dbPTM

CAP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAP1_HUMAN
UniProt AC	Q01518
Protein Name	Adenylyl cyclase-associated protein 1
Gene Name	CAP1
Organism	Homo sapiens (Human).
Sequence Length	475
Subcellular Localization	Cell membrane Peripheral membrane protein.
Protein Description	Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity..
Protein Sequence	MADMQNLVERLERAVGRLEAVSHTSDMHRGYADSPSKAGAAPYVQAFDSLLAGPVAEYLKISKEIGGDVQKHAEMVHTGLKLERALLVTASQCQQPAENKLSDLLAPISEQIKEVITFREKNRGSKLFNHLSAVSESIQALGWVAMAPKPGPYVKEMNDAAMFYTNRVLKEYKDVDKKHVDWVKAYLSIWTELQAYIKEFHTTGLAWSKTGPVAKELSGLPSGPSAGSCPPPPPPCPPPPPVSTISCSYESASRSSLFAQINQGESITHALKHVSDDMKTHKNPALKAQSGPVRSGPKPFSAPKPQTSPSPKRATKKEPAVLELEGKKWRVENQENVSNLVIEDTELKQVAYIYKCVNTTLQIKGKINSITVDNCKKLGLVFDDVVGIVEIINSKDVKVQVMGKVPTISINKTDGCHAYLSKNSLDCEIVSAKSSEMNVLIPTEGGDFNEFPVPEQFKTLWNGQKLVTTVTEIAG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADMQNLVE ------CHHHHHHHH	22.45	19413330
4	Sulfoxidation	----MADMQNLVERL ----CHHHHHHHHHH	1.75	28465586
22	Phosphorylation	VGRLEAVSHTSDMHR HHHHHHHCCCCCCCC	28.26	26074081
24	Phosphorylation	RLEAVSHTSDMHRGY HHHHHCCCCCCCCCC	20.93	26074081
25	Phosphorylation	LEAVSHTSDMHRGYA HHHHCCCCCCCCCCC	27.75	23401153
27	Sulfoxidation	AVSHTSDMHRGYADS HHCCCCCCCCCCCCC	2.02	30846556
31	Phosphorylation	TSDMHRGYADSPSKA CCCCCCCCCCCHHHC	13.75	30266825
31 (in isoform 2)	Phosphorylation	-	13.75	26434776
34	Phosphorylation	MHRGYADSPSKAGAA CCCCCCCCHHHCCCC	23.93	23401153
34 (in isoform 2)	Phosphorylation	-	23.93	29743597
36	Phosphorylation	RGYADSPSKAGAAPY CCCCCCHHHCCCCCH	38.80	30266825
36 (in isoform 2)	Phosphorylation	-	38.80	26434776
42 (in isoform 2)	Phosphorylation	-	29.33	26434776
43	Phosphorylation	SKAGAAPYVQAFDSL HHCCCCCHHHHHHHH	10.64	26307563
49	Phosphorylation	PYVQAFDSLLAGPVA CHHHHHHHHHHHHHH	20.87	28450419
63	Acetylation	AEYLKISKEIGGDVQ HHHHHHHHHHCCCHH	57.75	23749302
63	Ubiquitination	AEYLKISKEIGGDVQ HHHHHHHHHHCCCHH	57.75	-
63	2-Hydroxyisobutyrylation	AEYLKISKEIGGDVQ HHHHHHHHHHCCCHH	57.75	-
63	Malonylation	AEYLKISKEIGGDVQ HHHHHHHHHHCCCHH	57.75	26320211
70 (in isoform 2)	Ubiquitination	-	36.24	21890473
71	Ubiquitination	EIGGDVQKHAEMVHT HHCCCHHHHHHHHHH	44.63	21890473
71	Acetylation	EIGGDVQKHAEMVHT HHCCCHHHHHHHHHH	44.63	23236377
71	Malonylation	EIGGDVQKHAEMVHT HHCCCHHHHHHHHHH	44.63	26320211
