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Q9H0E7

- UBP44_HUMAN

UniProt

Q9H0E7 - UBP44_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 44

Gene

USP44

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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.2 Publications

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).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei282 – 2821Nucleophile
Active sitei636 – 6361Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri27 – 8862UBP-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
  2. negative regulation of mitotic anaphase-promoting complex activity Source: UniProtKB
  3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  4. protein deubiquitination Source: UniProtKB
  5. regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
  6. regulation of spindle checkpoint Source: UniProtKB
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:20064. USP44.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi282 – 2821C → S or A: Abolishes deubiquitinase activity. 2 Publications

Organism-specific databases

PharmGKBiPA134931457.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 712712Ubiquitin carboxyl-terminal hydrolase 44PRO_0000080673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei169 – 1691Phosphoserine1 Publication
Modified residuei239 – 2391Phosphoserine1 Publication
Modified residuei269 – 2691Phosphothreonine1 Publication
Modified residuei401 – 4011Phosphoserine1 Publication

Post-translational modificationi

Dephosphorylated by CTDP1.
Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9H0E7.
PRIDEiQ9H0E7.

PTM databases

PhosphoSiteiQ9H0E7.

Expressioni

Tissue specificityi

Expressed in testis. Expressed at high levels in T-cell acute lymphoblastic leukemia.2 Publications

Developmental stagei

Elevated in mitosis; levels increase in mitotic cells and rapidly decrease once cells have completed chromosome attachment and exit from mitosis.1 Publication

Inductioni

Transcriptionally regulated by POU5F1/OCT4 in embryonic stem cells and embryonal carcinoma cells.1 Publication

Gene expression databases

BgeeiQ9H0E7.
CleanExiHS_USP44.
ExpressionAtlasiQ9H0E7. baseline and differential.
GenevestigatoriQ9H0E7.

Organism-specific databases

HPAiHPA026543.

Interactioni

Protein-protein interaction databases

BioGridi123890. 12 interactions.
IntActiQ9H0E7. 11 interactions.
MINTiMINT-4719317.
STRINGi9606.ENSP00000258499.

Structurei

3D structure databases

ProteinModelPortaliQ9H0E7.
SMRiQ9H0E7. Positions 29-86, 268-678.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini273 – 678406USPAdd
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 fingeri27 – 8862UBP-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5077.
GeneTreeiENSGT00760000119203.
HOGENOMiHOG000015084.
HOVERGENiHBG018027.
InParanoidiQ9H0E7.
KOiK11834.
OMAiAIKSQNY.
OrthoDBiEOG7JX33S.
PhylomeDBiQ9H0E7.
TreeFamiTF315281.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
SMARTiSM00290. ZnF_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.

Q9H0E7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLAMDTCKHV GQLQLAQDHS SLNPQKWHCV DCNTTESIWA CLSCSHVACG
60 70 80 90 100
RYIEEHALKH FQESSHPVAL EVNEMYVFCY LCDDYVLNDN TTGDLKLLRR
110 120 130 140 150
TLSAIKSQNY HCTTRSGRFL RSMGTGDDSY FLHDGAQSLL QSEDQLYTAL
160 170 180 190 200
WHRRRILMGK IFRTWFEQSP IGRKKQEEPF QEKIVVKREV KKRRQELEYQ
210 220 230 240 250
VKAELESMPP RKSLRLQGLA QSTIIEIVSV QVPAQTPASP AKDKVLSTSE
260 270 280 290 300
NEISQKVSDS SVKRRPIVTP GVTGLRNLGN TCYMNSVLQV LSHLLIFRQC
310 320 330 340 350
FLKLDLNQWL AMTASEKTRS CKHPPVTDTV VYQMNECQEK DTGFVCSRQS
360 370 380 390 400
SLSSGLSGGA SKGRKMELIQ PKEPTSQYIS LCHELHTLFQ VMWSGKWALV
410 420 430 440 450
SPFAMLHSVW RLIPAFRGYA QQDAQEFLCE LLDKIQRELE TTGTSLPALI
460 470 480 490 500
PTSQRKLIKQ VLNVVNNIFH GQLLSQVTCL ACDNKSNTIE PFWDLSLEFP
510 520 530 540 550
ERYQCSGKDI ASQPCLVTEM LAKFTETEAL EGKIYVCDQC NSKRRRFSSK
560 570 580 590 600
PVVLTEAQKQ LMICHLPQVL RLHLKRFRWS GRNNREKIGV HVGFEEILNM
610 620 630 640 650
EPYCCRETLK SLRPECFIYD LSAVVMHHGK GFGSGHYTAY CYNSEGGFWV
660 670 680 690 700
HCNDSKLSMC TMDEVCKAQA YILFYTQRVT ENGHSKLLPP ELLLGSQHPN
710
EDADTSSNEI LS
Length:712
Mass (Da):81,185
Last modified:July 13, 2010 - v2
Checksum:iA8211DFAD78EE731
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911T → A.3 Publications
Corresponds to variant rs3812813 [ dbSNP | Ensembl ].
VAR_017125
Natural varianti316 – 3161E → Q.
Corresponds to variant rs7305024 [ dbSNP | Ensembl ].
VAR_057043
Natural varianti348 – 3481R → G.
Corresponds to variant rs7135642 [ dbSNP | Ensembl ].
VAR_057044

