dbPTM

CTNA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CTNA1_HUMAN
UniProt AC	P35221
Protein Name	Catenin alpha-1
Gene Name	CTNNA1
Organism	Homo sapiens (Human).
Sequence Length	906
Subcellular Localization	Isoform 1: Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell membrane Peripheral membrane protein Cytoplasmic side. Cell junction. Found at cell-cell boundaries and probably at cell-matrix boundaries. Isoform 3: Cell membrane Perip
Protein Description	Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation..
Protein Sequence	MTAVHAGNINFKWDPKSLEIRTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGDKIAKESQFLKEELVAAVEDVRKQGDLMKAAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQELKDVGHRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISNAAQATASDDASQHQGGGGGELAYALNNFDKQIIVDPLSFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLACSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRVLTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVTSEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLVYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTAVHAGNI ------CCCEECCCC	37.07	-
2	Phosphorylation	------MTAVHAGNI ------CCCEECCCC	37.07	28857561
12	Ubiquitination	HAGNINFKWDPKSLE ECCCCCCCCCCCCHH	46.31	21890473
12 (in isoform 2)	Ubiquitination	-	46.31	21890473
12 (in isoform 1)	Ubiquitination	-	46.31	21890473
12	Ubiquitination	HAGNINFKWDPKSLE ECCCCCCCCCCCCHH	46.31	21890473
16	Ubiquitination	INFKWDPKSLEIRTL CCCCCCCCCHHHHHH	66.26	21890473
16 (in isoform 2)	Ubiquitination	-	66.26	21890473
16 (in isoform 1)	Ubiquitination	-	66.26	21890473
16	Ubiquitination	INFKWDPKSLEIRTL CCCCCCCCCHHHHHH	66.26	21890473
17	Phosphorylation	NFKWDPKSLEIRTLA CCCCCCCCHHHHHHH	36.30	24719451
34	Phosphorylation	RLLEPLVTQVTTLVN HHHHHHHHHHHHHHC	25.63	25002506
37	Phosphorylation	EPLVTQVTTLVNTNS HHHHHHHHHHHCCCC	12.47	23403867
38	Phosphorylation	PLVTQVTTLVNTNSK HHHHHHHHHHCCCCC	29.83	23403867
42	Phosphorylation	QVTTLVNTNSKGPSN HHHHHHCCCCCCCCC	33.13	29255136
44	Phosphorylation	TTLVNTNSKGPSNKK HHHHCCCCCCCCCCC	36.63	29255136
45	Ubiquitination	TLVNTNSKGPSNKKR HHHCCCCCCCCCCCC	76.53	21906983
45 (in isoform 2)	Ubiquitination	-	76.53	21890473
45 (in isoform 1)	Ubiquitination	-	76.53	21890473
48	Phosphorylation	NTNSKGPSNKKRGRS CCCCCCCCCCCCCCC	70.70	29255136
50	Ubiquitination	NSKGPSNKKRGRSKK CCCCCCCCCCCCCCH	48.46	-
57	Ubiquitination	KKRGRSKKAHVLAAS CCCCCCCHHHHHHHH	45.00	-
57	Sumoylation	KKRGRSKKAHVLAAS CCCCCCCHHHHHHHH	45.00	28112733
64	Phosphorylation	KAHVLAASVEQATEN HHHHHHHHHHHHHHH	22.15	28857561
75	Ubiquitination	ATENFLEKGDKIAKE HHHHHHHHHHHHHHH	74.65	-
81	Ubiquitination	EKGDKIAKESQFLKE HHHHHHHHHHHHHHH	62.46	21906983
81 (in isoform 2)	Ubiquitination	-	62.46	21890473
81 (in isoform 1)	Ubiquitination	-	62.46	21890473
83	Phosphorylation	GDKIAKESQFLKEEL HHHHHHHHHHHHHHH	26.06	17855441
87	Ubiquitination	AKESQFLKEELVAAV HHHHHHHHHHHHHHH	50.89	-
117	Phosphorylation	EFADDPCSSVKRGNM CCCCCCCHHHHHHHH	43.48	25850435
118	Phosphorylation	FADDPCSSVKRGNMV CCCCCCHHHHHHHHH	38.07	25159151
120	Acetylation	DDPCSSVKRGNMVRA CCCCHHHHHHHHHHH	57.44	26051181
133	Phosphorylation	RAARALLSAVTRLLI HHHHHHHHHHHHHHH	22.88	24076635
136	Phosphorylation	RALLSAVTRLLILAD HHHHHHHHHHHHHHH	18.47	22817900
148	Phosphorylation	LADMADVYKLLVQLK HHHHHHHHHHHHHHC	9.10	21406692
155	Acetylation	YKLLVQLKVVEDGIL HHHHHHHCCCCCCEE	27.43	25953088
163	Ubiquitination	VVEDGILKLRNAGNE CCCCCEEEECCCCCC	43.40	-
163 (in isoform 2)	Ubiquitination	-	43.40	-
165	Methylation	EDGILKLRNAGNEQD CCCEEEECCCCCCCC	29.39	-
177	Phosphorylation	EQDLGIQYKALKPEV CCCCCCCHHHHCHHH	9.05	27273156
178	Ubiquitination	QDLGIQYKALKPEVD CCCCCCHHHHCHHHH	30.76	21890473
178 (in isoform 2)	Ubiquitination	-	30.76	21890473
178 (in isoform 1)	Ubiquitination	-	30.76	21890473
178	Ubiquitination	QDLGIQYKALKPEVD CCCCCCHHHHCHHHH	30.76	21890473
181	Acetylation	GIQYKALKPEVDKLN CCCHHHHCHHHHHHH	43.95	19608861
181	Ubiquitination	GIQYKALKPEVDKLN CCCHHHHCHHHHHHH	43.95	19608861
181 (in isoform 2)	Ubiquitination	-	43.95	21890473
181	Malonylation	GIQYKALKPEVDKLN CCCHHHHCHHHHHHH	43.95	26320211
181 (in isoform 1)	Ubiquitination	-	43.95	21890473
181	Ubiquitination	GIQYKALKPEVDKLN CCCHHHHCHHHHHHH	43.95	21890473
186	Acetylation	ALKPEVDKLNIMAAK HHCHHHHHHHHHHHH	48.92	23236377
186	Ubiquitination	ALKPEVDKLNIMAAK HHCHHHHHHHHHHHH	48.92	19608861
193	Acetylation	KLNIMAAKRQQELKD HHHHHHHHHHHHHHC	41.00	23236377
193	Ubiquitination	KLNIMAAKRQQELKD HHHHHHHHHHHHHHC	41.00	-
199	Ubiquitination	AKRQQELKDVGHRDQ HHHHHHHHCCCHHHH	50.01	-
216	Ubiquitination	AARGILQKNVPILYT HHHHHHHHCCCEEEE	57.37	21890473
216 (in isoform 2)	Ubiquitination	-	57.37	21890473
216 (in isoform 1)	Ubiquitination	-	57.37	21890473
216	Ubiquitination	AARGILQKNVPILYT HHHHHHHHCCCEEEE	57.37	21890473
222	Phosphorylation	QKNVPILYTASQACL HHCCCEEEECCHHHH	10.86	28152594
222 (in isoform 2)	Phosphorylation	-	10.86	27642862
223	Phosphorylation	KNVPILYTASQACLQ HCCCEEEECCHHHHH	19.18	28152594
225	Phosphorylation	VPILYTASQACLQHP CCEEEECCHHHHHCC	15.54	28152594
237	Phosphorylation	QHPDVAAYKANRDLI HCCCHHHHHHCHHHH	10.82	28152594
238	Ubiquitination	HPDVAAYKANRDLIY CCCHHHHHHCHHHHH	34.16	-
245	Phosphorylation	KANRDLIYKQLQQAV HHCHHHHHHHHHHHH	10.44	27259358
246	Ubiquitination	ANRDLIYKQLQQAVT HCHHHHHHHHHHHHH	37.22	-
262	Phosphorylation	ISNAAQATASDDASQ CCCHHHHHCCCCCHH	18.02	26356563
264	Phosphorylation	NAAQATASDDASQHQ CHHHHHCCCCCHHCC	31.50	26356563
268	Phosphorylation	ATASDDASQHQGGGG HHCCCCCHHCCCCCH	34.88	28152594
280	Phosphorylation	GGGGELAYALNNFDK CCHHHHHHHHCCCCC	25.01	28152594
280 (in isoform 2)	Phosphorylation	-	25.01	27642862
295	Phosphorylation	QIIVDPLSFSEERFR CEEECCCCCCHHHHC	31.92	26657352
297	Phosphorylation	IVDPLSFSEERFRPS EECCCCCCHHHHCCC	34.86	30266825
304	Phosphorylation	SEERFRPSLEERLES CHHHHCCCHHHHHHH	44.12	20860994
311	Phosphorylation	SLEERLESIISGAAL CHHHHHHHHHHHHHH	29.79	27251275
322	Phosphorylation	GAALMADSSCTRDDR HHHHHCCCCCCCCHH	20.13	25850435
323	Phosphorylation	AALMADSSCTRDDRR HHHHCCCCCCCCHHH	21.76	25850435
324	Glutathionylation	ALMADSSCTRDDRRE HHHCCCCCCCCHHHH	4.13	22555962
325	Phosphorylation	LMADSSCTRDDRRER HHCCCCCCCCHHHHH	38.80	25850435
361	Phosphorylation	NAGRKERSDALNSAI CCCHHHHHHHHHHHH	28.47	17855441
366	Phosphorylation	ERSDALNSAIDKMTK HHHHHHHHHHHHHHH	27.70	27050516
370	Ubiquitination	ALNSAIDKMTKKTRD HHHHHHHHHHHHHHH	42.21	-
372	Phosphorylation	NSAIDKMTKKTRDLR HHHHHHHHHHHHHHH	34.82	17855441
384	Ubiquitination	DLRRQLRKAVMDHVS HHHHHHHHHHHHHCC	54.66	-
391	Phosphorylation	KAVMDHVSDSFLETN HHHHHHCCHHHHHCC	24.90	28348404
393	Phosphorylation	VMDHVSDSFLETNVP HHHHCCHHHHHCCCC	24.99	28348404
414	Ubiquitination	AAKNGNEKEVKEYAQ HHHCCCHHHHHHHHH	72.33	21906983
414 (in isoform 1)	Ubiquitination	-	72.33	21890473
414 (in isoform 2)	Ubiquitination	-	72.33	21890473
417	Ubiquitination	NGNEKEVKEYAQVFR CCCHHHHHHHHHHHH	46.21	-
417	Malonylation	NGNEKEVKEYAQVFR CCCHHHHHHHHHHHH	46.21	26320211
419	Phosphorylation	NEKEVKEYAQVFREH CHHHHHHHHHHHHHH	9.16	28152594
429	Ubiquitination	VFREHANKLIEVANL HHHHHHHHHHHHHHH	52.18	-
439	Phosphorylation	EVANLACSISNNEEG HHHHHHHHCCCCHHH	24.36	26657352
441	Phosphorylation	ANLACSISNNEEGVK HHHHHHCCCCHHHHE	19.80	25072903
448	Ubiquitination	SNNEEGVKLVRMSAS CCCHHHHEEEEECHH	52.72	-
452	Sulfoxidation	EGVKLVRMSASQLEA HHHEEEEECHHHHHH	2.82	28465586
453	Phosphorylation	GVKLVRMSASQLEAL HHEEEEECHHHHHHH	17.76	26846344
455	Phosphorylation	KLVRMSASQLEALCP EEEEECHHHHHHHHH	28.17	26846344
472	Acetylation	INAALALAAKPQSKL HHHHHHHHHCCHHHH	14.08	19608861
477	Phosphorylation	ALAAKPQSKLAQENM HHHHCCHHHHHHHCH	37.86	28348404
478	Ubiquitination	LAAKPQSKLAQENMD HHHCCHHHHHHHCHH	42.46	21890473
478 (in isoform 2)	Ubiquitination	-	42.46	21890473
478 (in isoform 1)	Ubiquitination	-	42.46	21890473
478	Ubiquitination	LAAKPQSKLAQENMD HHHCCHHHHHHHCHH	42.46	21890473
493	Ubiquitination	LFKEQWEKQVRVLTD HHHHHHHHHHHHHHH	51.65	-
499	Phosphorylation	EKQVRVLTDAVDDIT HHHHHHHHHCCCCCC	21.03	20639409
506	Phosphorylation	TDAVDDITSIDDFLA HHCCCCCCCHHHHHH	26.99	20639409
507	Phosphorylation	DAVDDITSIDDFLAV HCCCCCCCHHHHHHH	25.10	28192239
515	Phosphorylation	IDDFLAVSENHILED HHHHHHHCCHHHHHH	27.37	20639409
533	Ubiquitination	CVIALQEKDVDGLDR HHHHHHHCCCCCCCC	50.52	-
541	Phosphorylation	DVDGLDRTAGAIRGR CCCCCCCCCHHHHHH	29.16	22210691
563	Phosphorylation	VTSEMDNYEPGVYTE EECCCCCCCCCCCHH	21.16	-
563 (in isoform 2)	Phosphorylation	-	21.16	27642862
571 (in isoform 2)	Ubiquitination	-	44.30	-
577	Ubiquitination	EKVLEATKLLSNTVM HHHHHHHHHHCCCCC	55.25	21890473
577 (in isoform 2)	Ubiquitination	-	55.25	21890473
577 (in isoform 1)	Ubiquitination	-	55.25	21890473
577	Ubiquitination	EKVLEATKLLSNTVM HHHHHHHHHHCCCCC	55.25	21890473
619	Phosphorylation	IDASRLVYDGIRDIR CCHHHHHHHHHHHHH	17.03	27273156
634	Phosphorylation	KAVLMIRTPEELDDS HHHHCCCCHHHCCCC	24.91	22167270
641	Phosphorylation	TPEELDDSDFETEDF CHHHCCCCCCCCCCC	43.81	19664994
645	Phosphorylation	LDDSDFETEDFDVRS CCCCCCCCCCCCCCC	40.63	22167270
652	Phosphorylation	TEDFDVRSRTSVQTE CCCCCCCCCCCEECC	39.49	19664994
654	Phosphorylation	DFDVRSRTSVQTEDD CCCCCCCCCEECCCC	34.20	29255136
655	Phosphorylation	FDVRSRTSVQTEDDQ CCCCCCCCEECCCCC	15.89	19664994
658	Phosphorylation	RSRTSVQTEDDQLIA CCCCCEECCCCCCCC	38.95	19664994
668	Phosphorylation	DQLIAGQSARAIMAQ CCCCCHHHHHHHHHC	20.85	23927012
673	Sulfoxidation	GQSARAIMAQLPQEQ HHHHHHHHHCCCHHH	1.57	21406390
681	Ubiquitination	AQLPQEQKAKIAEQV HCCCHHHHHHHHHHH	51.39	-
683	Ubiquitination	LPQEQKAKIAEQVAS CCHHHHHHHHHHHHH	49.86	-
683 (in isoform 2)	Ubiquitination	-	49.86	-
690	Phosphorylation	KIAEQVASFQEEKSK HHHHHHHHHHHHHHH	28.71	23911959
695	Ubiquitination	VASFQEEKSKLDAEV HHHHHHHHHHHHHHH	52.73	21906983
695 (in isoform 2)	Ubiquitination	-	52.73	21890473
695 (in isoform 1)	Ubiquitination	-	52.73	21890473
696	Phosphorylation	ASFQEEKSKLDAEVS HHHHHHHHHHHHHHH	41.55	28857561
727	Phosphorylation	CMIMMEMTDFTRGKG HHHHHHHCCCCCCCC	18.04	24043423
730	Phosphorylation	MMEMTDFTRGKGPLK HHHHCCCCCCCCCCC	41.12	24043423
737	Ubiquitination	TRGKGPLKNTSDVIS CCCCCCCCCHHHHHH	62.40	-
740	Phosphorylation	KGPLKNTSDVISAAK CCCCCCHHHHHHHHH	38.99	24275569
744	Phosphorylation	KNTSDVISAAKKIAE CCHHHHHHHHHHHHH	23.25	-
747	Acetylation	SDVISAAKKIAEAGS HHHHHHHHHHHHHHH	44.41	7705707
747	Ubiquitination	SDVISAAKKIAEAGS HHHHHHHHHHHHHHH	44.41	-
747	Malonylation	SDVISAAKKIAEAGS HHHHHHHHHHHHHHH	44.41	26320211
754	Phosphorylation	KKIAEAGSRMDKLGR HHHHHHHHHHHHHCC	31.32	21406692
758	Ubiquitination	EAGSRMDKLGRTIAD HHHHHHHHHCCHHHH	43.42	2190698
758 (in isoform 1)	Ubiquitination	-	43.42	21890473
758 (in isoform 2)	Ubiquitination	-	43.42	21890473
762	Phosphorylation	RMDKLGRTIADHCPD HHHHHCCHHHHHCCC	20.79	20860994
767	S-nitrosylation	GRTIADHCPDSACKQ CCHHHHHCCCCHHHH	4.05	2212679
770	Phosphorylation	IADHCPDSACKQDLL HHHHCCCCHHHHHHH	22.25	20860994
772	S-nitrosylation	DHCPDSACKQDLLAY HHCCCCHHHHHHHHH	4.75	2212679
773	Ubiquitination	HCPDSACKQDLLAYL HCCCCHHHHHHHHHH	46.71	-
779	Phosphorylation	CKQDLLAYLQRIALY HHHHHHHHHHHHHHH	11.88	28152594
797	Ubiquitination	LNICSKVKAEVQNLG HCCHHHHHHHHHHCC	42.43	21139048
797	Sumoylation	LNICSKVKAEVQNLG HCCHHHHHHHHHHCC	42.43	28112733
837	Phosphorylation	VQTVKASYVASTKYQ HHHHHHHHHHCCCCC	12.61	-
842	Acetylation	ASYVASTKYQKSQGM HHHHHCCCCCCCCCC	43.09	19608861
842	Ubiquitination	ASYVASTKYQKSQGM HHHHHCCCCCCCCCC	43.09	19608861
846	Phosphorylation	ASTKYQKSQGMASLN HCCCCCCCCCCCCCC	19.21	28348404
851	Phosphorylation	QKSQGMASLNLPAVS CCCCCCCCCCCCHHC	14.65	28112733
858	Phosphorylation	SLNLPAVSWKMKAPE CCCCCHHCCCCCCCC	24.08	28857561
880	Phosphorylation	EKQDETQTKIKRASQ HHCHHHHHHHHHHHH	42.00	26074081
886	Phosphorylation	QTKIKRASQKKHVNP HHHHHHHHHCCCCCH	46.71	26074081
898	Phosphorylation	VNPVQALSEFKAMDS CCHHHHHHHHHHHCC	43.96	26074081
901	Methylation	VQALSEFKAMDSI-- HHHHHHHHHHCCC--	38.46	-
