DNAJA2 (human)

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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
g	O-GlcNAc
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: metal ion binding; heat shock protein binding; unfolded protein binding; glycoprotein 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

Modification Sites and Domains

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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	K33-a	kAYRKLAkEYHPDkN
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	1	K121-a	EDMMHPLkVSLEDLY
0	1	Y128	kVSLEDLYNGkTTkL
0	1	K131-a	LEDLYNGkTTkLQLS
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-m2	VVKYPPGkVIEPGCV
0	1	K302	VVKYPPGKVIEPGCV
0	1	Y320	RGEGMPQYRNPFEkG
0	1	K326-u	QYRNPFEkGDLyIKF
0	1	Y330-p	PFEkGDLyIKFDVQF
0	2	Y391-p	GGQRREAyNDssDEE
0	6	S394-p	RREAyNDssDEESSS
0	6	S395-p	REAyNDssDEESSSH

	mouse

K33	KAYRKLAKEYHPDkN
K25	GASENELKKAYRKLA
K26	ASENELKKAYRKLAk
K33-u	KAYRKLAkEYHPDkN
K39-u	AkEYHPDkNPNAGDk
K46-u	kNPNAGDkFKEISFA
K62	EVLSNPEKRELYDRY
S78	EQGLREGSGGGGGMD
K121	EDMMHPLKVSLEDLy
Y128-p	KVSLEDLyNGkTTkL
K131	LEDLyNGKTTkLQLS
K131-u	LEDLyNGkTTkLQLS
K134-u	LyNGkTTkLQLSKNV
S144	LSKNVLCSACsGQGG
S147-p	NVLCSACsGQGGkSG
K152-u	ACsGQGGkSGAVQkC
K158-u	GkSGAVQkCSACRGR
K199	EGEVINEKDRCKKCE
K255-u	IVLLLQEkEHEVFQR
K302	VVKYPPGKVIEPGCV
K302-u	VVKYPPGkVIEPGCV
Y320	RGEGMPQYRNPFEKG
K326	QYRNPFEKGDLYIKF
Y330	PFEKGDLYIKFDVQF
Y391	GGQRREAYNDssDEE
S394-p	RREAYNDssDEESSS
S395-p	REAYNDssDEESSSH

	rat

K33	KAYRKLAKEYHPDKN
K25	GASENELKKAYRKLA
K26	ASENELKKAYRKLAK
K33	KAYRKLAKEYHPDKN
K39	AKEYHPDKNPNAGDK
K46	KNPNAGDKFKEISFA
K62	EVLSNPEKRELYDRY
S78	EQGLREGSGGGGGMD
K121	EDMMHPLKVSLEDLY
Y128	KVSLEDLYNGKTTKL
K131	LEDLYNGKTTKLQLS
K131	LEDLYNGKTTKLQLS
K134	LYNGKTTKLQLSKNV
S144	LSKNVLCSACSGQGG
S147	NVLCSACSGQGGKSG
K152	ACSGQGGKSGAVQKC
K158	GKSGAVQKCSACRGR
K199	EGEVINEKDRCKKCE
K255	IVLFVQEKEHEVFQR
K302	VVKYPPGKVIEPGCV
K302	VVKYPPGKVIEPGCV
Y320-p	RGEGMPQyRNPFEKG
K326	QyRNPFEKGDLYIKF
Y330	PFEKGDLYIKFDVQF
Y391	GGQRREAYNDSSDEE
S394	RREAYNDSSDEESSS
S395	REAYNDSSDEESSSH

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