CORO6_HUMAN - dbPTM
CORO6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CORO6_HUMAN
UniProt AC Q6QEF8
Protein Name Coronin-6
Gene Name CORO6
Organism Homo sapiens (Human).
Sequence Length 472
Subcellular Localization
Protein Description
Protein Sequence MSRRVVRQSKFRHVFGQAAKADQAYEDIRVSKVTWDSSFCAVNPKFLAIIVEAGGGGAFIVLPLAKTGRVDKNYPLVTGHTAPVLDIDWCPHNDNVIASASDDTTIMVWQIPDYTPMRNITEPIITLEGHSKRVGILSWHPTARNVLLSAGGDNVIIIWNVGTGEVLLSLDDMHPDVIHSVCWNSNGSLLATTCKDKTLRIIDPRKGQVVAEQARPHEGARPLRAVFTADGKLLSTGFSRMSERQLALWDPNNFEEPVALQEMDTSNGVLLPFYDPDSSIVYLCGKGDSSIRYFEITDEPPFVHYLNTFSSKEPQRGMGFMPKRGLDVSKCEIARFYKLHERKCEPIIMTVPRKSDLFQDDLYPDTPGPEPALEADEWLSGQDAEPVLISLRDGYVPPKHRELRVTKRNILDVRPPSGPRRSQSASDAPLSQQHTLETLLEEIKALRERVQAQEQRITALENMLCELVDGTD
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
2Phosphorylation------MSRRVVRQS
------CCHHHHHHH
28.8822210691
188 (in isoform 4)Phosphorylation-25.1826437602
190 (in isoform 4)Phosphorylation-4.2126437602
228 (in isoform 5)Phosphorylation-19.7620068231
235 (in isoform 5)Phosphorylation-36.6020068231
236PhosphorylationADGKLLSTGFSRMSE
CCCCEEECCCCCCCH
42.0623612710
236 (in isoform 5)Phosphorylation-42.0620068231
236 (in isoform 3)Phosphorylation-42.0626437602
238 (in isoform 3)Phosphorylation-4.1926437602
239PhosphorylationKLLSTGFSRMSERQL
CEEECCCCCCCHHHH
28.5520068231
239 (in isoform 5)Phosphorylation-28.5520068231
242 (in isoform 5)Phosphorylation-28.6320068231
312AcetylationYLNTFSSKEPQRGMG
EECCCCCCCCCCCCC
72.6926051181
338UbiquitinationCEIARFYKLHERKCE
HHHHHHHHHHHCCCE
40.43-
338AcetylationCEIARFYKLHERKCE
HHHHHHHHHHHCCCE
40.4326051181
344S-nitrosylationYKLHERKCEPIIMTV
HHHHHCCCEEEEEEC
10.612212679
417PhosphorylationILDVRPPSGPRRSQS
EECCCCCCCCCCCCC
65.2016674116
422PhosphorylationPPSGPRRSQSASDAP
CCCCCCCCCCCCCCC
29.7522673903
424PhosphorylationSGPRRSQSASDAPLS
CCCCCCCCCCCCCCC
30.8722673903
426PhosphorylationPRRSQSASDAPLSQQ
CCCCCCCCCCCCCHH
39.2822673903
431PhosphorylationSASDAPLSQQHTLET
CCCCCCCCHHHHHHH
27.0822673903
435PhosphorylationAPLSQQHTLETLLEE
CCCCHHHHHHHHHHH
23.1922673903
438PhosphorylationSQQHTLETLLEEIKA
CHHHHHHHHHHHHHH
39.4927542207

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 CORO6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CORO6_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 CORO6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COR1A_HUMANCORO1Aphysical
28514442
COR1C_HUMANCORO1Cphysical
28514442
UACA_HUMANUACAphysical
28514442
TARA_HUMANTRIOBPphysical
28514442
TACC3_HUMANTACC3physical
28514442
NBR1_HUMANNBR1physical
28514442
COR1B_HUMANCORO1Bphysical
28514442
POC1A_HUMANPOC1Aphysical
28514442
CSR2B_HUMANCSRP2BPphysical
28514442
CI016_HUMANC9orf16physical
28514442
TIGD5_HUMANTIGD5physical
28514442
PCGF6_HUMANPCGF6physical
28514442
TNIP1_HUMANTNIP1physical
28514442
IFT81_HUMANIFT81physical
28514442
ZN318_HUMANZNF318physical
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 CORO6_HUMAN

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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-338, AND MASS SPECTROMETRY.

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