dbPTM

CRYAA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CRYAA_HUMAN
UniProt AC	P02489
Protein Name	Alpha-crystallin A chain
Gene Name	CRYAA
Organism	Homo sapiens (Human).
Sequence Length	173
Subcellular Localization	Cytoplasm . Nucleus . Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
Protein Description	Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions..
Protein Sequence	MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDVTIQHP -------CCCEECCC	9.37	817940
6	Deamidated glutamine	--MDVTIQHPWFKRT --CCCEECCCCHHHC	27.50	-
6	Deamidation	--MDVTIQHPWFKRT --CCCEECCCCHHHC	27.50	9068373
11	Methylation	TIQHPWFKRTLGPFY EECCCCHHHCCCCCC	40.37	17022627
13	Phosphorylation	QHPWFKRTLGPFYPS CCCCHHHCCCCCCCH	36.34	22817900
18	Phosphorylation	KRTLGPFYPSRLFDQ HHCCCCCCCHHHHHH	11.93	-
20	Phosphorylation	TLGPFYPSRLFDQFF CCCCCCCHHHHHHHH	30.18	-
21	Methylation	LGPFYPSRLFDQFFG CCCCCCHHHHHHHHC	34.56	-
45	Phosphorylation	PFLSSTISPYYRQSL HHHHHCCCHHHHHHH	13.62	9068373
48	Phosphorylation	SSTISPYYRQSLFRT HHCCCHHHHHHHHHH	12.93	-
50	Deamidated glutamine	TISPYYRQSLFRTVL CCCHHHHHHHHHHHH	28.50	-
50	Deamidation	TISPYYRQSLFRTVL CCCHHHHHHHHHHHH	28.50	9068373
55	Phosphorylation	YRQSLFRTVLDSGIS HHHHHHHHHHHHCHH	20.34	24702127
70	Acetylation	EVRSDRDKFVIFLDV HHHCCCCEEEEEEEE	42.28	22120592
78	Acetylation	FVIFLDVKHFSPEDL EEEEEEECCCCHHHC	38.30	12060738
88	Acetylation	SPEDLTVKVQDDFVE CHHHCEEEEECCEEE	29.01	12060738
88	Methylation	SPEDLTVKVQDDFVE CHHHCEEEEECCEEE	29.01	23161681
90	Deamidated glutamine	EDLTVKVQDDFVEIH HHCEEEEECCEEEEC	38.55	-
90	Deamidation	EDLTVKVQDDFVEIH HHCEEEEECCEEEEC	38.55	9068373
99	Acetylation	DFVEIHGKHNERQDD CEEEECCCCCCCCCC	29.15	22120592
101	Deamidated asparagine	VEIHGKHNERQDDHG EEECCCCCCCCCCCC	50.02	-
101	Deamidation	VEIHGKHNERQDDHG EEECCCCCCCCCCCC	50.02	9068373
111	Phosphorylation	QDDHGYISREFHRRY CCCCCEECHHHHHHH	19.78	24425749
122	Phosphorylation	HRRYRLPSNVDQSAL HHHHCCCCCCCCCHH	54.82	9068373
123	Deamidation	RRYRLPSNVDQSALS HHHCCCCCCCCCHHH	39.17	18754677
123	Deamidated asparagine	RRYRLPSNVDQSALS HHHCCCCCCCCCHHH	39.17	-
131	Glutathionylation	VDQSALSCSLSADGM CCCCHHHCEECCCCC	5.02	22833525
140	Phosphorylation	LSADGMLTFCGPKIQ ECCCCCEEECCCEEC	14.16	22817900
142	Glutathionylation	ADGMLTFCGPKIQTG CCCCEEECCCEECCC	8.43	22833525
145	Acetylation	MLTFCGPKIQTGLDA CEEECCCEECCCCCC	32.50	12060738
147	Deamidated glutamine	TFCGPKIQTGLDATH EECCCEECCCCCCHH	35.32	-
147	Deamidation	TFCGPKIQTGLDATH EECCCEECCCCCCHH	35.32	9068373
148	Phosphorylation	FCGPKIQTGLDATHA ECCCEECCCCCCHHH	43.09	-
162	O-linked_Glycosylation	AERAIPVSREEKPTS HHHCCCCCCCCCCCC	28.72	UniProtKB CARBOHYD

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 CRYAA_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
70	K	Acetylation	9655350
Acetylation at Lys-70 may increase chaperone activity.
101	N	Amidation	8175657
Deamidation of Asn-101 in lens occurs mostly during the first 30 years of age, followed by a small additional amount of deamidation (approximately 5%) during the next approximately 38 years, resulting in a maximum of approximately 50% deamidation during the lifetime of the individual.
122	S	Phosphorylation	8175657
Phosphorylation on Ser-122 seems to be developmentally regulated.

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 CRYAA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CRYAB_HUMAN	CRYAB	physical	11700327
CRBB2_HUMAN	CRYBB2	physical	11700327
CRGC_HUMAN	CRYGC	physical	11700327
CRYAA_HUMAN	CRYAA	physical	11700327
HSPB1_HUMAN	HSPB1	physical	11700327
CRYAA_HUMAN	CRYAA	physical	17724207
CRGC_HUMAN	CRYGC	physical	12601044
CRYAA_HUMAN	CRYAA	physical	12601044
CRYAB_HUMAN	CRYAB	physical	12601044
CRBB2_HUMAN	CRYBB2	physical	12601044
CRGD_HUMAN	CRYGD	physical	12601044
HSPB1_HUMAN	HSPB1	physical	12601044
HSPB2_HUMAN	HSPB2	physical	12601044
CRYAB_HUMAN	CRYAB	physical	18401461
CRYAB_HUMAN	CRYAB	physical	22427585
CRYAA_HUMAN	CRYAA	physical	22427585
B2CL1_HUMAN	BCL2L1	physical	14752512
BAX_HUMAN	BAX	physical	14752512
CRBA1_HUMAN	CRYBA1	physical	19401464
CRYAA_HUMAN	CRYAA	physical	18639655
CRYAB_HUMAN	CRYAB	physical	18639655
CRYAA_HUMAN	CRYAA	physical	25416956
CRYAB_HUMAN	CRYAB	physical	25416956
SDCB1_HUMAN	SDCBP	physical	25416956
GORS2_HUMAN	GORASP2	physical	25416956
SPG21_HUMAN	SPG21	physical	25416956
NTAQ1_HUMAN	WDYHV1	physical	25416956
CRYAA_HUMAN	CRYAA	physical	22085609
CRYAB_HUMAN	CRYAB	physical	22085609
CRBA1_HUMAN	CRYBA1	physical	26657544
CRYAB_HUMAN	CRYAB	physical	26657544

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
OMIM Disease
0000269\|PubMed	Note=Alpha-crystallin A 1-172 is found at nearly twofold higher levels in diabetic lenses than in age-matched control lenses. {ECO
604219
Kegg Drug
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CRYAA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Acetylation of alphaA-crystallin in the human lens: effects onstructure and chaperone function."; Nagaraj R.H., Nahomi R.B., Shanthakumar S., Linetsky M.,Padmanabha S., Pasupuleti N., Wang B., Santhoshkumar P., Panda A.K.,Biswas A.; Biochim. Biophys. Acta 1822:120-129(2012). Cited for: FUNCTION, AND ACETYLATION AT LYS-70 AND LYS-99.	22120592 [Abstract]
"Shotgun identification of protein modifications from proteincomplexes and lens tissue."; MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M.,Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I.,Yates J.R. III; Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-45; SER-122 ANDTHR-140, ACETYLATION AT LYS-70; LYS-78; LYS-88 AND LYS-145,METHYLATION AT ARG-21 AND LYS-88, SUSCEPTIBILITY TO OXIDATION, ANDMASS SPECTROMETRY.	12060738 [Abstract]
"In vivo acetylation identified at lysine 70 of human lens alphaA-crystallin."; Lin P.P., Barry R.C., Smith D.L., Smith J.B.; Protein Sci. 7:1451-1457(1998). Cited for: PROTEOLYTIC PROCESSING OF C-TERMINAL, ACETYLATION AT LYS-70,PHOSPHORYLATION, DEAMIDATION AT ASN-101, AND MASS SPECTROMETRY.	9655350 [Abstract]
Deamidation
Reference	PubMed
"In vivo acetylation identified at lysine 70 of human lens alphaA-crystallin."; Lin P.P., Barry R.C., Smith D.L., Smith J.B.; Protein Sci. 7:1451-1457(1998). Cited for: PROTEOLYTIC PROCESSING OF C-TERMINAL, ACETYLATION AT LYS-70,PHOSPHORYLATION, DEAMIDATION AT ASN-101, AND MASS SPECTROMETRY.	9655350 [Abstract]
"Quantitation of asparagine-101 deamidation from alpha-A crystallinduring aging of the human lens."; Takemoto L.J.; Curr. Eye Res. 17:247-250(1998). Cited for: DEAMIDATION AT ASN-101.	9543632 [Abstract]
"Post-translational modifications of water-soluble human lenscrystallins from young adults."; Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L.,Smith J.B.; J. Biol. Chem. 269:12494-12502(1994). Cited for: PHOSPHORYLATION AT SER-122, DISULFIDE BOND, PROTEOLYTIC PROCESSING OFC-TERMINAL, DEAMIDATION AT ASN-101, AND MASS SPECTROMETRY.	8175657 [Abstract]
Methylation
Reference	PubMed
"Shotgun identification of protein modifications from proteincomplexes and lens tissue."; MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M.,Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I.,Yates J.R. III; Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-45; SER-122 ANDTHR-140, ACETYLATION AT LYS-70; LYS-78; LYS-88 AND LYS-145,METHYLATION AT ARG-21 AND LYS-88, SUSCEPTIBILITY TO OXIDATION, ANDMASS SPECTROMETRY.	12060738 [Abstract]
Phosphorylation
Reference	PubMed
"Shotgun identification of protein modifications from proteincomplexes and lens tissue."; MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M.,Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I.,Yates J.R. III; Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-45; SER-122 ANDTHR-140, ACETYLATION AT LYS-70; LYS-78; LYS-88 AND LYS-145,METHYLATION AT ARG-21 AND LYS-88, SUSCEPTIBILITY TO OXIDATION, ANDMASS SPECTROMETRY.	12060738 [Abstract]
"Differential phosphorylation of alpha-A crystallin in human lens ofdifferent age."; Takemoto L.J.; Exp. Eye Res. 62:499-504(1996). Cited for: PHOSPHORYLATION AT SER-122.	8759518 [Abstract]
"Post-translational modifications of water-soluble human lenscrystallins from young adults."; Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L.,Smith J.B.; J. Biol. Chem. 269:12494-12502(1994). Cited for: PHOSPHORYLATION AT SER-122, DISULFIDE BOND, PROTEOLYTIC PROCESSING OFC-TERMINAL, DEAMIDATION AT ASN-101, AND MASS SPECTROMETRY.	8175657 [Abstract]

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