CAZA1_HUMAN - dbPTM
CAZA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAZA1_HUMAN
UniProt AC P52907
Protein Name F-actin-capping protein subunit alpha-1
Gene Name CAPZA1
Organism Homo sapiens (Human).
Sequence Length 286
Subcellular Localization Cytoplasm, cytoskeleton.
Protein Description F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions..
Protein Sequence MADFDDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVKIEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEADGGLKSWRESCDSALRAYVKDHYSNGFCTVYAKTIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSLTVSNEAQTAKEFIKIIENAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
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 Orthologous
Protein Cluster
2Acetylation------MADFDDRVS
------CCCCCCCCC		26.6119413330
7Methylation-MADFDDRVSDEEKV
-CCCCCCCCCHHHHH		31.51-
9PhosphorylationADFDDRVSDEEKVRI
CCCCCCCCHHHHHHH		39.9523401153
13UbiquitinationDRVSDEEKVRIAAKF
CCCCHHHHHHHHHHH		34.4623000965
19AcetylationEKVRIAAKFITHAPP
HHHHHHHHHHHCCCC		28.4219608861
19UbiquitinationEKVRIAAKFITHAPP
HHHHHHHHHHHCCCC		28.4223000965
19MalonylationEKVRIAAKFITHAPP
HHHHHHHHHHHCCCC		28.4226320211
57PhosphorylationAAHAFAQYNMDQFTP
HHHHHHHCCHHHCCC		14.7127080861
59SulfoxidationHAFAQYNMDQFTPVK
HHHHHCCHHHCCCEE		3.4930846556
63PhosphorylationQYNMDQFTPVKIEGY
HCCHHHCCCEEEECC		22.8729255136
66UbiquitinationMDQFTPVKIEGYEDQ
HHHCCCEEEECCCCE		35.9221963094
70PhosphorylationTPVKIEGYEDQVLIT
CCEEEECCCCEEEEE		11.98-
93UbiquitinationRFLDPRNKISFKFDH
CCCCCCCCEEEEHHH		40.7922817900
95PhosphorylationLDPRNKISFKFDHLR
CCCCCCEEEEHHHHH		24.8024719451
97AcetylationPRNKISFKFDHLRKE
CCCCEEEEHHHHHHC		42.9919608861
97UbiquitinationPRNKISFKFDHLRKE
CCCCEEEEHHHHHHC		42.9921906983
103UbiquitinationFKFDHLRKEASDPQP
EEHHHHHHCCCCCCC		65.0821906983
106PhosphorylationDHLRKEASDPQPEEA
HHHHHCCCCCCCHHC		51.4128450419
118UbiquitinationEEADGGLKSWRESCD
HHCCCCHHHHHHHHH		51.7723000965
118AcetylationEEADGGLKSWRESCD
HHCCCCHHHHHHHHH		51.7725953088
123PhosphorylationGLKSWRESCDSALRA
CHHHHHHHHHHHHHH		18.0427251275
131PhosphorylationCDSALRAYVKDHYSN
HHHHHHHHHHHHHCC		11.1230576142
133AcetylationSALRAYVKDHYSNGF
HHHHHHHHHHHCCCE		26.5526051181
133UbiquitinationSALRAYVKDHYSNGF
HHHHHHHHHHHCCCE		26.5521906983
137PhosphorylationAYVKDHYSNGFCTVY
HHHHHHHCCCEEEEE		27.3629496907
142PhosphorylationHYSNGFCTVYAKTID
HHCCCEEEEEEEEEC		17.8130576142
144PhosphorylationSNGFCTVYAKTIDGQ
CCCEEEEEEEEECCE		5.5729496907
157S-palmitoylationGQQTIIACIESHQFQ
CEEEEEEEEECCCCC		2.2129575903
160O-linked_GlycosylationTIIACIESHQFQPKN
EEEEEEECCCCCCCC		11.5929351928
166UbiquitinationESHQFQPKNFWNGRW
ECCCCCCCCCCCCCC		54.7321906983
178UbiquitinationGRWRSEWKFTITPPT
CCCCCEEEEEECCCC		28.6923000965
198PhosphorylationVLKIQVHYYEDGNVQ
EEEEEEEEEECCCEE		15.08-
210UbiquitinationNVQLVSHKDVQDSLT
CEEEEEECCCCCCEE		52.6829967540
215PhosphorylationSHKDVQDSLTVSNEA
EECCCCCCEEECCHH		14.6223911959
217PhosphorylationKDVQDSLTVSNEAQT
CCCCCCEEECCHHHH		26.3220071362
219PhosphorylationVQDSLTVSNEAQTAK
CCCCEEECCHHHHHH		24.5828102081
