dbPTM

CNKR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CNKR1_HUMAN
UniProt AC	Q969H4
Protein Name	Connector enhancer of kinase suppressor of ras 1
Gene Name	CNKSR1
Organism	Homo sapiens (Human).
Sequence Length	720
Subcellular Localization	Cytoplasm. Membrane Peripheral membrane protein.
Protein Description	May function as an adapter protein or regulator of Ras signaling pathways..
Protein Sequence	MEPVETWTPGKVATWLRGLDDSLQDYPFEDWQLPGKNLLQLCPQSLEALAVRSLGHQELILGGVEQLQALSSRLQTENLQSLTEGLLGATHDFQSIVQGCLGDCAKTPIDVLCAAVELLHEADALLFWLSRYLFSHLNDFSACQEIRDLLEELSQVLHEDGPAAEKEGTVLRICSHVAGICHNILVCCPKELLEQKAVLEQVQLDSPLGLEIHTTSNCQHFVSQVDTQVPTDSRLQIQPGDEVVQINEQVVVREERDMVGWPRKNMVRELLREPAGLSLVLKKIPIPETPPQTPPQVLDSPHQRSPSLSLAPLSPRAPSEDVFAFDLSSNPSPGPSPAWTDSASLGPEPLPIPPEPPAILPAGVAGTPGLPESPDKSPVGRKKSKGLATRLSRRRVSCRELGRPDCDGWLLLRKAPGGFMGPRWRRRWFVLKGHTLYWYRQPQDEKAEGLINVSNYSLESGHDQKKKYVFQLTHDVYKPFIFAADTLTDLSMWVRHLITCISKYQSPGRAPPPREEDCYSETEAEDPDDEAGSHSASPSPAQAGSPLHGDTSPAATPTQRSPRTSFGSLTDSSEEALEGMVRGLRQGGVSLLGQPQPLTQEQWRSSFMRRNRDPQLNERVHRVRALQSTLKAKLQELQVLEEVLGDPELTGEKFRQWKEQNRELYSEGLGAWGVAQAEGSSHILTSDSTEQSPHSLPSDPEEHSHLCPLTSESSLRPPDL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MEPVETWTPGKVA --CCCCCCCCCCHHH	34.57	26270265
8	Phosphorylation	MEPVETWTPGKVATW CCCCCCCCCCHHHHH	29.59	26270265
8 (in isoform 2)	Phosphorylation	-	29.59	27251275
22	Phosphorylation	WLRGLDDSLQDYPFE HHHCCCCCCCCCCCC	27.83	-
26	Phosphorylation	LDDSLQDYPFEDWQL CCCCCCCCCCCCCCC	9.25	-
278	Phosphorylation	LREPAGLSLVLKKIP HHCCCCCEEEEECCC	18.60	-
282 (in isoform 2)	Phosphorylation	-	40.97	24719451
286 (in isoform 2)	Phosphorylation	-	5.69	24719451
289	Phosphorylation	KKIPIPETPPQTPPQ ECCCCCCCCCCCCCC	34.61	30278072
293	Phosphorylation	IPETPPQTPPQVLDS CCCCCCCCCCCCCCC	42.59	30278072
293 (in isoform 2)	Phosphorylation	-	42.59	24719451
298 (in isoform 2)	Phosphorylation	-	4.55	24719451
300	Phosphorylation	TPPQVLDSPHQRSPS CCCCCCCCCCCCCCC	21.81	30278072
300 (in isoform 2)	Phosphorylation	-	21.81	24719451
305	Phosphorylation	LDSPHQRSPSLSLAP CCCCCCCCCCCCCCC	16.57	25159151
307 (in isoform 2)	Phosphorylation	-	31.66	24719451
307	Phosphorylation	SPHQRSPSLSLAPLS CCCCCCCCCCCCCCC	31.66	19664994
309	Phosphorylation	HQRSPSLSLAPLSPR CCCCCCCCCCCCCCC	27.16	22167270
314	Phosphorylation	SLSLAPLSPRAPSED CCCCCCCCCCCCCCC	15.98	19664994
385 (in isoform 2)	Phosphorylation	-	67.81	24719451
389	Phosphorylation	KKSKGLATRLSRRRV CCHHHHHHHHHHHCC	36.87	27251275
392	Phosphorylation	KGLATRLSRRRVSCR HHHHHHHHHHCCCHH	22.05	29496963
