dbPTM

CRYAB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CRYAB_HUMAN
UniProt AC	P02511
Protein Name	Alpha-crystallin B chain
Gene Name	CRYAB
Organism	Homo sapiens (Human).
Sequence Length	175
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 (PubMed:19464326). Localizes at the Z-bands and the intercalated disk in cardiomyocytes (Pub
Protein Description	May contribute 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	MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDIAIHHP -------CCCEECCC	8.31	838078
19	Phosphorylation	RPFFPFHSPSRLFDQ CCCCCCCCHHHHHHH	25.58	26055452
21	Phosphorylation	FFPFHSPSRLFDQFF CCCCCCHHHHHHHHH	44.63	21082442
22	Methylation	FPFHSPSRLFDQFFG CCCCCHHHHHHHHHH	42.64	12060738
43	Phosphorylation	DLFPTSTSLSPFYLR CCCCCCCCCCCCCCC	26.98	22817900
45	Phosphorylation	FPTSTSLSPFYLRPP CCCCCCCCCCCCCCH	16.84	16928191
50	Methylation	SLSPFYLRPPSFLRA CCCCCCCCCHHHHCC	29.69	12060738
53	Phosphorylation	PFYLRPPSFLRAPSW CCCCCCHHHHCCCCC	39.33	22817900
59	Phosphorylation	PSFLRAPSWFDTGLS HHHHCCCCCCCCCCC	39.11	28355574
63	Phosphorylation	RAPSWFDTGLSEMRL CCCCCCCCCCCHHCC	30.46	29691806
66	Phosphorylation	SWFDTGLSEMRLEKD CCCCCCCCHHCCCCC	30.59	28857561
68	Sulfoxidation	FDTGLSEMRLEKDRF CCCCCCHHCCCCCCE	5.49	30846556
74	Methylation	EMRLEKDRFSVNLDV HHCCCCCCEEEEEEC	36.49	-
76	Phosphorylation	RLEKDRFSVNLDVKH CCCCCCEEEEEECCC	15.81	21082442
82	Ubiquitination	FSVNLDVKHFSPEEL EEEEEECCCCCHHHH	38.30	-
85	Phosphorylation	NLDVKHFSPEELKVK EEECCCCCHHHHEEE	30.99	28857561
90	Acetylation	HFSPEELKVKVLGDV CCCHHHHEEEEEEEE	43.20	22424773
90	Ubiquitination	HFSPEELKVKVLGDV CCCHHHHEEEEEEEE	43.20	-
92	Malonylation	SPEELKVKVLGDVIE CHHHHEEEEEEEEEE	30.10	26320211
92	Ubiquitination	SPEELKVKVLGDVIE CHHHHEEEEEEEEEE	30.10	22120592
92	Acetylation	SPEELKVKVLGDVIE CHHHHEEEEEEEEEE	30.10	22120592
115	Phosphorylation	QDEHGFISREFHRKY CCCCCCCCHHHHHHH	24.40	26437602
132	Phosphorylation	PADVDPLTITSSLSS CCCCCCCEEEECCCC	27.83	-
134	Phosphorylation	DVDPLTITSSLSSDG CCCCCEEEECCCCCC	13.66	-
135	Phosphorylation	VDPLTITSSLSSDGV CCCCEEEECCCCCCE	25.98	28348404
136	Phosphorylation	DPLTITSSLSSDGVL CCCEEEECCCCCCEE	24.50	28348404
138	Phosphorylation	LTITSSLSSDGVLTV CEEEECCCCCCEEEE	28.47	28348404
139	Phosphorylation	TITSSLSSDGVLTVN EEEECCCCCCEEEEC	43.61	28857561
144	Phosphorylation	LSSDGVLTVNGPRKQ CCCCCEEEECCCCCC	14.98	-
150	Ubiquitination	LTVNGPRKQVSGPER EEECCCCCCCCCCCC	59.18	-
153	Phosphorylation	NGPRKQVSGPERTIP CCCCCCCCCCCCEEC	46.25	26437602
158	Phosphorylation	QVSGPERTIPITREE CCCCCCCEECCCCCC	29.46	28857561
162	O-linked_Glycosylation	PERTIPITREEKPAV CCCEECCCCCCCCCC	27.03	31492838
162	Phosphorylation	PERTIPITREEKPAV CCCEECCCCCCCCCC	27.03	26437602
166	Ubiquitination	IPITREEKPAVTAAP ECCCCCCCCCCCCCC	33.26	22120592
166	Acetylation	IPITREEKPAVTAAP ECCCCCCCCCCCCCC	33.26	22120592
170	O-linked_Glycosylation	REEKPAVTAAPKK-- CCCCCCCCCCCCC--	21.14	31492838
170	Phosphorylation	REEKPAVTAAPKK-- CCCCCCCCCCCCC--	21.14	26437602
170	O-linked_Glycosylation	REEKPAVTAAPKK-- CCCCCCCCCCCCC--	21.14	8639509

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
59	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CISY_HUMAN	CS	physical	11377425
HSPB1_HUMAN	HSPB1	physical	1560006
CRYAB_HUMAN	CRYAB	physical	10625651
HSPB2_HUMAN	HSPB2	physical	10625651
CRYAA_HUMAN	CRYAA	physical	11700327
CRBB2_HUMAN	CRYBB2	physical	11700327
CRGC_HUMAN	CRYGC	physical	11700327
CRYAB_HUMAN	CRYAB	physical	11700327
HSPB1_HUMAN	HSPB1	physical	11700327
PSA3_HUMAN	PSMA3	physical	11341940
CCND1_HUMAN	CCND1	physical	17081987
CRYAB_HUMAN	CRYAB	physical	16480679
CRYAA_HUMAN	CRYAA	physical	16142923
A4_HUMAN	APP	physical	16053447
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
LALBA_HUMAN	LALBA	physical	21152271
MDHM_HUMAN	MDH2	physical	21152271
BCL2_HUMAN	BCL2	physical	20841355
CRYAB_HUMAN	CRYAB	physical	19140694
CD40L_HUMAN	CD40LG	physical	21357544
FCG2A_HUMAN	FCGR2A	physical	21357544
ALBU_HUMAN	ALB	physical	21357544
CRYAB_HUMAN	CRYAB	physical	17075130
CRYAA_HUMAN	CRYAA	physical	17260942
CRYAB_HUMAN	CRYAB	physical	18941542
CRBB1_BOVIN	CRYBB1	physical	22090033
HSPB1_HUMAN	HSPB1	physical	20863832
UBC_RAT	Ubc	physical	20863832
BAG3_HUMAN	BAG3	physical	21423662
CRYAB_HUMAN	CRYAB	physical	20802487
CRYAB_HUMAN	CRYAB	physical	19646995
CRYAB_HUMAN	CRYAB	physical	22143763
LBH_HUMAN	LBH	physical	20587334
P53_HUMAN	TP53	physical	19799611
FGF2_HUMAN	FGF2	physical	17487982
NGF_HUMAN	NGF	physical	17487982
VEGFA_HUMAN	VEGFA	physical	17487982
INS_HUMAN	INS	physical	17487982
CTNB1_HUMAN	CTNNB1	physical	17487982
CAD16_HUMAN	CDH16	physical	18343407
DESM_HUMAN	DES	physical	17590381
GFAP_HUMAN	GFAP	physical	17590381
ACTA_RABIT	ACTA2	physical	17590381
CASP3_HUMAN	CASP3	physical	18669646
TPPP_BOVIN	TPPP	physical	20668689
B2CL1_HUMAN	BCL2L1	physical	14752512
BAX_HUMAN	BAX	physical	14752512
CRBA1_HUMAN	CRYBA1	physical	19401464
CRYAB_HUMAN	CRYAB	physical	18639655
CRYAA_HUMAN	CRYAA	physical	18639655
CRYAA_HUMAN	CRYAA	physical	16760894
A4_HUMAN	APP	physical	21961594
UB2D1_HUMAN	UBE2D1	physical	17081987
SYUA_HUMAN	SNCA	physical	20197038
CTNB1_HUMAN	CTNNB1	physical	22158051
CADH1_HUMAN	CDH1	physical	22158051
CRYAA_HUMAN	CRYAA	physical	23188086
HSPB2_HUMAN	HSPB2	physical	23188086
HSPB1_HUMAN	HSPB1	physical	23188086
SMAD4_HUMAN	SMAD4	physical	24307592
TRI33_HUMAN	TRIM33	physical	24307592
HSPB1_HUMAN	HSPB1	physical	23532854
HSPB2_HUMAN	HSPB2	physical	23532854
DDX20_HUMAN	DDX20	physical	24023879
CRYAB_HUMAN	CRYAB	physical	18330356
HSPB1_HUMAN	HSPB1	physical	18330356
CRYAB_HUMAN	CRYAB	physical	25416956
BACH_HUMAN	ACOT7	physical	25416956
TNPO2_HUMAN	TNPO2	physical	25416956
RM11_HUMAN	MRPL11	physical	25416956
TPC6A_HUMAN	TRAPPC6A	physical	25416956
KRA81_HUMAN	KRTAP8-1	physical	25416956
KR195_HUMAN	KRTAP19-5	physical	25416956
NYNRI_HUMAN	NYNRIN	physical	26186194
DDX20_HUMAN	DDX20	physical	26186194
SEH1_HUMAN	SEH1L	physical	26186194
GEMI4_HUMAN	GEMIN4	physical	26186194
IQGA3_HUMAN	IQGAP3	physical	26186194
CDC23_HUMAN	CDC23	physical	26186194
HNRL2_HUMAN	HNRNPUL2	physical	26186194
GOPC_HUMAN	GOPC	physical	26186194
HSPB1_HUMAN	HSPB1	physical	26186194
TIRR_HUMAN	NUDT16L1	physical	26186194
MAP1B_HUMAN	MAP1B	physical	26186194
BAG3_HUMAN	BAG3	physical	26186194
NFL_HUMAN	NEFL	physical	26186194
TPC2A_HUMAN	TRAPPC2	physical	26186194
TPC2B_HUMAN	TRAPPC2	physical	26186194
PRLD1_HUMAN	PRELID1	physical	26186194
SMCR8_HUMAN	SMCR8	physical	26186194
FBX21_HUMAN	FBXO21	physical	26186194
CC85C_HUMAN	CCDC85C	physical	26186194
VP33A_HUMAN	VPS33A	physical	26186194
LENG8_HUMAN	LENG8	physical	26186194
C2D1A_HUMAN	CC2D1A	physical	26186194
TPPC9_HUMAN	TRAPPC9	physical	26186194
CC85B_HUMAN	CCDC85B	physical	26186194
FA83D_HUMAN	FAM83D	physical	26186194
CRYAB_HUMAN	CRYAB	physical	25449278
DHSO_HUMAN	SORD	physical	26344197
CRYAA_HUMAN	CRYAA	physical	25694240
CRYAB_HUMAN	CRYAB	physical	25962097
CCND1_HUMAN	CCND1	physical	19767775
SCN5A_HUMAN	SCN5A	physical	26961874
NED4L_HUMAN	NEDD4L	physical	26961874
CRYAB_HUMAN	CRYAB	physical	26458046
LYSC_HUMAN	LYZ	physical	26458046
A4_HUMAN	APP	physical	26458046
A4_HUMAN	APP	physical	23106396
NYNRI_HUMAN	NYNRIN	physical	28514442
PRLD1_HUMAN	PRELID1	physical	28514442
C2D1A_HUMAN	CC2D1A	physical	28514442
CC85B_HUMAN	CCDC85B	physical	28514442
CDC23_HUMAN	CDC23	physical	28514442
CC85C_HUMAN	CCDC85C	physical	28514442
HNRL2_HUMAN	HNRNPUL2	physical	28514442
SMCR8_HUMAN	SMCR8	physical	28514442
TIRR_HUMAN	NUDT16L1	physical	28514442
HSPB1_HUMAN	HSPB1	physical	28514442
GEMI4_HUMAN	GEMIN4	physical	28514442
SEH1_HUMAN	SEH1L	physical	28514442
TPC2A_HUMAN	TRAPPC2	physical	28514442
TPC2B_HUMAN	TRAPPC2	physical	28514442
LENG8_HUMAN	LENG8	physical	28514442
BAG3_HUMAN	BAG3	physical	28514442
MAP1B_HUMAN	MAP1B	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608810	Myopathy, myofibrillar, 2 (MFM2)
613763	Cataract 16, multiple types (CTRCT16)
613869	Myopathy, myofibrillar, fatal infantile hypertonic, alpha-B crystallin-related (MFMFIH-CRYAB)
615184	Cardiomyopathy, dilated 1II (CMD1II)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CRYAB_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Simultaneous racemization and isomerization at specific aspartic acidresidues in alpha B-crystallin from the aged human lens."; Fujii N., Ishibashi Y., Satoh K., Fujino M., Harada K.; Biochim. Biophys. Acta 1204:157-163(1994). Cited for: RACEMIZATION/ISOMERIZATION OF SPECIFIC ASP.	8142454 [Abstract]
"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: ACETYLATION AT LYS-92 AND LYS-166.	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 SER-19; SER-21; SER-43;SER-45; SER-53; SER-59 AND SER-76, METHYLATION AT ARG-22 AND ARG-50,ACETYLATION AT LYS-92, SUSCEPTIBILITY TO OXIDATION, AND MASSSPECTROMETRY.	12060738 [Abstract]
"In vivo carbamylation and acetylation of water-soluble human lensalphaB-crystallin lysine 92."; Lapko V.N., Smith D.L., Smith J.B.; Protein Sci. 10:1130-1136(2001). Cited for: ACETYLATION AT LYS-92.	11369851 [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 SER-19; SER-21; SER-43;SER-45; SER-53; SER-59 AND SER-76, METHYLATION AT ARG-22 AND ARG-50,ACETYLATION AT LYS-92, SUSCEPTIBILITY TO OXIDATION, AND MASSSPECTROMETRY.	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 SER-19; SER-21; SER-43;SER-45; SER-53; SER-59 AND SER-76, METHYLATION AT ARG-22 AND ARG-50,ACETYLATION AT LYS-92, SUSCEPTIBILITY TO OXIDATION, AND MASSSPECTROMETRY.	12060738 [Abstract]
"Ser-59 is the major phosphorylation site in alphaB-crystallinaccumulated in the brains of patients with Alexander's disease."; Kato K., Inaguma Y., Ito H., Iida K., Iwamoto I., Kamei K., Ochi N.,Ohta H., Kishikawa M.; J. Neurochem. 76:730-736(2001). Cited for: PHOSPHORYLATION AT SER-45 AND SER-59.	11158243 [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-19; SER-45 AND SER-59, AND MASS SPECTROMETRY.	8175657 [Abstract]