71 (in isoform 1)	Ubiquitination	-	44.63	21890473
75	Sulfoxidation	DVQKHAEMVHTGLKL CHHHHHHHHHHCCHH	2.51	30846556
81	Acetylation	EMVHTGLKLERALLV HHHHHCCHHHHHHHH	50.04	19608861
81	Ubiquitination	EMVHTGLKLERALLV HHHHHCCHHHHHHHH	50.04	19608861
81	Malonylation	EMVHTGLKLERALLV HHHHHCCHHHHHHHH	50.04	26320211
81	Succinylation	EMVHTGLKLERALLV HHHHHCCHHHHHHHH	50.04	23954790
93	S-nitrosocysteine	LLVTASQCQQPAENK HHHHHHHCCCCHHCH	3.62	-
93	S-nitrosylation	LLVTASQCQQPAENK HHHHHHHCCCCHHCH	3.62	19483679
93	S-palmitoylation	LLVTASQCQQPAENK HHHHHHHCCCCHHCH	3.62	29575903
100	Ubiquitination	CQQPAENKLSDLLAP CCCCHHCHHHHHHHH	40.65	-
100	Acetylation	CQQPAENKLSDLLAP CCCCHHCHHHHHHHH	40.65	23236377
102	Phosphorylation	QPAENKLSDLLAPIS CCHHCHHHHHHHHHH	28.02	21712546
102	O-linked_Glycosylation	QPAENKLSDLLAPIS CCHHCHHHHHHHHHH	28.02	28510447
109	Phosphorylation	SDLLAPISEQIKEVI HHHHHHHHHHHHHHH	23.53	21712546
113	Ubiquitination	APISEQIKEVITFRE HHHHHHHHHHHHHHH	45.69	-
149	Ubiquitination	GWVAMAPKPGPYVKE CCEEECCCCCCCCHH	53.74	-
155	Malonylation	PKPGPYVKEMNDAAM CCCCCCCHHHHHHHH	45.46	26320211
157	Sulfoxidation	PGPYVKEMNDAAMFY CCCCCHHHHHHHHHH	4.57	30846556
162	Sulfoxidation	KEMNDAAMFYTNRVL HHHHHHHHHHHHHHH	2.57	30846556
164	Phosphorylation	MNDAAMFYTNRVLKE HHHHHHHHHHHHHHH	7.04	19702290
165	Phosphorylation	NDAAMFYTNRVLKEY HHHHHHHHHHHHHHC	12.79	20068231
170	Acetylation	FYTNRVLKEYKDVDK HHHHHHHHHCCCCCH	57.02	26051181
172	Phosphorylation	TNRVLKEYKDVDKKH HHHHHHHCCCCCHHH	15.76	20068231
173	Acetylation	NRVLKEYKDVDKKHV HHHHHHCCCCCHHHH	52.98	26051181
177	Acetylation	KEYKDVDKKHVDWVK HHCCCCCHHHHHHHH	44.63	25953088
178	Ubiquitination	EYKDVDKKHVDWVKA HCCCCCHHHHHHHHH	44.38	-
178	2-Hydroxyisobutyrylation	EYKDVDKKHVDWVKA HCCCCCHHHHHHHHH	44.38	-
178	Acetylation	EYKDVDKKHVDWVKA HCCCCCHHHHHHHHH	44.38	25953088
184	Methylation	KKHVDWVKAYLSIWT HHHHHHHHHHHHHHH	27.36	-
209	Acetylation	TTGLAWSKTGPVAKE HCCCCCCCCCCCHHH	46.96	23236377
209	Malonylation	TTGLAWSKTGPVAKE HCCCCCCCCCCCHHH	46.96	26320211
218	Phosphorylation	GPVAKELSGLPSGPS CCCHHHHCCCCCCCC	39.10	-
222	Phosphorylation	KELSGLPSGPSAGSC HHHCCCCCCCCCCCC	69.27	-
245	Phosphorylation	PPPPVSTISCSYESA CCCCCCEEEECCCCC	2.81	27251275
246	Phosphorylation	PPPVSTISCSYESAS CCCCCEEEECCCCCC	9.33	24719451
255	Phosphorylation	SYESASRSSLFAQIN CCCCCCCCHHHEEHH	28.97	27251275
266	Phosphorylation	AQINQGESITHALKH EEHHHCCCHHHHHHH	39.34	24719451