224PhosphorylationTVSNEAQTAKEFIKI
EECCHHHHHHHHHHH		46.9020071362
226UbiquitinationSNEAQTAKEFIKIIE
CCHHHHHHHHHHHHH		57.4521963094
226SuccinylationSNEAQTAKEFIKIIE
CCHHHHHHHHHHHHH		57.4523954790
226AcetylationSNEAQTAKEFIKIIE
CCHHHHHHHHHHHHH		57.4525953088
230UbiquitinationQTAKEFIKIIENAEN
HHHHHHHHHHHCCHH		42.8422817900
239PhosphorylationIENAENEYQTAISEN
HHCCHHHHHHHHHHC		23.81-
247PhosphorylationQTAISENYQTMSDTT
HHHHHHCCCCCCHHH		10.99-
250SulfoxidationISENYQTMSDTTFKA
HHHCCCCCCHHHHHH		1.6930846556
256UbiquitinationTMSDTTFKALRRQLP
CCCHHHHHHHHHHCC		44.4021906983
256MethylationTMSDTTFKALRRQLP
CCCHHHHHHHHHHCC		44.40-
268SumoylationQLPVTRTKIDWNKIL
HCCCCCCEECHHHHH		35.06-
268MalonylationQLPVTRTKIDWNKIL
HCCCCCCEECHHHHH		35.0626320211
268UbiquitinationQLPVTRTKIDWNKIL
HCCCCCCEECHHHHH		35.0623000965
268SumoylationQLPVTRTKIDWNKIL
HCCCCCCEECHHHHH		35.06-
273UbiquitinationRTKIDWNKILSYKIG
CCEECHHHHHHHHCH		40.5523000965
273SumoylationRTKIDWNKILSYKIG
CCEECHHHHHHHHCH		40.55-
273SumoylationRTKIDWNKILSYKIG
CCEECHHHHHHHHCH		40.5519608861
273MalonylationRTKIDWNKILSYKIG
CCEECHHHHHHHHCH		40.5526320211
273AcetylationRTKIDWNKILSYKIG
CCEECHHHHHHHHCH		40.5570453
277PhosphorylationDWNKILSYKIGKEMQ
CHHHHHHHHCHHHHH		11.81-
278SumoylationWNKILSYKIGKEMQN
HHHHHHHHCHHHHHC		41.42-
278UbiquitinationWNKILSYKIGKEMQN
HHHHHHHHCHHHHHC		41.4223000965
278MalonylationWNKILSYKIGKEMQN
HHHHHHHHCHHHHHC		41.4226320211
278AcetylationWNKILSYKIGKEMQN
HHHHHHHHCHHHHHC		41.427910605
278SumoylationWNKILSYKIGKEMQN
HHHHHHHHCHHHHHC		41.42-
281UbiquitinationILSYKIGKEMQNA--
HHHHHCHHHHHCC--		54.1921906983
288UbiquitinationKEMQNA---------
HHHHCC---------		22817900
300Ubiquitination---------------------
---------------------		23000965
305Ubiquitination--------------------------
--------------------------		23000965
310Ubiquitination-------------------------------
-------------------------------		23000965
313Ubiquitination----------------------------------
----------------------------------		22817900
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
9SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAZA1_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 CAZA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP7C_HUMANHSPA8physical
20884878
CAPZB_HUMANCAPZBphysical
22863883
CPIN1_HUMANCIAPIN1physical
22863883
ARP2_HUMANACTR2physical
26344197
RHG01_HUMANARHGAP1physical
26344197
ARPC2_HUMANARPC2physical
26344197
CAPZB_HUMANCAPZBphysical
26344197
MCFD2_HUMANMCFD2physical
26344197
MYO5C_HUMANMYO5Cphysical
26344197
NLRP9_HUMANNLRP9physical
26344197
PSA1_HUMANPSMA1physical
26344197
PSB6_HUMANPSMB6physical
26344197
ST1C3_HUMANSULT1C3physical
26344197
DCTN2_HUMANDCTN2physical
27173435
DCTN1_HUMANDCTN1physical
27173435
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 CAZA1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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, AND MASS SPECTROMETRY.
"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-19 AND LYS-97, AND MASSSPECTROMETRY.

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