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136825 mRNA. Translation: CAB66759.1.
AK315697 mRNA. Translation: BAG38060.1.
AC018475 Genomic DNA. No translation available.
BC030704 mRNA. Translation: AAH30704.1.
CCDSiCCDS9053.1.
RefSeqiNP_001035862.1. NM_001042403.2.
NP_001265322.1. NM_001278393.1.
NP_115523.2. NM_032147.4.
UniGeneiHs.646421.
Hs.710121.

Genome annotation databases

EnsembliENST00000258499; ENSP00000258499; ENSG00000136014.
ENST00000393091; ENSP00000376806; ENSG00000136014.
ENST00000537435; ENSP00000442629; ENSG00000136014.
GeneIDi84101.
KEGGihsa:84101.
UCSCiuc001teg.3. human.

Polymorphism databases

DMDMi300669621.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136825 mRNA. Translation: CAB66759.1 .
AK315697 mRNA. Translation: BAG38060.1 .
AC018475 Genomic DNA. No translation available.
BC030704 mRNA. Translation: AAH30704.1 .
CCDSi CCDS9053.1.
RefSeqi NP_001035862.1. NM_001042403.2.
NP_001265322.1. NM_001278393.1.
NP_115523.2. NM_032147.4.
UniGenei Hs.646421.
Hs.710121.

3D structure databases

ProteinModelPortali Q9H0E7.
SMRi Q9H0E7. Positions 29-86, 268-678.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123890. 12 interactions.
IntActi Q9H0E7. 11 interactions.
MINTi MINT-4719317.
STRINGi 9606.ENSP00000258499.

Protein family/group databases

MEROPSi C19.057.

PTM databases

PhosphoSitei Q9H0E7.

Polymorphism databases

DMDMi 300669621.

Proteomic databases

PaxDbi Q9H0E7.
PRIDEi Q9H0E7.

Protocols and materials databases

DNASUi 84101.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258499 ; ENSP00000258499 ; ENSG00000136014 .
ENST00000393091 ; ENSP00000376806 ; ENSG00000136014 .
ENST00000537435 ; ENSP00000442629 ; ENSG00000136014 .
GeneIDi 84101.
KEGGi hsa:84101.
UCSCi uc001teg.3. human.

Organism-specific databases

CTDi 84101.
GeneCardsi GC12M095910.
H-InvDB HIX0010895.
HGNCi HGNC:20064. USP44.
HPAi HPA026543.
MIMi 610993. gene.
neXtProti NX_Q9H0E7.
PharmGKBi PA134931457.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5077.
GeneTreei ENSGT00760000119203.
HOGENOMi HOG000015084.
HOVERGENi HBG018027.
InParanoidi Q9H0E7.
KOi K11834.
OMAi AIKSQNY.
OrthoDBi EOG7JX33S.
PhylomeDBi Q9H0E7.
TreeFami TF315281.

Miscellaneous databases

ChiTaRSi USP44. human.
GeneWikii USP44.
GenomeRNAii 84101.
NextBioi 73349.
PROi Q9H0E7.
SOURCEi Search...

Gene expression databases

Bgeei Q9H0E7.
CleanExi HS_USP44.
ExpressionAtlasi Q9H0E7. baseline and differential.
Genevestigatori Q9H0E7.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view ]
SMARTi SM00290. ZnF_UBP. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiUBP44_HUMAN
AccessioniPrimary (citable) accession number: Q9H0E7
Secondary accession number(s): B2RDW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: July 13, 2010
Last modified: November 26, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3