275	Phosphorylation	THALKHVSDDMKTHK HHHHHHCCHHHHHCC	27.84	27251275
278	Sulfoxidation	LKHVSDDMKTHKNPA HHHCCHHHHHCCCCC	6.91	30846556
279	Methylation	KHVSDDMKTHKNPAL HHCCHHHHHCCCCCH	55.24	-
279	2-Hydroxyisobutyrylation	KHVSDDMKTHKNPAL HHCCHHHHHCCCCCH	55.24	-
280	Phosphorylation	HVSDDMKTHKNPALK HCCHHHHHCCCCCHH	31.29	20068231
282	Ubiquitination	SDDMKTHKNPALKAQ CHHHHHCCCCCHHCC	70.61	-
282	2-Hydroxyisobutyrylation	SDDMKTHKNPALKAQ CHHHHHCCCCCHHCC	70.61	-
282	Acetylation	SDDMKTHKNPALKAQ CHHHHHCCCCCHHCC	70.61	26210075
287	Methylation	THKNPALKAQSGPVR HCCCCCHHCCCCCCC	46.62	24129315
287	Ubiquitination	THKNPALKAQSGPVR HCCCCCHHCCCCCCC	46.62	-
287	2-Hydroxyisobutyrylation	THKNPALKAQSGPVR HCCCCCHHCCCCCCC	46.62	-
287	Malonylation	THKNPALKAQSGPVR HCCCCCHHCCCCCCC	46.62	26320211
290	Phosphorylation	NPALKAQSGPVRSGP CCCHHCCCCCCCCCC	50.34	18669648
295	Phosphorylation	AQSGPVRSGPKPFSA CCCCCCCCCCCCCCC	60.73	30266825
298	Methylation	GPVRSGPKPFSAPKP CCCCCCCCCCCCCCC	63.32	-
298	Ubiquitination	GPVRSGPKPFSAPKP CCCCCCCCCCCCCCC	63.32	-
298	Acetylation	GPVRSGPKPFSAPKP CCCCCCCCCCCCCCC	63.32	23236377
298	Malonylation	GPVRSGPKPFSAPKP CCCCCCCCCCCCCCC	63.32	26320211
301	Phosphorylation	RSGPKPFSAPKPQTS CCCCCCCCCCCCCCC	52.79	23927012
304	Malonylation	PKPFSAPKPQTSPSP CCCCCCCCCCCCCCC	49.85	26320211
307	Phosphorylation	FSAPKPQTSPSPKRA CCCCCCCCCCCCCCC	51.65	22167270
308	Phosphorylation	SAPKPQTSPSPKRAT CCCCCCCCCCCCCCC	20.38	29255136
310	Phosphorylation	PKPQTSPSPKRATKK CCCCCCCCCCCCCCC	42.70	29255136
312	Acetylation	PQTSPSPKRATKKEP CCCCCCCCCCCCCCC	60.03	26051181
312	2-Hydroxyisobutyrylation	PQTSPSPKRATKKEP CCCCCCCCCCCCCCC	60.03	-
315	Phosphorylation	SPSPKRATKKEPAVL CCCCCCCCCCCCEEE	46.83	26074081
316	Malonylation	PSPKRATKKEPAVLE CCCCCCCCCCCEEEE	54.90	26320211
317	Ubiquitination	SPKRATKKEPAVLEL CCCCCCCCCCEEEEE	65.65	-
317	Malonylation	SPKRATKKEPAVLEL CCCCCCCCCCEEEEE	65.65	26320211
327	Ubiquitination	AVLELEGKKWRVENQ EEEEECCCEEEECCC	39.52	-
327	2-Hydroxyisobutyrylation	AVLELEGKKWRVENQ EEEEECCCEEEECCC	39.52	-
327	Malonylation	AVLELEGKKWRVENQ EEEEECCCEEEECCC	39.52	26320211
327	Acetylation	AVLELEGKKWRVENQ EEEEECCCEEEECCC	39.52	25953088
328	Ubiquitination	VLELEGKKWRVENQE EEEECCCEEEECCCH	51.60	-
338	Phosphorylation	VENQENVSNLVIEDT ECCCHHHCCEEECCC	35.71	25693802
348	Ubiquitination	VIEDTELKQVAYIYK EECCCHHHHHEHHHH	36.17	-