414	Acetylation	DGWLLLRKAPGGFMG CCEEEEECCCCCCCC	59.92	412439279
456	Phosphorylation	GLINVSNYSLESGHD CCEEEECCCCCCCCC	13.71	-
515 (in isoform 2)	Phosphorylation	-	65.05	27251275
519	Phosphorylation	PPREEDCYSETEAED CCCHHHCCCCCCCCC	23.12	27251275
520	Phosphorylation	PREEDCYSETEAEDP CCHHHCCCCCCCCCC	44.36	28348404
522	Phosphorylation	EEDCYSETEAEDPDD HHHCCCCCCCCCCCC	34.26	28348404
526 (in isoform 2)	Phosphorylation	-	60.00	27251275
533	Phosphorylation	DPDDEAGSHSASPSP CCCCCCCCCCCCCCH	22.71	27251275
557 (in isoform 2)	Phosphorylation	-	23.08	27251275
558 (in isoform 2)	Phosphorylation	-	32.06	24719451
561 (in isoform 2)	Phosphorylation	-	14.65	27251275
563 (in isoform 2)	Phosphorylation	-	44.22	24719451
564	Phosphorylation	PTQRSPRTSFGSLTD CCCCCCCCCCCCCCC	31.62	24719451
565	Phosphorylation	TQRSPRTSFGSLTDS CCCCCCCCCCCCCCC	28.96	25106551
568	Phosphorylation	SPRTSFGSLTDSSEE CCCCCCCCCCCCCHH	26.53	25106551
570	Phosphorylation	RTSFGSLTDSSEEAL CCCCCCCCCCCHHHH	35.22	28857561
572	Phosphorylation	SFGSLTDSSEEALEG CCCCCCCCCHHHHHH	34.12	28348404
573	Phosphorylation	FGSLTDSSEEALEGM CCCCCCCCHHHHHHH	42.12	24719451
590	Phosphorylation	GLRQGGVSLLGQPQP HHHHCCCCCCCCCCC	22.58	24043423
599	Phosphorylation	LGQPQPLTQEQWRSS CCCCCCCCHHHHHHH	36.42	24043423
599 (in isoform 2)	Phosphorylation	-	36.42	24719451
606	Phosphorylation	TQEQWRSSFMRRNRD CHHHHHHHHHHHCCC	17.94	24719451
665	Phosphorylation	KEQNRELYSEGLGAW HHHHHHHHHCCCCHH	10.42	-

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
26	Y	Phosphorylation	Kinase	SRC	P12931	PSP
519	Y	Phosphorylation	Kinase	SRC	P12931	PSP
665	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CNKR1_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 CNKR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RASF1_HUMAN	RASSF1	physical	15075335
STK3_HUMAN	STK3	physical	15075335
STK4_HUMAN	STK4	physical	15075335
RAF1_HUMAN	RAF1	physical	15075335
GNDS_HUMAN	RALGDS	physical	14749388
CYH4_HUMAN	CYTH4	physical	25416956
RHOA_HUMAN	RHOA	physical	14749388
RHPN1_HUMAN	RHPN1	physical	14749388
CYH2_HUMAN	CYTH2	physical	28514442
CYH1_HUMAN	CYTH1	physical	28514442
CYH3_HUMAN	CYTH3	physical	28514442
HAUS5_HUMAN	HAUS5	physical	28514442
ASPM_HUMAN	ASPM	physical	28514442
PHLB3_HUMAN	PHLDB3	physical	28514442
TIF1A_HUMAN	TRIM24	physical	28514442
BRCA2_HUMAN	BRCA2	physical	28514442
TRI33_HUMAN	TRIM33	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 CNKR1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-307 AND SER-314, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-314, ANDMASS SPECTROMETRY.	16964243 [Abstract]