CORO7_HUMAN - dbPTM
CORO7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CORO7_HUMAN
UniProt AC P57737
Protein Name Coronin-7
Gene Name CORO7
Organism Homo sapiens (Human).
Sequence Length 925
Subcellular Localization Golgi apparatus membrane. Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle. Cytoplasm, cytosol. Predominantly cytosolic. Detected on vesicle-like cytoplasmic structures and on the cis-Golgi. Not associated with actin filaments.
Protein Description F-actin regulator involved in anterograde Golgi to endosome transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and localizes to the trans-Golgi network, where it promotes actin polymerization, thereby facilitating post-Golgi trafficking. May play a role in the maintenance of the Golgi apparatus morphology..
Protein Sequence MNRFRVSKFRHTEARPPRRESWISDIRAGTAPSCRNHIKSSCSLIAFNSDRPGVLGIVPLQGQGEDKRRVAHLGCHSDLVTDLDFSPFDDFLLATGSADRTVKLWRLPGPGQALPSAPGVVLGPEDLPVEVLQFHPTSDGILVSAAGTTVKVWDAAKQQPLTELAAHGDLVQSAVWSRDGALVGTACKDKQLRIFDPRTKPRASQSTQAHENSRDSRLAWMGTWEHLVSTGFNQMREREVKLWDTRFFSSALASLTLDTSLGCLVPLLDPDSGLLVLAGKGERQLYCYEVVPQQPALSPVTQCVLESVLRGAALVPRQALAVMSCEVLRVLQLSDTAIVPIGYHVPRKAVEFHEDLFPDTAGCVPATDPHSWWAGDNQQVQKVSLNPACRPHPSFTSCLVPPAEPLPDTAQPAVMETPVGDADASEGFSSPPSSLTSPSTPSSLGPSLSSTSGIGTSPSLRSLQSLLGPSSKFRHAQGTVLHRDSHITNLKGLNLTTPGESDGFCANKLRVAVPLLSSGGQVAVLELRKPGRLPDTALPTLQNGAAVTDLAWDPFDPHRLAVAGEDARIRLWRVPAEGLEEVLTTPETVLTGHTEKICSLRFHPLAANVLASSSYDLTVRIWDLQAGADRLKLQGHQDQIFSLAWSPDGQQLATVCKDGRVRVYRPRSGPEPLQEGPGPKGGRGARIVWVCDGRCLLVSGFDSQSERQLLLYEAEALAGGPLAVLGLDVAPSTLLPSYDPDTGLVLLTGKGDTRVFLYELLPESPFFLECNSFTSPDPHKGLVLLPKTECDVREVELMRCLRLRQSSLEPVAFRLPRVRKEFFQDDVFPDTAVIWEPVLSAEAWLQGANGQPWLLSLQPPDMSPVSQAPREAPARRAPSSAQYLEEKSDQQKKEELLNAMVAKLGNREDPLPQDSFEGVDEDEWD
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
21PhosphorylationARPPRRESWISDIRA
CCCCCCHHHHHHHHC
28.0923401153
21 (in isoform 3)Phosphorylation-28.0924719451
24PhosphorylationPRRESWISDIRAGTA
CCCHHHHHHHHCCCC
22.2623403867
24 (in isoform 3)Phosphorylation-22.2627251275
40PhosphorylationSCRNHIKSSCSLIAF
HHHHHHHHCCEEEEE
35.6524247654
41PhosphorylationCRNHIKSSCSLIAFN
HHHHHHHCCEEEEEC
11.6127251275
43PhosphorylationNHIKSSCSLIAFNSD
HHHHHCCEEEEECCC
25.4328857561
43 (in isoform 3)Phosphorylation-25.4327251275
67UbiquitinationLQGQGEDKRRVAHLG
CCCCCCCCCCEEECC
37.4929967540
103UbiquitinationGSADRTVKLWRLPGP
CCCCCEEEEEECCCC
41.5422817900
105UbiquitinationADRTVKLWRLPGPGQ
CCCEEEEEECCCCCC
8.2722817900
139UbiquitinationLQFHPTSDGILVSAA
EEECCCCCCEEEECC
51.1029967540
157UbiquitinationVKVWDAAKQQPLTEL
EEEHHHHHCCCHHHH
51.7129967540
170UbiquitinationELAAHGDLVQSAVWS
HHHHCCCHHHHHHHC
4.4622817900
172UbiquitinationAAHGDLVQSAVWSRD
HHCCCHHHHHHHCCC
32.7322817900
188UbiquitinationALVGTACKDKQLRIF
CEEEEEECCCCEEEE
66.5521906983
190UbiquitinationVGTACKDKQLRIFDP
EEEEECCCCEEEECC
36.4122817900
241UbiquitinationQMREREVKLWDTRFF
HHHHHHHHHHHHHHH
38.82-
242PhosphorylationMREREVKLWDTRFFS
HHHHHHHHHHHHHHH
6.3832142685
252UbiquitinationTRFFSSALASLTLDT
HHHHHHHHHHCHHCC
3.4330230243
263UbiquitinationTLDTSLGCLVPLLDP
HHCCCCCCEEEEECC
4.1429967540
288PhosphorylationGERQLYCYEVVPQQP
CCEEEEEEEECCCCC
9.7522817900
288UbiquitinationGERQLYCYEVVPQQP
CCEEEEEEEECCCCC
9.7530230243
297UbiquitinationVVPQQPALSPVTQCV
ECCCCCCCCHHHHHH
8.2829967540
330UbiquitinationMSCEVLRVLQLSDTA
HHHHHHHHCCCCCCE
3.3229967540
348UbiquitinationIGYHVPRKAVEFHED
CCEECCHHHHHHCHH
51.1929967540
364UbiquitinationFPDTAGCVPATDPHS
CCCCCCCEECCCCCC
3.3729967540
376UbiquitinationPHSWWAGDNQQVQKV
CCCCCCCCCCCEEEE
41.8530230243
377PhosphorylationHSWWAGDNQQVQKVS
CCCCCCCCCCEEEEE
33.0132142685
382UbiquitinationGDNQQVQKVSLNPAC
CCCCCEEEEECCCCC
34.6329967540
387AcetylationVQKVSLNPACRPHPS
EEEEECCCCCCCCCC
37.7219608861
387UbiquitinationVQKVSLNPACRPHPS
EEEEECCCCCCCCCC
37.7223000965
387 (in isoform 2)Ubiquitination-37.7221890473
406UbiquitinationLVPPAEPLPDTAQPA
CCCCCCCCCCCCCCE
4.5122817900
423UbiquitinationETPVGDADASEGFSS
ECCCCCCCCCCCCCC
56.2022817900
444PhosphorylationSPSTPSSLGPSLSST
CCCCCHHCCCCCCCC
15.9732142685
454AcetylationSLSSTSGIGTSPSLR
CCCCCCCCCCCHHHH
5.6519608861
454UbiquitinationSLSSTSGIGTSPSLR
CCCCCCCCCCCHHHH
5.6523000965
460UbiquitinationGIGTSPSLRSLQSLL
CCCCCHHHHHHHHHH
4.9730230243
462PhosphorylationGTSPSLRSLQSLLGP
CCCHHHHHHHHHHCC
35.7330576142
462 (in isoform 3)Phosphorylation-35.7324719451
465PhosphorylationPSLRSLQSLLGPSSK
HHHHHHHHHHCCCHH
30.7523401153
465 (in isoform 3)Phosphorylation-30.7524719451
470PhosphorylationLQSLLGPSSKFRHAQ
HHHHHCCCHHHHCCC
44.3428857561
470 (in isoform 3)Phosphorylation-44.3427251275
471PhosphorylationQSLLGPSSKFRHAQG
HHHHCCCHHHHCCCC
38.6628857561
472UbiquitinationSLLGPSSKFRHAQGT
HHHCCCHHHHCCCCC
51.2421890473
472AcetylationSLLGPSSKFRHAQGT
HHHCCCHHHHCCCCC
51.2419608861
472UbiquitinationSLLGPSSKFRHAQGT
HHHCCCHHHHCCCCC
51.2423000965
472 (in isoform 1)Ubiquitination-51.2421890473
473UbiquitinationLLGPSSKFRHAQGTV
HHCCCHHHHCCCCCE
8.1622817900
