dbPTM

DNJA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DNJA1_HUMAN
UniProt AC	P31689
Protein Name	DnaJ homolog subfamily A member 1
Gene Name	DNAJA1
Organism	Homo sapiens (Human).
Sequence Length	397
Subcellular Localization	Membrane Lipid-anchor . Cytoplasm . Microsome. Nucleus . Cytoplasm, perinuclear region . Mitochondrion. Primarily associated with microsomes. A minor proportion is associated with mitochondria (By similarity). Primarily cytoplasmic. A minor proport
Protein Description	Co-chaperone for HSPA8/Hsc70. [PubMed: 10816573 Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro)]
Protein Sequence	MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MVKETTYYDV -----CCCEEEEEEH	48.31	-
6	Phosphorylation	--MVKETTYYDVLGV --CCCEEEEEEHHCC	22.60	29496907
7	Phosphorylation	-MVKETTYYDVLGVK -CCCEEEEEEHHCCC	12.70	25839225
8	Phosphorylation	MVKETTYYDVLGVKP CCCEEEEEEHHCCCC	9.48	29496907
14	Ubiquitination	YYDVLGVKPNATQEE EEEHHCCCCCCCHHH	30.65	21890473
14	Ubiquitination	YYDVLGVKPNATQEE EEEHHCCCCCCCHHH	30.65	21890473
14	Ubiquitination	YYDVLGVKPNATQEE EEEHHCCCCCCCHHH	30.65	21906983
23	Ubiquitination	NATQEELKKAYRKLA CCCHHHHHHHHHHHH	38.34	21906983
23	Acetylation	NATQEELKKAYRKLA CCCHHHHHHHHHHHH	38.34	23954790
24	Ubiquitination	ATQEELKKAYRKLAL CCHHHHHHHHHHHHH	64.37	-
28	Ubiquitination	ELKKAYRKLALKYHP HHHHHHHHHHHHHCC	25.99	-
32	Acetylation	AYRKLALKYHPDKNP HHHHHHHHHCCCCCC	35.59	23236377
32	Ubiquitination	AYRKLALKYHPDKNP HHHHHHHHHCCCCCC	35.59	21890473
32	Ubiquitination	AYRKLALKYHPDKNP HHHHHHHHHCCCCCC	35.59	21890473
32	Ubiquitination	AYRKLALKYHPDKNP HHHHHHHHHCCCCCC	35.59	21890473
33	Phosphorylation	YRKLALKYHPDKNPN HHHHHHHHCCCCCCC	21.31	28152594
37	Acetylation	ALKYHPDKNPNEGEK HHHHCCCCCCCCCHH	77.93	25953088
37	Ubiquitination	ALKYHPDKNPNEGEK HHHHCCCCCCCCCHH	77.93	21890473
37	Ubiquitination	ALKYHPDKNPNEGEK HHHHCCCCCCCCCHH	77.93	21890473
37	Ubiquitination	ALKYHPDKNPNEGEK HHHHCCCCCCCCCHH	77.93	21890473
44	Ubiquitination	KNPNEGEKFKQISQA CCCCCCHHHHHHHHH	69.58	21906983
44	Acetylation	KNPNEGEKFKQISQA CCCCCCHHHHHHHHH	69.58	23749302
46	Ubiquitination	PNEGEKFKQISQAYE CCCCHHHHHHHHHHH	58.76	21906983
46	Ubiquitination	PNEGEKFKQISQAYE CCCCHHHHHHHHHHH	58.76	21890473
46	Acetylation	PNEGEKFKQISQAYE CCCCHHHHHHHHHHH	58.76	26051181
46	Ubiquitination	PNEGEKFKQISQAYE CCCCHHHHHHHHHHH	58.76	21890473
49	Phosphorylation	GEKFKQISQAYEVLS CHHHHHHHHHHHHHH	13.28	28152594
52	Phosphorylation	FKQISQAYEVLSDAK HHHHHHHHHHHHHHH	10.03	28796482
56	Phosphorylation	SQAYEVLSDAKKREL HHHHHHHHHHHHHHH	40.47	28152594
59	Ubiquitination	YEVLSDAKKRELYDK HHHHHHHHHHHHHHC	58.30	21906983
59	Acetylation	YEVLSDAKKRELYDK HHHHHHHHHHHHHHC	58.30	25953088
59	Ubiquitination	YEVLSDAKKRELYDK HHHHHHHHHHHHHHC	58.30	21890473
59	Ubiquitination	YEVLSDAKKRELYDK HHHHHHHHHHHHHHC	58.30	21890473
60	Acetylation	EVLSDAKKRELYDKG HHHHHHHHHHHHHCC	53.47	25953088
60	Ubiquitination	EVLSDAKKRELYDKG HHHHHHHHHHHHHCC	53.47	21906983
64	Phosphorylation	DAKKRELYDKGGEQA HHHHHHHHHCCHHHH	15.74	28152594
66	Ubiquitination	KKRELYDKGGEQAIK HHHHHHHCCHHHHHH	56.08	19608861
66	Acetylation	KKRELYDKGGEQAIK HHHHHHHCCHHHHHH	56.08	19608861
