CRIP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CRIP2_HUMAN
• UniProt AC: P52943
• Protein Name: Cysteine-rich protein 2
• Gene Name: CRIP2
• Organism: Homo sapiens (Human).
• Sequence Length: 208
• Protein Sequence: MASKCPKCDKTVYFAEKVSSLGKDWHKFCLKCERCSKTLTPGGHAEHDGKPFCHKPCYATLFGPKGVNIGGAGSYIYEKPLAEGPQVTGPIEVPAARAEERKASGPPKGPSRASSVTTFTGEPNTCPRCSKKVYFAEKVTSLGKDWHRPCLRCERCGKTLTPGGHAEHDGQPYCHKPCYGILFGPKGVNTGAVGSYIYDRDPEGKVQP

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	KCPKCDKTVYFAEKV CCCCCCCCHHHHHHH	13.74	28152594
13	Phosphorylation	PKCDKTVYFAEKVSS CCCCCCHHHHHHHHH	11.42	28152594
17	Acetylation	KTVYFAEKVSSLGKD CCHHHHHHHHHCCCC	43.94	27452117
19	Phosphorylation	VYFAEKVSSLGKDWH HHHHHHHHHCCCCHH	30.80	29396449
20	Phosphorylation	YFAEKVSSLGKDWHK HHHHHHHHCCCCHHH	44.09	28857561
23	Acetylation	EKVSSLGKDWHKFCL HHHHHCCCCHHHHHH	64.04	22424773
31	Acetylation	DWHKFCLKCERCSKT CHHHHHHHCCCCCCE	34.92	27452117
38	Phosphorylation	KCERCSKTLTPGGHA HCCCCCCEECCCCCC	21.41	27251275
40	Phosphorylation	ERCSKTLTPGGHAEH CCCCCEECCCCCCCC	25.72	25159151
58	Phosphorylation	PFCHKPCYATLFGPK CCCCCCEEEEHHCCC	15.91	25159151
60	Phosphorylation	CHKPCYATLFGPKGV CCCCEEEEHHCCCCC	8.99	28348404
74	Phosphorylation	VNIGGAGSYIYEKPL CEECCCCCCEECCCC	14.07	21945579
75	Phosphorylation	NIGGAGSYIYEKPLA EECCCCCCEECCCCC	13.45	21945579
77	Phosphorylation	GGAGSYIYEKPLAEG CCCCCCEECCCCCCC	15.07	21945579
79	Acetylation	AGSYIYEKPLAEGPQ CCCCEECCCCCCCCC	28.49	23236377
88	O-linked_Glycosylation	LAEGPQVTGPIEVPA CCCCCCCCCCEECCC	31.80	31373491
88	Phosphorylation	LAEGPQVTGPIEVPA CCCCCCCCCCEECCC	31.80	21945579
104	Phosphorylation	RAEERKASGPPKGPS HHHHHHHCCCCCCCC	55.67	22617229
111	Phosphorylation	SGPPKGPSRASSVTT CCCCCCCCCCCCEEE	49.50	25849741
112	Phosphorylation	GPPKGPSRASSVTTF CCCCCCCCCCCEEEE	41.44	27251275
114	Phosphorylation	PKGPSRASSVTTFTG CCCCCCCCCEEEECC	25.00	23401153
115	Phosphorylation	KGPSRASSVTTFTGE CCCCCCCCEEEECCC	23.62	29255136
117	Phosphorylation	PSRASSVTTFTGEPN CCCCCCEEEECCCCC	20.38	30266825
118	Phosphorylation	SRASSVTTFTGEPNT CCCCCEEEECCCCCC	19.62	30266825
120	Phosphorylation	ASSVTTFTGEPNTCP CCCEEEECCCCCCCC	38.24	29255136
125	Phosphorylation	TFTGEPNTCPRCSKK EECCCCCCCCCCCCE	34.30	29255136
126	S-nitrosylation	FTGEPNTCPRCSKKV ECCCCCCCCCCCCEE	2.25	2212679
134	Phosphorylation	PRCSKKVYFAEKVTS CCCCCEEEEHHHHHH	13.12	28152594
138	Acetylation	KKVYFAEKVTSLGKD CEEEEHHHHHHCCCC	47.59	19608861
141	Phosphorylation	YFAEKVTSLGKDWHR EEHHHHHHCCCCCCC	37.80	28857561
144	Ubiquitination	EKVTSLGKDWHRPCL HHHHHCCCCCCCCCC	64.04	29967540
144	Acetylation	EKVTSLGKDWHRPCL HHHHHCCCCCCCCCC	64.04	72623839
148	Phosphorylation	SLGKDWHRPCLRCER HCCCCCCCCCCCCCC	21.26	27251275
151	Phosphorylation	KDWHRPCLRCERCGK CCCCCCCCCCCCCCC	8.54	27251275
159	Phosphorylation	RCERCGKTLTPGGHA CCCCCCCEECCCCCC	22.58	28258704
161	Phosphorylation	ERCGKTLTPGGHAEH CCCCCEECCCCCCCC	25.72	28258704
162	Phosphorylation	RCGKTLTPGGHAEHD CCCCEECCCCCCCCC	50.29	27251275
178	Phosphorylation	QPYCHKPCYGILFGP CCCCCCCCEEEEECC	6.07	27251275
179	Phosphorylation	PYCHKPCYGILFGPK CCCCCCCEEEEECCC	18.74	28258704
185	Phosphorylation	CYGILFGPKGVNTGA CEEEEECCCCCCCCC	23.93	27251275
189	Phosphorylation	LFGPKGVNTGAVGSY EECCCCCCCCCCCCE	41.27	32645325
190	Phosphorylation	FGPKGVNTGAVGSYI ECCCCCCCCCCCCEE	24.90	21945579
192	Phosphorylation	PKGVNTGAVGSYIYD CCCCCCCCCCCEECC	10.64	27251275
194	Phosphorylation	GVNTGAVGSYIYDRD CCCCCCCCCEECCCC	17.75	27251275
195	Phosphorylation	VNTGAVGSYIYDRDP CCCCCCCCEECCCCC	11.19	21945579
196	Phosphorylation	NTGAVGSYIYDRDPE CCCCCCCEECCCCCC	9.51	21945579
198	Phosphorylation	GAVGSYIYDRDPEGK CCCCCEECCCCCCCC	9.19	21945579
199	Phosphorylation	AVGSYIYDRDPEGKV CCCCEECCCCCCCCC	38.66	27251275
205	Acetylation	YDRDPEGKVQP---- CCCCCCCCCCC----	35.71	23236377
212	Acetylation	KVQP----------- CCCC-----------		19608861
218	Ubiquitination	----------------- -----------------		29967540
233	Phosphorylation	-------------------------------- --------------------------------		27251275
235	Phosphorylation	---------------------------------- ----------------------------------		27251275
269	Phosphorylation	-------------------------------------------------------------------- --------------------------------------------------------------------		27251275

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
104	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CRIP2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CRIP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-138, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-77, AND MASSSPECTROMETRY.
PubMed: 18083107