D2HBJ8 (UBP44_AILME) 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
ORF Names:	PANDA_007904

Organism

Ailuropoda melanoleuca (Giant panda) [Reference proteome]

Taxonomic identifier

9646 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Ursidae › Ailuropoda

Protein attributes

Sequence length	711 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity.
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 By similarity. Note: Peaks in interphase, with relatively low levels maintained throughout mitosis By similarity.
Post-translational modification	Dephosphorylated by CTDP1 By similarity. Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome By similarity.
Sequence similarities	Belongs to the peptidase C19 family. USP44 subfamily. Contains 1 UBP-type zinc finger.

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 sequence or structural similarity. Source: UniProtKB 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 sequence or structural similarity. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB protein deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitotic cell cycle spindle assembly checkpoint Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ubiquitin thiolesterase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB 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_0000395810
Regions
	Zinc finger	27 – 88	62	UBP-type
Sites
	Active site	281	1	Nucleophile By similarity
	Active site	635	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	D2HBJ8 [UniParc]. Last modified February 9, 2010. Version 1. Checksum: 00C0350EA2E949E1	FASTA	711	81,364
	10 20 30 40 50 60 MLTMDKCKHI GQLRLAQDHS ILNPQKWHCV DCNTTESIWA CLSCSHVACG RYIEEHALKH 70 80 90 100 110 120 FQESSHPVAL EVNEMYVFCY LCDDYVLNDN ATGDLKLLRS MLSAIKSQNY QCTTRSGRVL 130 140 150 160 170 180 RSMGTSDDTY YLHDGTQSLL QNEDQMYTAL WHRRRILMSK IFRTWFEQSP TGRKRQEEQF 190 200 210 220 230 240 QEKIAKREVK KRRQELEYQV KAELETIHPR KSLRLQGLAQ STTVEIVPVQ VPLQTPASPA 250 260 270 280 290 300 KDKVVSTSED VRLKKASDSS GKRRPIVTPG VTGLRNLGNT CYMNSVLQVL SHLLIFRQCF 310 320 330 340 350 360 LKLDLNQWLA VTASDKTRSP YKHPSITDTV YQMNECQETD TGSAPSRHPS LSLGLSGGAS 370 380 390 400 410 420 KSRKMELIQP REPSSQYISL CHELHTLFQV MWSGKWALVS PFAMLHSVWR LIPAFRGYAQ 430 440 450 460 470 480 QDAQEFLCEL LDKIQHELET TGTRLPALIP TSQRKLIKQV LNVVNNIFHG QLLSQVTCLA 490 500 510 520 530 540 CDNKSNTIEP FWDLSLEFPE RYQCNGKDIA SQPCRVTEML AKFTETEALE GKIYVCDHCN 550 560 570 580 590 600 SKRRRFSSKS VVLTEAQKQL MICHLPQVLR LHLKRFRWSG RNNREKIGVH VGFEEILNME 610 620 630 640 650 660 PYCCRESLKS LRPECFIYDL SAVVMHHGKG FGSGHYTAYC YNSEGGFWVH CNDSKLSMCT 670 680 690 700 710 MDEVCKAQAY ILFYTQRVTE NGHSKLLPPE LLSGSQHPNE EADTSSNEIL S

References

[1]

"The sequence and de novo assembly of the giant panda genome." Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J. , Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J., Wang J. Nature 463:311-317(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	GL192660 Genomic DNA. Translation: EFB15980.1.
RefSeq	XP_002919284.1. XM_002919238.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSAMET00000002387; ENSAMEP00000002292; ENSAMEG00000002189.
GeneID	100470180.
KEGG	aml:100470180.
Organism-specific databases
CTD	84101.
Phylogenomic databases
GeneTree	ENSGT00690000101718.
HOGENOM	HOG000015084.
KO	K11834.
OMA	AIKSQNY.
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]
SMART	SM00290. ZnF_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...

Entry information

Entry name

UBP44_AILME

Accession

Primary (citable) accession number: D2HBJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 13, 2010
Last sequence update:	February 9, 2010
Last modified:	April 3, 2013
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program