348	Sumoylation	VIEDTELKQVAYIYK EECCCHHHHHEHHHH	36.17	25114211
352	Phosphorylation	TELKQVAYIYKCVNT CHHHHHEHHHHHHCC	13.11	26356563
354	Phosphorylation	LKQVAYIYKCVNTTL HHHHEHHHHHHCCCE	5.90	21082442
359	Phosphorylation	YIYKCVNTTLQIKGK HHHHHHCCCEEECCE	14.42	23403867
360	Phosphorylation	IYKCVNTTLQIKGKI HHHHHCCCEEECCEE	16.09	23403867
364	2-Hydroxyisobutyrylation	VNTTLQIKGKINSIT HCCCEEECCEEEEEE	40.99	-
364	Acetylation	VNTTLQIKGKINSIT HCCCEEECCEEEEEE	40.99	25953088
366	Malonylation	TTLQIKGKINSITVD CCEEECCEEEEEEEC	33.44	26320211
366	Acetylation	TTLQIKGKINSITVD CCEEECCEEEEEEEC	33.44	25953088
376	Acetylation	SITVDNCKKLGLVFD EEEECCHHHHCCEEC	58.23	23236377
376	Malonylation	SITVDNCKKLGLVFD EEEECCHHHHCCEEC	58.23	26320211
398	Ubiquitination	IINSKDVKVQVMGKV EECCCCCEEEEEEEC	36.76	-
398	Acetylation	IINSKDVKVQVMGKV EECCCCCEEEEEEEC	36.76	25953088
404	Ubiquitination	VKVQVMGKVPTISIN CEEEEEEECCEEEEE	27.26	-
404	Malonylation	VKVQVMGKVPTISIN CEEEEEEECCEEEEE	27.26	26320211
404	Acetylation	VKVQVMGKVPTISIN CEEEEEEECCEEEEE	27.26	25953088
407	Phosphorylation	QVMGKVPTISINKTD EEEEECCEEEEECCC	30.28	-
409	Phosphorylation	MGKVPTISINKTDGC EEECCEEEEECCCCC	23.68	21712546
411 (in isoform 2)	Ubiquitination	-	34.09	21890473
412	Acetylation	VPTISINKTDGCHAY CCEEEEECCCCCEEE	46.45	23749302
412	Ubiquitination	VPTISINKTDGCHAY CCEEEEECCCCCEEE	46.45	21890473
412	2-Hydroxyisobutyrylation	VPTISINKTDGCHAY CCEEEEECCCCCEEE	46.45	-
412	Malonylation	VPTISINKTDGCHAY CCEEEEECCCCCEEE	46.45	26320211
412 (in isoform 1)	Ubiquitination	-	46.45	21890473
413	Phosphorylation	PTISINKTDGCHAYL CEEEEECCCCCEEEE	32.89	28152594
419	Phosphorylation	KTDGCHAYLSKNSLD CCCCCEEEECCCCCC	6.45	28152594
419	Nitration	KTDGCHAYLSKNSLD CCCCCEEEECCCCCC	6.45	-
421	Phosphorylation	DGCHAYLSKNSLDCE CCCEEEECCCCCCCE	19.67	28152594
422	Ubiquitination	GCHAYLSKNSLDCEI CCEEEECCCCCCCEE	48.21	-
422	Malonylation	GCHAYLSKNSLDCEI CCEEEECCCCCCCEE	48.21	26320211
422	Acetylation	GCHAYLSKNSLDCEI CCEEEECCCCCCCEE	48.21	25953088
424	Phosphorylation	HAYLSKNSLDCEIVS EEEECCCCCCCEEEE	29.35	21712546
427	Glutathionylation	LSKNSLDCEIVSAKS ECCCCCCCEEEEECC	4.69	22555962
431	Phosphorylation	SLDCEIVSAKSSEMN CCCCEEEEECCCCCE	35.32	21712546
434	Phosphorylation	CEIVSAKSSEMNVLI CEEEEECCCCCEEEE	31.11	28450419
435	Phosphorylation	EIVSAKSSEMNVLIP EEEEECCCCCEEEEE	39.91	28450419
437	Sulfoxidation	VSAKSSEMNVLIPTE EEECCCCCEEEEECC	4.55	30846556
443	Phosphorylation	EMNVLIPTEGGDFNE CCEEEEECCCCCCCC	40.02	28450419
458	Acetylation	FPVPEQFKTLWNGQK CCCCHHHHHHHCCCE	42.26	7960469
459	O-linked_Glycosylation	PVPEQFKTLWNGQKL CCCHHHHHHHCCCEE	37.99	28510447

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
308	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
310	S	Phosphorylation	Kinase	GSK3B	P49841	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CAP1_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 CAP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAG6_MOUSE	Bag6	physical	8761950
CAP1_MOUSE	Cap1	physical	8761950
CAP1_HUMAN	CAP1	physical	8761950
CAP2_HUMAN	CAP2	physical	8761950
ACTG_HUMAN	ACTG1	physical	8761950
PSME2_HUMAN	PSME2	physical	22939629
ML12A_HUMAN	MYL12A	physical	22939629
HTRA2_HUMAN	HTRA2	physical	22939629
ABI2_HUMAN	ABI2	physical	22863883
FAS_HUMAN	FASN	physical	22863883
HS90A_HUMAN	HSP90AA1	physical	22863883
HS90B_HUMAN	HSP90AB1	physical	22863883
MCM2_HUMAN	MCM2	physical	22863883
MCM3_HUMAN	MCM3	physical	22863883
MCM4_HUMAN	MCM4	physical	22863883
MCM6_HUMAN	MCM6	physical	22863883
OGA_HUMAN	MGEA5	physical	22863883
TPM3_HUMAN	TPM3	physical	22863883
DPH2_HUMAN	DPH2	physical	26344197
DPYL2_HUMAN	DPYSL2	physical	26344197
NPL4_HUMAN	NPLOC4	physical	26344197
RNH2C_HUMAN	RNASEH2C	physical	26344197
TTC38_HUMAN	TTC38	physical	26344197
ACTS_HUMAN	ACTA1	physical	28514442
CAP2_HUMAN	CAP2	physical	28514442
POTEI_HUMAN	POTEI	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
ACTB_HUMAN	ACTB	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 CAP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-308, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.	12665801 [Abstract]
"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-81 AND LYS-209, AND MASSSPECTROMETRY.	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-310, AND MASSSPECTROMETRY.	19690332 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-308, AND MASS SPECTROMETRY.	19413330 [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-290; SER-295; SER-301;THR-307; SER-308 AND SER-310, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307 AND SER-310, ANDMASS SPECTROMETRY.	17924679 [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 TYR-164, AND MASSSPECTROMETRY.	16807684 [Abstract]