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Protein Page:
USP9Y (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
USP9Y May function as a ubiquitin-protein or polyubiquitin hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. May therefore play an important role regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin. Essential component of TGF-beta/BMP signaling cascade. Deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33. Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF- beta/BMP signaling cascade. Deubiqitination of SMAD4 by USP9X re- empowers its competence to mediate TGF-beta signaling. USP9Y is located in the 'azoospermia factor a' (AZFa) region on chromosome Y which is deleted in Sertoli cell- only syndrome. This is an infertility disorder in which no germ cells are visible in seminiferous tubules leading to azoospermia. However, AZFa deletions resulting in complete loss of USP9Y have also been found in normospermic men (PubMed:19246359). Defects in USP9Y may be a cause of spermatogenic failure Y-linked type 2 (SPGFY2). It is a disorder resulting in the absence (azoospermia) or reduction (oligozoospermia) of sperm in the semen, leading to male infertility. The role of USP9Y in spermatogenesis failure is uncertain. A 4-bp deletion in a splice-donor site, causing exon skipping and protein truncation has been observed in non-obstructive azoospermia (PubMed:10581029). However, complete USP9Y deletion has been detected in individuals with no spermatogenic defects (PubMed:19246359). Belongs to the peptidase C19 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.19.12; Protease; EC 3.1.2.15; Ubiquitin conjugating system; Ubiquitin-specific protease
Cellular Component: cytoplasm
Molecular Function: ubiquitin-specific protease activity; cysteine-type peptidase activity
Biological Process: BMP signaling pathway; ubiquitin-dependent protein catabolic process; protein deubiquitination; transforming growth factor beta receptor signaling pathway; spermatogenesis
Reference #:  O00507 (UniProtKB)
Alt. Names/Synonyms: Deubiquitinating enzyme FAF-Y; DFFRY; fat facets protein related, Y-linked; Fat facets protein-related, Y-linked; fat facets-like homolog; FLJ33043; Probable ubiquitin carboxyl-terminal hydrolase FAF-Y; ubiquitin specific peptidase 9, Y-linked; ubiquitin specific peptidase 9, Y-linked (fat facets-like, Drosophila); Ubiquitin thioesterase FAF-Y; ubiquitin thiolesterase FAF-Y; ubiquitin-specific processing protease FAF-Y; Ubiquitin-specific protease 9, Y chromosome; Ubiquitin-specific-processing protease FAF-Y; USP10; USP9Y
Gene Symbols: USP9Y
Molecular weight: 291,077 Da
Basal Isoelectric point: 5.56  Predict pI for various phosphorylation states
Select Structure to View Below

USP9Y

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 A102 LEVLLEAAIDLSVKG
0 1 K300-ac EELKKEAkNEAkNDA
0 1 K304-ac KEAkNEAkNDALSMI
0 2 K316-ac SMIIKSLkNLASRIS
0 1 Y861 VLTVIKEYINECDSD
0 1 Y869-p INECDSDyHKERMIL
0 1 S879-p ERMILPMsRAFRGKH
0 1 K931 IKANVAHKKIELFVG
0 1 S1030-p WQVADLGsNLNMPPL
0 1 S1121-p FQVHFLKsGGLPLVL
0 1 S1129-p GGLPLVLsMLIRNNF
0 1 S1219-p ECVLRNEsILLAQEI
0 1 S1227-p ILLAQEIsNEAsRYM
0 1 S1231-p QEIsNEAsRYMPDIC
0 1 K1328-ub LLLHCPSkTVRQLAQ
0 1 T1361 FFITLLFTILGSTAR
0 2 K1813-ub WERECAIkFNDYFEF
0 2 Y1817 CAIkFNDYFEFPREL
0 1 Y1829-p RELDMGPytVAGVAN
0 1 T1830-p ELDMGPytVAGVANL
0 2 S1985-p RPHQIIMsPAIERSV
0 2 N2163 HLLRATLNLLRREVS
0 1 T2205-p LKLNVPAtFMLVSLD
0 3 K2220-ub EGPGPPIkYQYAELG
  mouse

 
S101-p LEVLLETsIDLTKKG
K299 EELKKETKTEVKNDT
K303 KETKTEVKNDTISMI
K315 SMIIKFLKNLASRIP
Y860-p ILTVLREyISEYDSD
Y868 ISEYDSDYHEERMIL
S878 ERMILPMSRAFRGKH
T930-p MNVNVAHtKIELFIG
S1030 WQVADLGSMLTVPTL
S1121 FQYHFLKSGGLPLVL
S1129 GGLPLVLSMLIQNNF
S1219 ECMLRNVSVHLAQQI
S1227 VHLAQQISGLASRYI
S1231 QQISGLASRYIPDIC
K1328 LLLYCPSKTVRQLAQ
T1361-p FFITLLFtILGGAAN
K1813-ub WERECAIkFNDyFEF
Y1817-p CAIkFNDyFEFPREL
Y1829 RELDMEPYTVAGATK
T1830 ELDMEPYTVAGATKL
S1984 TRPHQIMSPAIERSV
S2166-p HLLKAVLsLLRREVS
T2208 LKLNVPATFMLVSLD
K2223 EGPGPPVKYQYAELS
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