901	Ubiquitination	VQALSEFKAMDSI-- HHHHHHHHHHCCC--	38.46	-
901 (in isoform 1)	Ubiquitination	-	38.46	21890473
905	Phosphorylation	SEFKAMDSI------ HHHHHHCCC------	19.67	24719451
925 (in isoform 2)	Ubiquitination	-		21890473

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
641	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
641	S	Phosphorylation	Kinase	CK2	-	Uniprot
652	S	Phosphorylation	Kinase	CK1	-	Uniprot
655	S	Phosphorylation	Kinase	CK1	-	Uniprot
658	T	Phosphorylation	Kinase	CK1	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CTNA1_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 CTNA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CTNA1_HUMAN	CTNNA1	physical	9762469
CTNB1_HUMAN	CTNNB1	physical	9762469
PLAK_HUMAN	JUP	physical	9762469
CTND1_HUMAN	CTNND1	physical	7651399
AFAD_HUMAN	MLLT4	physical	11907041
PLAK_HUMAN	JUP	physical	7650039
CTNB1_HUMAN	CTNNB1	physical	7706414
CADH3_HUMAN	CDH3	physical	10381631
CADH1_HUMAN	CDH1	physical	10381631
VINC_HUMAN	VCL	physical	9700171
DLG1_HUMAN	DLG1	physical	9512503
CTNB1_HUMAN	CTNNB1	physical	9512503
SPTB2_HUMAN	SPTBN1	physical	11069925
PLAK_HUMAN	JUP	physical	20936779
RN219_HUMAN	RNF219	physical	20936779
ZGPAT_HUMAN	ZGPAT	physical	20936779
ARMC8_HUMAN	ARMC8	physical	18215130
A4_HUMAN	APP	physical	21832049
PLAK_HUMAN	JUP	physical	22939629
SRC8_HUMAN	CTTN	physical	22863883
CUL2_HUMAN	CUL2	physical	22863883
IF4B_HUMAN	EIF4B	physical	22863883
HS105_HUMAN	HSPH1	physical	22863883
ANM3_HUMAN	PRMT3	physical	22863883
XPO7_HUMAN	XPO7	physical	22863883
CTNB1_HUMAN	CTNNB1	physical	26344197
DMD_HUMAN	DMD	physical	26344197
PLAK_HUMAN	JUP	physical	26344197
IQEC1_HUMAN	IQSEC1	physical	16807291
CTNB1_HUMAN	CTNNB1	physical	19941816

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
137215	Hereditary diffuse gastric cancer (HDGC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CTNA1_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-186, AND MASS SPECTROMETRY.	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-641 AND SER-652, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASSSPECTROMETRY.	19369195 [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-641; SER-652; THR-654;SER-655 AND THR-658, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND THR-645, ANDMASS SPECTROMETRY.	18318008 [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-641; SER-652; SER-655AND THR-658, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-652 ANDTHR-658, AND MASS SPECTROMETRY.	17487921 [Abstract]
"Phosphoproteomic analysis of the human pituitary."; Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; Pituitary 9:109-120(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASSSPECTROMETRY.	16807684 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASSSPECTROMETRY.	15302935 [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-177 AND TYR-619, ANDMASS SPECTROMETRY.	18083107 [Abstract]