNNIFH GQLLSQVTCL 

       490        500        510        520        530        540 
ACDNKSNTIE PFWDLSLEFP ERYQCSGKDI ASQPCLVTEM LAKFTETEAL EGKIYVCDQC 

       550        560        570        580        590        600 
NSKRRRFSSK PVVLTEAQKQ LMICHLPQVL RLHLKRFRWS GRNNREKIGV HVGFEEILNM 

       610        620        630        640        650        660 
EPYCCRETLK SLRPECFIYD LSAVVMHHGK GFGSGHYTAY CYNSEGGFWV HCNDSKLSMC 

       670        680        690        700        710 
TMDEVCKAQA YILFYTQRVT ENGHSKLLPP ELLLGSQHPN EDADTSSNEI LS 

« Hide

References

« Hide 'large scale' references
[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-91.
Tissue: Testis.
[2]"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. expand/collapse author list , 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], VARIANT ALA-91.
Tissue: Testis.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
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], VARIANT ALA-91.
Tissue: Testis.
[5]"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.
[6]"Anaphase initiation is regulated by antagonistic ubiquitination and deubiquitination activities."
Stegmeier F., Rape M., Draviam V.M., Nalepa G., Sowa M.E., Ang X.L., McDonald E.R. III, Li M.Z., Hannon G.J., Sorger P.K., Kirschner M.W., Harper J.W., Elledge S.J.
Nature 446:876-881(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-282.
[7]"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: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF CYS-282.
[8]"A data integration approach to mapping OCT4 gene regulatory networks operative in embryonic stem cells and embryonal carcinoma cells."
Jung M., Peterson H., Chavez L., Kahlem P., Lehrach H., Vilo J., Adjaye J.
PLoS ONE 5:E10709-E10709(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[9]"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: TISSUE SPECIFICITY.
[10]"RNF20 and USP44 regulate stem cell differentiation by modulating H2B monoubiquitylation."
Fuchs G., Shema E., Vesterman R., Kotler E., Wolchinsky Z., Wilder S., Golomb L., Pribluda A., Zhang F., Haj-Yahya M., Feldmesser E., Brik A., Yu X., Hanna J., Aberdam D., Domany E., Oren M.
Mol. Cell 46:662-673(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit."
Visconti R., Palazzo L., Della Monica R., Grieco D.
Nat. Commun. 3:894-894(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-169; SER-239; THR-269 AND SER-401, DEPHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL136825 mRNA. Translation: CAB66759.1.
AK315697 mRNA. Translation: BAG38060.1.
AC018475 Genomic DNA. No translation available.
BC030704 mRNA. Translation: AAH30704.1.
RefSeqNP_001035862.1. NM_001042403.2.
NP_001265322.1. NM_001278393.1.
NP_115523.2. NM_032147.3.
UniGeneHs.646421.
Hs.710121.

3D structure databases

ProteinModelPortalQ9H0E7.
SMRQ9H0E7. Positions 29-86, 270-678.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123890. 12 interactions.
IntActQ9H0E7. 11 interactions.
MINTMINT-4719317.
STRING9606.ENSP00000258499.

Protein family/group databases

MEROPSC19.057.

PTM databases

PhosphoSiteQ9H0E7.

Polymorphism databases

DMDM300669621.

Proteomic databases

PaxDbQ9H0E7.
PRIDEQ9H0E7.

Protocols and materials databases

DNASU84101.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258499; ENSP00000258499; ENSG00000136014.
ENST00000393091; ENSP00000376806; ENSG00000136014.
ENST00000537435; ENSP00000442629; ENSG00000136014.
GeneID84101.
KEGGhsa:84101.
UCSCuc001teg.3. human.

Organism-specific databases

CTD84101.
GeneCardsGC12M095910.
H-InvDBHIX0010895.
HGNCHGNC:20064. USP44.
HPAHPA026543.
MIM610993. gene.
neXtProtNX_Q9H0E7.
PharmGKBPA134931457.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5077.
HOGENOMHOG000015084.
HOVERGENHBG018027.
InParanoidQ9H0E7.
KOK11834.
OMAAIKSQNY.
OrthoDBEOG7JX33S.
PhylomeDBQ9H0E7.
TreeFamTF315281.

Gene expression databases

ArrayExpressQ9H0E7.
BgeeQ9H0E7.
CleanExHS_USP44.
GenevestigatorQ9H0E7.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
SMARTSM00290. ZnF_UBP. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiUSP44.
GenomeRNAi84101.
NextBio73349.
PROQ9H0E7.
SOURCESearch...

Entry information

Entry nameUBP44_HUMAN
AccessionPrimary (citable) accession number: Q9H0E7
Secondary accession number(s): B2RDW3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: July 13, 2010
Last modified: March 19, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM