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Protein Page:
DNAJA2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
DNAJA2 Co-chaperone of Hsc70. Note: This description may include information from UniProtKB.
Protein type: Cell cycle regulation; Chaperone
Cellular Component: membrane
Molecular Function: protein binding; metal ion binding; heat shock protein binding; unfolded protein binding; ATP binding
Biological Process: protein folding; response to heat; positive regulation of cell proliferation
Reference #:  O60884 (UniProtKB)
Alt. Names/Synonyms: cell cycle progression 3 protein; Cell cycle progression restoration gene 3 protein; CPR3; Dj3; DJA2; DNAJ; DnaJ (Hsp40) homolog, subfamily A, member 2; DnaJ homolog subfamily A member 2; DNAJA2; Dnj3; DNJA2; HIRA interacting protein 4; HIRA-interacting protein 4; HIRIP4; PRO3015; RDJ2; Renal carcinoma antigen NY-REN-14
Gene Symbols: DNAJA2
Molecular weight: 45,746 Da
Basal Isoelectric point: 6.06  Predict pI for various phosphorylation states
Select Structure to View Below

DNAJA2

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 2 K25-u GASENELkkAYRKLA
0 1 K26-u ASENELkkAYRKLAK
0 1 K33 kAYRKLAKEYHPDkN
0 2 K39-u AKEYHPDkNPNAGDK
0 1 K46 kNPNAGDKFKEISFA
0 2 K62-u EVLSNPEkRELYDRY
0 2 S78-p EQGLREGsGGGGGMD
0 2 K131-u LEDLYNGkTTkLQLS
0 9 K134-u LYNGkTTkLQLSKNV
0 1 S144-p LSKNVLCsACSGQGG
0 1 S147 NVLCsACSGQGGkSG
0 37 K152-u ACSGQGGkSGAVQkC
0 14 K158-u GkSGAVQkCSACRGR
0 1 K199-u EGEVINEkDRCKKCE
0 3 K255-u IVLLLQEkEHEVFQR
0 1 K302 VVKYPPGKVIEPGCV
0 1 K326-u QYRNPFEkGDLYIKF
0 2 Y391-p GGQRREAyNDssDEE
0 6 S394-p RREAyNDssDEESSS
0 6 S395-p REAyNDssDEESSSH
  mouse

 
K25 GASENELKKAYRKLA
K26 ASENELKKAYRKLAk
K33-u KAYRKLAkEYHPDkN
K39-u AkEYHPDkNPNAGDk
K46-u kNPNAGDkFKEISFA
K62 EVLSNPEKRELYDRY
S78 EQGLREGSGGGGGMD
K131-u LEDLYNGkTTkLQLS
K134-u LYNGkTTkLQLSKNV
S144 LSKNVLCSACsGQGG
S147-p NVLCSACsGQGGkSG
K152-u ACsGQGGkSGAVQkC
K158-u GkSGAVQkCSACRGR
K199 EGEVINEKDRCKKCE
K255-u IVLLLQEkEHEVFQR
K302-u VVKYPPGkVIEPGCV
K326 QYRNPFEKGDLYIKF
Y391 GGQRREAYNDssDEE
S394-p RREAYNDssDEESSS
S395-p REAYNDssDEESSSH
  rat

 
K25 GASENELKKAYRKLA
K26 ASENELKKAYRKLAK
K33 KAYRKLAKEYHPDKN
K39 AKEYHPDKNPNAGDK
K46 KNPNAGDKFKEISFA
K62 EVLSNPEKRELYDRY
S78 EQGLREGSGGGGGMD
K131 LEDLYNGKTTKLQLS
K134 LYNGKTTKLQLSKNV
S144 LSKNVLCSACSGQGG
S147 NVLCSACSGQGGKSG
K152 ACSGQGGKSGAVQKC
K158 GKSGAVQKCSACRGR
K199 EGEVINEKDRCKKCE
K255 IVLFVQEKEHEVFQR
K302 VVKYPPGKVIEPGCV
K326 QYRNPFEKGDLYIKF
Y391 GGQRREAYNDSSDEE
S394 RREAYNDSSDEESSS
S395 REAYNDSSDEESSSH
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