66	Malonylation	KKRELYDKGGEQAIK HHHHHHHCCHHHHHH	56.08	26320211
73	Ubiquitination	KGGEQAIKEGGAGGG CCHHHHHHHCCCCCC	54.01	-
83	Phosphorylation	GAGGGFGSPMDIFDM CCCCCCCCHHHHHHH	18.13	25159151
85	Sulfoxidation	GGGFGSPMDIFDMFF CCCCCCHHHHHHHHC	7.08	28183972
105	Ubiquitination	MQRERRGKNVVHQLS HHHHHCCCCCEEEEE	44.77	21890473
105	Ubiquitination	MQRERRGKNVVHQLS HHHHHCCCCCEEEEE	44.77	21890473
105	Ubiquitination	MQRERRGKNVVHQLS HHHHHCCCCCEEEEE	44.77	21890473
112	Phosphorylation	KNVVHQLSVTLEDLY CCCEEEEECCHHHHH	13.39	25159151
114	Phosphorylation	VVHQLSVTLEDLYNG CEEEEECCHHHHHCC	22.51	28450419
119	Phosphorylation	SVTLEDLYNGATRKL ECCHHHHHCCHHHHH	24.71	27273156
123	Phosphorylation	EDLYNGATRKLALQK HHHHCCHHHHHHHHC	29.72	28442448
125	Ubiquitination	LYNGATRKLALQKNV HHCCHHHHHHHHCCE	33.48	-
130	Ubiquitination	TRKLALQKNVICDKC HHHHHHHCCEEEECC	54.77	-
130	Acetylation	TRKLALQKNVICDKC HHHHHHHCCEEEECC	54.77	25953088
136	Ubiquitination	QKNVICDKCEGRGGK HCCEEEECCCCCCCC	29.76	-
136	Acetylation	QKNVICDKCEGRGGK HCCEEEECCCCCCCC	29.76	23749302
136	Malonylation	QKNVICDKCEGRGGK HCCEEEECCCCCCCC	29.76	26320211
143	Ubiquitination	KCEGRGGKKGAVECC CCCCCCCCCCCEEEC	51.35	-
144	Ubiquitination	CEGRGGKKGAVECCP CCCCCCCCCCEEECC	56.21	21906983
156	Phosphorylation	CCPNCRGTGMQIRIH ECCCCCCCCCEEEEE	15.32	21406692
175	Phosphorylation	GMVQQIQSVCMECQG HHHHHHHHHHHHCCC	20.93	30576142
180	Glutathionylation	IQSVCMECQGHGERI HHHHHHHCCCCCCCC	2.04	22555962
188	Phosphorylation	QGHGERISPKDRCKS CCCCCCCCHHHHCHH	31.92	22617229
206	Ubiquitination	RKIVREKKILEVHID CHHEECEEEEEEEEC	48.01	-
214	Acetylation	ILEVHIDKGMKDGQK EEEEEECCCCCCCCE	61.37	25953088
214	Ubiquitination	ILEVHIDKGMKDGQK EEEEEECCCCCCCCE	61.37	-
217	Ubiquitination	VHIDKGMKDGQKITF EEECCCCCCCCEEEE	68.33	-
246	Ubiquitination	IIIVLDQKDHAVFTR EEEEEECCCCEEEEE	51.66	-
253	Methylation	KDHAVFTRRGEDLFM CCCEEEEECCCCEEE	32.89	-
278	Phosphorylation	CGFQKPISTLDNRTI HCCCCCCCCCCCCEE	31.29	20860994
284	Phosphorylation	ISTLDNRTIVITSHP CCCCCCCEEEEECCC	26.33	21406692
288	Phosphorylation	DNRTIVITSHPGQIV CCCEEEEECCCCCEE	15.30	21406692
289	Phosphorylation	NRTIVITSHPGQIVK CCEEEEECCCCCEEE	19.29	21406692
296	Ubiquitination	SHPGQIVKHGDIKCV CCCCCEEECCCEEEE	43.42	21906983
296	Ubiquitination	SHPGQIVKHGDIKCV CCCCCEEECCCEEEE	43.42	21890473
296	Acetylation	SHPGQIVKHGDIKCV CCCCCEEECCCEEEE	43.42	21466224
296	Ubiquitination	SHPGQIVKHGDIKCV CCCCCEEECCCEEEE	43.42	21890473
301	Ubiquitination	IVKHGDIKCVLNEGM EEECCCEEEEEECCC	24.03	-
301	Acetylation	IVKHGDIKCVLNEGM EEECCCEEEEEECCC	24.03	26051181
302	Glutathionylation	VKHGDIKCVLNEGMP EECCCEEEEEECCCC	4.26	22555962
311	Phosphorylation	LNEGMPIYRRPYEKG EECCCCCEECCCCCC	8.49	25147952
335	Phosphorylation	FPENGFLSPDKLSLL CCCCCCCCHHHHHHH	28.88	19664994
338	Acetylation	NGFLSPDKLSLLEKL CCCCCHHHHHHHHHH	43.27	25953088
338	Ubiquitination	NGFLSPDKLSLLEKL CCCCCHHHHHHHHHH	43.27	21890473
338	Ubiquitination	NGFLSPDKLSLLEKL CCCCCHHHHHHHHHH	43.27	21890473
338	Ubiquitination	NGFLSPDKLSLLEKL CCCCCHHHHHHHHHH	43.27	21890473
340	Phosphorylation	FLSPDKLSLLEKLLP CCCHHHHHHHHHHCC	36.33	30266825
344	Ubiquitination	DKLSLLEKLLPERKE HHHHHHHHHCCCCCC	56.12	21890473
