COTL1_HUMAN - dbPTM
COTL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COTL1_HUMAN
UniProt AC Q14019
Protein Name Coactosin-like protein
Gene Name COTL1
Organism Homo sapiens (Human).
Sequence Length 142
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Nucleus .
Protein Description Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis..
Protein Sequence MATKIDKEACRAAYNLVRDDGSAVIWVTFKYDGSTIVPGEQGAEYQHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGENVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIKSELKKAGGANYDAQTE
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------MATKIDKEA
------CCCHHCHHH		20.0122814378
4Acetylation----MATKIDKEACR
----CCCHHCHHHHH		39.0921339330
4Ubiquitination----MATKIDKEACR
----CCCHHCHHHHH		39.09-
4Malonylation----MATKIDKEACR
----CCCHHCHHHHH		39.0926320211
72-Hydroxyisobutyrylation-MATKIDKEACRAAY
-CCCHHCHHHHHHHH		51.16-
7Acetylation-MATKIDKEACRAAY
-CCCHHCHHHHHHHH		51.1623749302
7Ubiquitination-MATKIDKEACRAAY
-CCCHHCHHHHHHHH		51.16-
14PhosphorylationKEACRAAYNLVRDDG
HHHHHHHHHHHCCCC		14.1928152594
57MethylationQQCTDDVRLFAFVRF
HHCCCCCEEEEEEEE		30.96-
70SulfoxidationRFTTGDAMSKRSKFA
EEECCCHHCHHHHEE		6.0530846556
71PhosphorylationFTTGDAMSKRSKFAL
EECCCHHCHHHHEEE		27.0029255136
72AcetylationTTGDAMSKRSKFALI
ECCCHHCHHHHEEEE		47.8323236377
72UbiquitinationTTGDAMSKRSKFALI
ECCCHHCHHHHEEEE		47.83-
722-HydroxyisobutyrylationTTGDAMSKRSKFALI
ECCCHHCHHHHEEEE		47.83-
72MalonylationTTGDAMSKRSKFALI
ECCCHHCHHHHEEEE		47.8326320211
75AcetylationDAMSKRSKFALITWI
CHHCHHHHEEEEEEC		38.3925953088
98AcetylationRAKTGTDKTLVKEVV
HCCCCCCHHHHHHHH		43.5325953088
98MalonylationRAKTGTDKTLVKEVV
HCCCCCCHHHHHHHH		43.5326320211
98UbiquitinationRAKTGTDKTLVKEVV
HCCCCCCHHHHHHHH		43.53-
982-HydroxyisobutyrylationRAKTGTDKTLVKEVV
HCCCCCCHHHHHHHH		43.53-
102SuccinylationGTDKTLVKEVVQNFA
CCCHHHHHHHHHHHH		48.1523954790
102UbiquitinationGTDKTLVKEVVQNFA
CCCHHHHHHHHHHHH		48.1519608861
1022-HydroxyisobutyrylationGTDKTLVKEVVQNFA
CCCHHHHHHHHHHHH		48.15-
102AcetylationGTDKTLVKEVVQNFA
CCCHHHHHHHHHHHH		48.1519608861
110UbiquitinationEVVQNFAKEFVISDR
HHHHHHHHHHHCCCH		47.7719608861
110SuccinylationEVVQNFAKEFVISDR
HHHHHHHHHHHCCCH		47.7723954790
110AcetylationEVVQNFAKEFVISDR
HHHHHHHHHHHCCCH		47.7719608861
115PhosphorylationFAKEFVISDRKELEE
HHHHHHCCCHHHHHH		26.5116097034
117MethylationKEFVISDRKELEEDF
HHHHCCCHHHHHHHH		27.79-
118UbiquitinationEFVISDRKELEEDFI
HHHCCCHHHHHHHHH		72.19-
1182-HydroxyisobutyrylationEFVISDRKELEEDFI
HHHCCCHHHHHHHHH		72.19-
118MalonylationEFVISDRKELEEDFI
HHHCCCHHHHHHHHH		72.1926320211
1262-HydroxyisobutyrylationELEEDFIKSELKKAG
HHHHHHHHHHHHHCC		37.56-
126SuccinylationELEEDFIKSELKKAG
HHHHHHHHHHHHHCC		37.5623954790
126UbiquitinationELEEDFIKSELKKAG
HHHHHHHHHHHHHCC		37.5619608861
126SumoylationELEEDFIKSELKKAG
HHHHHHHHHHHHHCC		37.5619608861
126SumoylationELEEDFIKSELKKAG
HHHHHHHHHHHHHCC		37.56-
126AcetylationELEEDFIKSELKKAG
HHHHHHHHHHHHHCC		37.5619608861
127PhosphorylationLEEDFIKSELKKAGG
HHHHHHHHHHHHCCC		43.2628060719
130UbiquitinationDFIKSELKKAGGANY
HHHHHHHHHCCCCCC		36.20-
130AcetylationDFIKSELKKAGGANY
HHHHHHHHHCCCCCC		36.2023749302
131UbiquitinationFIKSELKKAGGANYD
HHHHHHHHCCCCCCC		65.96-
137PhosphorylationKKAGGANYDAQTE--
HHCCCCCCCCCCC--		16.4828796482
141PhosphorylationGANYDAQTE------
CCCCCCCCC------		45.4428985074
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 COTL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COTL1_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 COTL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LOX5_HUMANALOX5physical
11297527
ACTS_HUMANACTA1physical
11297527
ACTG_HUMANACTG1physical
11297527
ACTB_HUMANACTBphysical
11583571
LOX5_HUMANALOX5physical
19807693
GDIR1_HUMANARHGDIAphysical
26344197
COF1_HUMANCFL1physical
26344197
CRIP1_HUMANCRIP1physical
26344197
DUT_HUMANDUTphysical
26344197
JUPI1_HUMANHN1physical
26344197
MDHM_HUMANMDH2physical
26344197
PCBP1_HUMANPCBP1physical
26344197
SH3L1_HUMANSH3BGRLphysical
26344197
TAGL2_HUMANTAGLN2physical
26344197
TIAR_HUMANTIAL1physical
26344197
TKT_HUMANTKTphysical
26344197
UBC12_HUMANUBE2Mphysical
26344197
LOX5_HUMANALOX5physical
16924104
LOX5_HUMANALOX5physical
19579006
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 COTL1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-102 AND LYS-126, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory