EXOC2_HUMAN - dbPTM
EXOC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXOC2_HUMAN
UniProt AC Q96KP1
Protein Name Exocyst complex component 2
Gene Name EXOC2
Organism Homo sapiens (Human).
Sequence Length 924
Subcellular Localization Midbody, Midbody ring . Recruitment to the midbody does not require RALA, nor RALB (PubMed:18756269). Colocalizes with CNTRL/centriolin at the midbody ring (PubMed:16213214).
Protein Description Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane..
Protein Sequence MSRSRQPPLVTGISPNEGIPWTKVTIRGENLGTGPTDLIGLTICGHNCLLTAEWMSASKIVCRVGQAKNDKGDIIVTTKSGGRGTSTVSFKLLKPEKIGILDQSAVWVDEMNYYDMRTDRNKGIPPLSLRPANPLGIEIEKSKFSQKDLEMLFHGMSADFTSENFSAAWYLIENHSNTSFEQLKMAVTNLKRQANKKSEGSLAYVKGGLSTFFEAQDALSAIHQKLEADGTEKVEGSMTQKLENVLNRASNTADTLFQEVLGRKDKADSTRNALNVLQRFKFLFNLPLNIERNIQKGDYDVVINDYEKAKSLFGKTEVQVFKKYYAEVETRIEALRELLLDKLLETPSTLHDQKRYIRYLSDLHASGDPAWQCIGAQHKWILQLMHSCKEGYVKDLKGNPGLHSPMLDLDNDTRPSVLGHLSQTASLKRGSSFQSGRDDTWRYKTPHRVAFVEKLTKLVLSQLPNFWKLWISYVNGSLFSETAEKSGQIERSKNVRQRQNDFKKMIQEVMHSLVKLTRGALLPLSIRDGEAKQYGGWEVKCELSGQWLAHAIQTVRLTHESLTALEIPNDLLQTIQDLILDLRVRCVMATLQHTAEEIKRLAEKEDWIVDNEGLTSLPCQFEQCIVCSLQSLKGVLECKPGEASVFQQPKTQEEVCQLSINIMQVFIYCLEQLSTKPDADIDTTHLSVDVSSPDLFGSIHEDFSLTSEQRLLIVLSNCCYLERHTFLNIAEHFEKHNFQGIEKITQVSMASLKELDQRLFENYIELKADPIVGSLEPGIYAGYFDWKDCLPPTGVRNYLKEALVNIIAVHAEVFTISKELVPRVLSKVIEAVSEELSRLMQCVSSFSKNGALQARLEICALRDTVAVYLTPESKSSFKQALEALPQLSSGADKKLLEELLNKFKSSMHLQLTCFQAASSTMMKT
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
25PhosphorylationGIPWTKVTIRGENLG
CCCCEEEEECCCCCC		13.4024719451
68UbiquitinationVCRVGQAKNDKGDII
EEEHHCCCCCCCCEE		58.76-
71UbiquitinationVGQAKNDKGDIIVTT
HHCCCCCCCCEEEEE		68.80-
79UbiquitinationGDIIVTTKSGGRGTS
CCEEEEECCCCCCEE		37.42-
83MethylationVTTKSGGRGTSTVSF
EEECCCCCCEEEEEE		49.06115493575
89PhosphorylationGRGTSTVSFKLLKPE
CCCEEEEEEEECCHH		19.42-
113PhosphorylationVWVDEMNYYDMRTDR
EEEECCCCEECCCCC		10.2622817900
122UbiquitinationDMRTDRNKGIPPLSL
ECCCCCCCCCCCCCC		60.14-
143UbiquitinationGIEIEKSKFSQKDLE
CCEEEECCCCHHHHH		61.17-
191UbiquitinationKMAVTNLKRQANKKS
HHHHHHHHHHHCCCC		44.53-
197UbiquitinationLKRQANKKSEGSLAY
HHHHHCCCCCCCEEE		54.25-
198PhosphorylationKRQANKKSEGSLAYV
HHHHCCCCCCCEEEE		49.1224719451
201PhosphorylationANKKSEGSLAYVKGG
HCCCCCCCEEEECCC		13.0328122231
204PhosphorylationKSEGSLAYVKGGLST
CCCCCEEEECCCHHH		14.1624719451
206UbiquitinationEGSLAYVKGGLSTFF
CCCEEEECCCHHHHH		34.29-
210PhosphorylationAYVKGGLSTFFEAQD
EEECCCHHHHHHHHH		26.8328122231
211PhosphorylationYVKGGLSTFFEAQDA
EECCCHHHHHHHHHH		37.0728122231
225UbiquitinationALSAIHQKLEADGTE
HHHHHHHHHHCCCCC		33.85-
231PhosphorylationQKLEADGTEKVEGSM
HHHHCCCCCCCCCHH		32.9329083192
233UbiquitinationLEADGTEKVEGSMTQ
HHCCCCCCCCCHHHH		45.4821890473
237PhosphorylationGTEKVEGSMTQKLEN
CCCCCCCHHHHHHHH		12.7329083192
