CLCA_HUMAN - dbPTM
CLCA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLCA_HUMAN
UniProt AC P09496
Protein Name Clathrin light chain A
Gene Name CLTA
Organism Homo sapiens (Human).
Sequence Length 248
Subcellular Localization Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Membrane, coated pit
Peripheral membrane protein
Cytoplasmic side. Cytoplasm, cytoskeleton, spindle . Cytoplasmic face of coated pits and vesicles. In complex with TACC3 a
Protein Description Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. [PubMed: 15858577]
Protein Sequence MAELDPFGAPAGAPGGPALGNGVAGAGEEDPAAAFLAQQESEIAGIENDEAFAILDGGAPGPQPHGEPPGGPDAVDGVMNGEYYQESNGPTDSYAAISQVDRLQSEPESIRKWREEQMERLEALDANSRKQEAEWKEKAIKELEEWYARQDEQLQKTKANNRVADEAFYKQPFADVIGYVTNINHPCYSLEQAAEEAFVNDIDESSPGTEWERVARLCDFNPKSSKQAKDVSRMRSVLISLKQAPLVH
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
83PhosphorylationDGVMNGEYYQESNGP
CCCCCCCEEHHHCCC		16.3122817900
84PhosphorylationGVMNGEYYQESNGPT
CCCCCCEEHHHCCCC		11.0822817900
87PhosphorylationNGEYYQESNGPTDSY
CCCEEHHHCCCCCHH		31.4024275569
91PhosphorylationYQESNGPTDSYAAIS
EHHHCCCCCHHHHHH		38.69-
93PhosphorylationESNGPTDSYAAISQV
HHCCCCCHHHHHHHH		21.1024275569
94PhosphorylationSNGPTDSYAAISQVD
HCCCCCHHHHHHHHH		11.6722817900
105 (in isoform 2)Phosphorylation-60.7624719451
105 (in isoform 3)Phosphorylation-60.76-
105PhosphorylationSQVDRLQSEPESIRK
HHHHHHHCCCHHHHH		60.7619664994
109PhosphorylationRLQSEPESIRKWREE
HHHCCCHHHHHHHHH		38.1122167270
109 (in isoform 2)Phosphorylation-38.1121406692
109 (in isoform 3)Phosphorylation-38.11-
118SulfoxidationRKWREEQMERLEALD
HHHHHHHHHHHHHHC		3.5130846556
123 (in isoform 5)Phosphorylation-18.4829116813
124 (in isoform 5)Phosphorylation-4.7025849741
127 (in isoform 5)Phosphorylation-41.8529514088
128PhosphorylationLEALDANSRKQEAEW
HHHHCHHHHHHHHHH		42.4421712546
130UbiquitinationALDANSRKQEAEWKE
HHCHHHHHHHHHHHH		52.92-
141 (in isoform 1)Ubiquitination-62.1921890473
141UbiquitinationEWKEKAIKELEEWYA
HHHHHHHHHHHHHHH		62.1921890473
1412-HydroxyisobutyrylationEWKEKAIKELEEWYA
HHHHHHHHHHHHHHH		62.19-
141 (in isoform 2)Ubiquitination-62.1921890473
141 (in isoform 3)Ubiquitination-62.1921890473
141UbiquitinationEWKEKAIKELEEWYA
HHHHHHHHHHHHHHH		62.1921890473
147PhosphorylationIKELEEWYARQDEQL
HHHHHHHHHHHHHHH		8.6628796482
156AcetylationRQDEQLQKTKANNRV
HHHHHHHHHHHHCHH		61.6625953088
156UbiquitinationRQDEQLQKTKANNRV
HHHHHHHHHHHHCHH		61.66-
175 (in isoform 2)Phosphorylation-32.7129116813
176 (in isoform 2)Phosphorylation-3.0725849741
179 (in isoform 2)Phosphorylation-7.9329514088
194 (in isoform 3)Phosphorylation-18.17-
205PhosphorylationFVNDIDESSPGTEWE
HHHCCCCCCCCCHHH		37.7822167270
206 (in isoform 2)Phosphorylation-25.87-
206PhosphorylationVNDIDESSPGTEWER
HHCCCCCCCCCHHHH		25.8722167270
209PhosphorylationIDESSPGTEWERVAR
CCCCCCCCHHHHHHH		41.1122167270
212 (in isoform 2)Ubiquitination-30.92-
223AcetylationRLCDFNPKSSKQAKD
HHHCCCCCCCHHHHH		69.3526051181
223MalonylationRLCDFNPKSSKQAKD
HHHCCCCCCCHHHHH		69.3526320211
2232-HydroxyisobutyrylationRLCDFNPKSSKQAKD
HHHCCCCCCCHHHHH		69.35-
223MethylationRLCDFNPKSSKQAKD
HHHCCCCCCCHHHHH		69.35-
223UbiquitinationRLCDFNPKSSKQAKD
HHHCCCCCCCHHHHH		69.35-
224PhosphorylationLCDFNPKSSKQAKDV
HHCCCCCCCHHHHHH		43.9818691976
224 (in isoform 3)Phosphorylation-43.98-
226UbiquitinationDFNPKSSKQAKDVSR
CCCCCCCHHHHHHHH		62.46-
226MethylationDFNPKSSKQAKDVSR
CCCCCCCHHHHHHHH		62.46-
232PhosphorylationSKQAKDVSRMRSVLI
CHHHHHHHHHHHHHH		30.4129514088
236PhosphorylationKDVSRMRSVLISLKQ
HHHHHHHHHHHHHHH		16.3623911959
240PhosphorylationRMRSVLISLKQAPLV
HHHHHHHHHHHCCCC		25.9223403867
2422-HydroxyisobutyrylationRSVLISLKQAPLVH-
HHHHHHHHHCCCCC-		37.31-
242AcetylationRSVLISLKQAPLVH-
HHHHHHHHHCCCCC-		37.3123954790
242MalonylationRSVLISLKQAPLVH-
HHHHHHHHHCCCCC-		37.3126320211
242UbiquitinationRSVLISLKQAPLVH-
HHHHHHHHHCCCCC-		37.31-
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

Oops, there are no upstream regulatory protein records of CLCA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLCA_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 CLCA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP7C_HUMANHSPA8physical
1975516
MD2L2_HUMANMAD2L2physical
21152103
TERA_HUMANVCPphysical
8413590
RGS2_HUMANRGS2physical
21988832
CLH1_HUMANCLTCphysical
26344197
CLH2_HUMANCLTCL1physical
26344197
DP13A_HUMANAPPL1physical
27173435
CLCB_HUMANCLTBphysical
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 CLCA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-206, AND MASSSPECTROMETRY.
"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-206 AND SER-236, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-206 ANDSER-236, AND MASS SPECTROMETRY.

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