479PhosphorylationKFRHAQGTVLHRDSH
HHHCCCCCEECCCCC
14.0728857561
485PhosphorylationGTVLHRDSHITNLKG
CCEECCCCCCCCCCC
19.4228857561
490UbiquitinationRDSHITNLKGLNLTT
CCCCCCCCCCCCCCC
3.3122817900
491UbiquitinationDSHITNLKGLNLTTP
CCCCCCCCCCCCCCC
64.5221906983
508UbiquitinationSDGFCANKLRVAVPL
CCCCCCCCEEEEEEE
21.1021906983
511UbiquitinationFCANKLRVAVPLLSS
CCCCCEEEEEEEECC
10.2422817900
517PhosphorylationRVAVPLLSSGGQVAV
EEEEEEECCCCEEEE
34.3228348404
517 (in isoform 3)Phosphorylation-34.3227251275
518PhosphorylationVAVPLLSSGGQVAVL
EEEEEECCCCEEEEE
47.0820068231
529UbiquitinationVAVLELRKPGRLPDT
EEEEEECCCCCCCCC
65.53-
572UbiquitinationEDARIRLWRVPAEGL
CCCEEEEEECCCCCH
6.8629967540
578UbiquitinationLWRVPAEGLEEVLTT
EEECCCCCHHHHHCC
40.2622817900
584PhosphorylationEGLEEVLTTPETVLT
CCHHHHHCCCCEEEC
45.5423312004
584 (in isoform 3)Phosphorylation-45.5427251275
585PhosphorylationGLEEVLTTPETVLTG
CHHHHHCCCCEEECC
18.2430377224
587PhosphorylationEEVLTTPETVLTGHT
HHHHCCCCEEECCCC
49.8332142685
588PhosphorylationEVLTTPETVLTGHTE
HHHCCCCEEECCCCH
23.2423312004
595UbiquitinationTVLTGHTEKICSLRF
EEECCCCHHEEECCC
34.4522817900
596UbiquitinationVLTGHTEKICSLRFH
EECCCCHHEEECCCC
50.6021906983
612PhosphorylationLAANVLASSSYDLTV
HHHHHHHCCCCEEEE
18.6927251275
612 (in isoform 3)Phosphorylation-18.6927251275
613PhosphorylationAANVLASSSYDLTVR
HHHHHHCCCCEEEEE
27.5824247654
615PhosphorylationNVLASSSYDLTVRIW
HHHHCCCCEEEEEEE
19.54-
632UbiquitinationQAGADRLKLQGHQDQ
CCCCCEEEECCCHHH
39.39-
639UbiquitinationKLQGHQDQIFSLAWS
EECCCHHHEEEEEEC
31.8629967540
657UbiquitinationQQLATVCKDGRVRVY
CCEEEEECCCCEEEE
59.9029967540
662UbiquitinationVCKDGRVRVYRPRSG
EECCCCEEEECCCCC
20.5622817900
667UbiquitinationRVRVYRPRSGPEPLQ
CEEEECCCCCCCCCC
45.2932015554
668PhosphorylationVRVYRPRSGPEPLQE
EEEECCCCCCCCCCC
62.4730108239
680UbiquitinationLQEGPGPKGGRGARI
CCCCCCCCCCCCCEE
78.7821906983
702UbiquitinationCLLVSGFDSQSERQL
EEEEECCCCHHHHHH
49.6629967540
722PhosphorylationEALAGGPLAVLGLDV
HHHHCCCEEEECEEE
6.1032142685
758PhosphorylationGDTRVFLYELLPESP
CCCEEEEEECCCCCC
7.9622817900
764PhosphorylationLYELLPESPFFLECN
EEECCCCCCCEEECC
25.68-
769UbiquitinationPESPFFLECNSFTSP
CCCCCEEECCCCCCC
26.8829967540
772PhosphorylationPFFLECNSFTSPDPH
CCEEECCCCCCCCCC
41.3725627689
774PhosphorylationFLECNSFTSPDPHKG
EEECCCCCCCCCCCC
38.8925627689
775PhosphorylationLECNSFTSPDPHKGL
EECCCCCCCCCCCCE
25.8725627689
780UbiquitinationFTSPDPHKGLVLLPK
CCCCCCCCCEEEEEC
60.37-
787UbiquitinationKGLVLLPKTECDVRE
CCEEEEECCCCCHHH
57.8529967540
789PhosphorylationLVLLPKTECDVREVE
EEEEECCCCCHHHHH
34.5432142685
802UbiquitinationVELMRCLRLRQSSLE
HHHHHHHHHHHHCCC
31.3032015554
806PhosphorylationRCLRLRQSSLEPVAF
HHHHHHHHCCCCCHH
30.3823403867
806 (in isoform 3)Phosphorylation-30.3824719451
807PhosphorylationCLRLRQSSLEPVAFR
HHHHHHHCCCCCHHC
28.5423403867
808UbiquitinationLRLRQSSLEPVAFRL
HHHHHHCCCCCHHCC
11.9029967540
818UbiquitinationVAFRLPRVRKEFFQD
CHHCCHHHHHHHHCC
10.9421890473
818 (in isoform 2)Ubiquitination-10.9421890473
869UbiquitinationMSPVSQAPREAPARR
CCCCCCCCCCCCCCC
27.3232015554
875UbiquitinationAPREAPARRAPSSAQ
CCCCCCCCCCCCHHH
33.9529967540
879PhosphorylationAPARRAPSSAQYLEE
CCCCCCCCHHHHHHH
37.0025159151
879 (in isoform 3)Phosphorylation-37.0024719451
880PhosphorylationPARRAPSSAQYLEEK
CCCCCCCHHHHHHHH
20.5221815630
883PhosphorylationRAPSSAQYLEEKSDQ
CCCCHHHHHHHHCHH
18.7930108239
883 (in isoform 3)Phosphorylation-18.7927642862
885UbiquitinationPSSAQYLEEKSDQQK
CCHHHHHHHHCHHHH
59.4521890473
887UbiquitinationSAQYLEEKSDQQKKE
HHHHHHHHCHHHHHH
50.3832015554
892UbiquitinationEEKSDQQKKEELLNA
HHHCHHHHHHHHHHH
57.42-
893UbiquitinationEKSDQQKKEELLNAM
HHCHHHHHHHHHHHH
52.6729967540
900SulfoxidationKEELLNAMVAKLGNR
HHHHHHHHHHHHCCC
2.6821406390
903UbiquitinationLLNAMVAKLGNREDP
HHHHHHHHHCCCCCC
45.5821890473
903UbiquitinationLLNAMVAKLGNREDP
HHHHHHHHHCCCCCC
45.5822817900
903 (in isoform 1)Ubiquitination-45.5821890473
915PhosphorylationEDPLPQDSFEGVDED
CCCCCCCCCCCCCCC
21.6825159151
927 (in isoform 3)Phosphorylation--
989 (in isoform 3)Phosphorylation-27251275
992 (in isoform 3)Phosphorylation-24719451

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
288YPhosphorylationKinaseSRCP12931
PSP
758YPhosphorylationKinaseSRCP12931
PSP
-KUbiquitinationE3 ubiquitin ligaseKLHL20Q9Y2M5
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CORO7_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 CORO7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOB1_HUMANTOB1physical
21130766
DAG1_HUMANDAG1physical
22939629
ACTB_HUMANACTBphysical
24768539
EPS15_HUMANEPS15physical
24768539
JUN_HUMANJUNphysical
24768539
AP1G1_HUMANAP1G1physical
16905771

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 CORO7_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-472, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-915, 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-21 AND SER-915, AND MASSSPECTROMETRY.

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