344	Ubiquitination	DKLSLLEKLLPERKE HHHHHHHHHCCCCCC	56.12	21890473
344	Ubiquitination	DKLSLLEKLLPERKE HHHHHHHHHCCCCCC	56.12	21890473
350	Ubiquitination	EKLLPERKEVEETDE HHHCCCCCCCCCCCC	65.53	2190698
358	Sulfoxidation	EVEETDEMDQVELVD CCCCCCCCCEEEEEE	4.93	28465586
376	Phosphorylation	NQERRRHYNGEAYED CCHHHHHCCCCCCCC	24.05	21945579
381	Phosphorylation	RHYNGEAYEDDEHHP HHCCCCCCCCCCCCC	18.65	21945579
394	Methylation	HPRGGVQCQTS---- CCCCCCCCCCC----	4.41	-
394	Farnesylation	HPRGGVQCQTS---- CCCCCCCCCCC----	4.41	14752510
394	Farnesylation	HPRGGVQCQTS---- CCCCCCCCCCC----	4.41	14752510

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of DNJA1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DNJA1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DNJA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSP7C_HUMAN	HSPA8	physical	10075921
PTTG1_HUMAN	PTTG1	physical	9915854
ERG_HUMAN	ERG	physical	19940115
CFTR_HUMAN	CFTR	physical	11146634
GRP75_HUMAN	HSPA9	physical	22939629
TPP1_HUMAN	TPP1	physical	22939629
SAP_HUMAN	PSAP	physical	22939629
SPTN1_HUMAN	SPTAN1	physical	22939629
TRA2B_HUMAN	TRA2B	physical	22939629
KCNQ4_HUMAN	KCNQ4	physical	23431407
ZEP1_HUMAN	HIVEP1	physical	21988832
AIMP1_HUMAN	AIMP1	physical	22863883
MCA3_HUMAN	EEF1E1	physical	22863883
IF2G_HUMAN	EIF2S3	physical	22863883
IQGA1_HUMAN	IQGAP1	physical	22863883
SYQ_HUMAN	QARS	physical	22863883
RLA0_HUMAN	RPLP0	physical	22863883
HERC2_HUMAN	HERC2	physical	26186194
NUCG_HUMAN	ENDOG	physical	26186194
OSB11_HUMAN	OSBPL11	physical	26186194
OSBL9_HUMAN	OSBPL9	physical	26186194
PLD2_HUMAN	PLD2	physical	26186194
QCR8_HUMAN	UQCRQ	physical	26186194
ACADM_HUMAN	ACADM	physical	26344197
AHSA1_HUMAN	AHSA1	physical	26344197
CALX_HUMAN	CANX	physical	26344197
TCPB_HUMAN	CCT2	physical	26344197
TCPG_HUMAN	CCT3	physical	26344197
CLGN_HUMAN	CLGN	physical	26344197
FAF1_HUMAN	FAF1	physical	26344197
GRP78_HUMAN	HSPA5	physical	26344197
HSP7C_HUMAN	HSPA8	physical	26344197
GRP75_HUMAN	HSPA9	physical	26344197
HYOU1_HUMAN	HYOU1	physical	26344197
IMA3_HUMAN	KPNA4	physical	26344197
LDHB_HUMAN	LDHB	physical	26344197
GLU2B_HUMAN	PRKCSH	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PRS10_HUMAN	PSMC6	physical	26344197
PSD11_HUMAN	PSMD11	physical	26344197
QCR8_HUMAN	UQCRQ	physical	26344197
USO1_HUMAN	USO1	physical	26344197
RN207_HUMAN	RNF207	physical	25281747
P53_HUMAN	TP53	physical	27775703
NUCG_HUMAN	ENDOG	physical	28514442
OSBL9_HUMAN	OSBPL9	physical	28514442
OSB11_HUMAN	OSBPL11	physical	28514442
HERC2_HUMAN	HERC2	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DNJA1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44 AND LYS-66, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-340, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, AND MASSSPECTROMETRY.	15592455 [Abstract]
Prenylation
Reference	PubMed
"HSDJ, a human homolog of DnaJ, is farnesylated and is involved inprotein import into mitochondria."; Kanazawa M., Terada K., Kato S., Mori M.; J. Biochem. 121:890-895(1997). Cited for: CHARACTERIZATION, AND ISOPRENYLATION AT CYS-394.	9192730 [Abstract]