239PhosphorylationEKVEGSMTQKLENVL
CCCCCHHHHHHHHHH		25.0129083192
241UbiquitinationVEGSMTQKLENVLNR
CCCHHHHHHHHHHHH		48.9121890473
250PhosphorylationENVLNRASNTADTLF
HHHHHHHHHHHHHHH		31.3228122231
252PhosphorylationVLNRASNTADTLFQE
HHHHHHHHHHHHHHH		24.3428122231
255PhosphorylationRASNTADTLFQEVLG
HHHHHHHHHHHHHHC		27.3228122231
281UbiquitinationLNVLQRFKFLFNLPL
HHHHHHHHHHHCCCC		43.26-
296UbiquitinationNIERNIQKGDYDVVI
CHHHHHHCCCCEEEE		50.3721890473
296UbiquitinationNIERNIQKGDYDVVI
CHHHHHHCCCCEEEE		50.3721890473
299PhosphorylationRNIQKGDYDVVINDY
HHHHCCCCEEEECCH		21.2127642862
308UbiquitinationVVINDYEKAKSLFGK
EEECCHHHHHHHHCC		55.6821890473
310UbiquitinationINDYEKAKSLFGKTE
ECCHHHHHHHHCCCC		59.78-
315UbiquitinationKAKSLFGKTEVQVFK
HHHHHHCCCCHHHHH		33.89-
322UbiquitinationKTEVQVFKKYYAEVE
CCCHHHHHHHHHHHH		40.80-
323UbiquitinationTEVQVFKKYYAEVET
CCHHHHHHHHHHHHH		31.84-
325PhosphorylationVQVFKKYYAEVETRI
HHHHHHHHHHHHHHH		12.7429496907
342UbiquitinationLRELLLDKLLETPST
HHHHHHHHHHCCCCC		55.74-
342AcetylationLRELLLDKLLETPST
HHHHHHHHHHCCCCC		55.7418584595
3542-HydroxyisobutyrylationPSTLHDQKRYIRYLS
CCCHHHHHHHHHHHH		53.91-
354MalonylationPSTLHDQKRYIRYLS
CCCHHHHHHHHHHHH		53.9126320211
354AcetylationPSTLHDQKRYIRYLS
CCCHHHHHHHHHHHH		53.9125953088
354UbiquitinationPSTLHDQKRYIRYLS
CCCHHHHHHHHHHHH		53.91-
361PhosphorylationKRYIRYLSDLHASGD
HHHHHHHHHHHHCCC		29.23-
392PhosphorylationMHSCKEGYVKDLKGN
HHHCCCCCCCCCCCC		12.8622461510
394UbiquitinationSCKEGYVKDLKGNPG
HCCCCCCCCCCCCCC		49.19-
404PhosphorylationKGNPGLHSPMLDLDN
CCCCCCCCCCCCCCC		19.6325159151
413PhosphorylationMLDLDNDTRPSVLGH
CCCCCCCCCHHHHHH		51.2220873877
416PhosphorylationLDNDTRPSVLGHLSQ
CCCCCCHHHHHHHHC		27.0420873877
422PhosphorylationPSVLGHLSQTASLKR
HHHHHHHHCCCCCCC		21.5825159151
424PhosphorylationVLGHLSQTASLKRGS
HHHHHHCCCCCCCCC		18.1629255136
426PhosphorylationGHLSQTASLKRGSSF
HHHHCCCCCCCCCCC		37.5029255136
428UbiquitinationLSQTASLKRGSSFQS
HHCCCCCCCCCCCCC		52.82-
431PhosphorylationTASLKRGSSFQSGRD
CCCCCCCCCCCCCCC		31.8223927012
432PhosphorylationASLKRGSSFQSGRDD
CCCCCCCCCCCCCCC		30.0823927012
435PhosphorylationKRGSSFQSGRDDTWR
CCCCCCCCCCCCCCC		33.5123401153
440PhosphorylationFQSGRDDTWRYKTPH
CCCCCCCCCCCCCHH		19.0122115753
454UbiquitinationHRVAFVEKLTKLVLS
HHHHHHHHHHHHHHH		57.0419608861
454AcetylationHRVAFVEKLTKLVLS
HHHHHHHHHHHHHHH		57.0419608861
503UbiquitinationRQRQNDFKKMIQEVM
HHHHHHHHHHHHHHH		44.27-
504UbiquitinationQRQNDFKKMIQEVMH
HHHHHHHHHHHHHHH		41.03-
512PhosphorylationMIQEVMHSLVKLTRG
HHHHHHHHHHHHHHC		19.4320873877
515UbiquitinationEVMHSLVKLTRGALL
HHHHHHHHHHHCCEE		49.81-
532UbiquitinationSIRDGEAKQYGGWEV
EECCCCCCEECCEEE		39.49-
534PhosphorylationRDGEAKQYGGWEVKC
CCCCCCEECCEEEEE		19.5225147952
639UbiquitinationLKGVLECKPGEASVF
HCCHHHCCCCCCCCC		46.83-
743UbiquitinationHNFQGIEKITQVSMA
CCCCCHHHHHHHHHH		49.48-
753UbiquitinationQVSMASLKELDQRLF
HHHHHHHHHHHHHHH		54.4521890473
763PhosphorylationDQRLFENYIELKADP
HHHHHHHHHHHCCCC		6.6427642862
833PhosphorylationSKVIEAVSEELSRLM
HHHHHHHHHHHHHHH		32.1923898821
837PhosphorylationEAVSEELSRLMQCVS
HHHHHHHHHHHHHHH		27.0123898821
844PhosphorylationSRLMQCVSSFSKNGA
HHHHHHHHHCCCCCH		33.0430576142
845PhosphorylationRLMQCVSSFSKNGAL
HHHHHHHHCCCCCHH		17.0924719451
848UbiquitinationQCVSSFSKNGALQAR
HHHHHCCCCCHHHHH		58.34-
868PhosphorylationLRDTVAVYLTPESKS
CCCEEEEEECCCCHH		8.6322817900
874UbiquitinationVYLTPESKSSFKQAL
EEECCCCHHHHHHHH		48.75-
878UbiquitinationPESKSSFKQALEALP
CCCHHHHHHHHHHHH		36.29-
888PhosphorylationLEALPQLSSGADKKL
HHHHHHCCCCCCHHH		22.8321815630
889PhosphorylationEALPQLSSGADKKLL
HHHHHCCCCCCHHHH		46.7423186163
893MalonylationQLSSGADKKLLEELL
HCCCCCCHHHHHHHH		44.8026320211
893AcetylationQLSSGADKKLLEELL
HCCCCCCHHHHHHHH		44.8025953088
894UbiquitinationLSSGADKKLLEELLN
CCCCCCHHHHHHHHH		59.87-
902UbiquitinationLLEELLNKFKSSMHL
HHHHHHHHHHHCHHH		54.89-
924PhosphorylationASSTMMKT-------
HHHHHCCC-------		26.41-
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 EXOC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXOC2_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 EXOC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXOC8_HUMANEXOC8physical
14525976
RALB_HUMANRALBphysical
14525976
RALA_HUMANRALAphysical
12839989
RALA_HUMANRALAphysical
12624092
EXOC4_HUMANEXOC4physical
22939629
EXOC8_HUMANEXOC8physical
22939629
EXOC3_HUMANEXOC3physical
22939629
EXOC7_HUMANEXOC7physical
22939629
EXOC5_HUMANEXOC5physical
22939629
EXOC6_HUMANEXOC6physical
22939629
EXOC8_HUMANEXOC8physical
24056301
RALB_HUMANRALBphysical
24056301
TBK1_HUMANTBK1physical
24056301
UBP33_HUMANUSP33physical
24056301
BECN1_HUMANBECN1physical
24056301
RUBIC_HUMANKIAA0226physical
21241894
BAKOR_HUMANATG14physical
21241894
BECN1_HUMANBECN1physical
21241894
RALA_HUMANRALAphysical
21241894
RALB_HUMANRALBphysical
21241894
EXOC4_HUMANEXOC4physical
21241894
PK3C3_HUMANPIK3C3physical
21241894
ULK1_HUMANULK1physical
21241894
EXOC3_HUMANEXOC3physical
26344197
EXOC4_HUMANEXOC4physical
26344197
EXOC6_HUMANEXOC6physical
26344197
EXOC7_HUMANEXOC7physical
26344197
EXOC8_HUMANEXOC8physical
26344197
SPTN2_HUMANSPTBN2physical
26344197
EXOC3_HUMANEXOC3physical
27173435
EXOC4_HUMANEXOC4physical
27173435
EXOC1_HUMANEXOC1physical
27173435
EXOC5_HUMANEXOC5physical
27173435
EXOC6_HUMANEXOC6physical
27173435
EXOC7_HUMANEXOC7physical
27173435
EXOC8_HUMANEXOC8physical
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 EXOC2_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-454, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND MASSSPECTROMETRY.

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