OCLN_MOUSE - dbPTM
OCLN_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OCLN_MOUSE
UniProt AC Q61146
Protein Name Occludin
Gene Name Ocln
Organism Mus musculus (Mouse).
Sequence Length 521
Subcellular Localization Cell membrane
Multi-pass membrane protein . Cell junction, tight junction .
Protein Description May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier..
Protein Sequence MSVRPFESPPPYRPDEFKPNHYAPSNDMYGGEMHVRPMLSQPAYSFYPEDEILHFYKWTSPPGVIRILSMLIIVMCIAIFACVASTLAWDRGYGTGLFGGSLNYPYSGFGYGGGYGGGYGGYGYGYGGYTDPRAAKGFLLAMAAFCFIASLVIFVTSVIRSGMSRTRRYYLIVIIVSAILGIMVFIATIVYIMGVNPTAQASGSMYGSQIYMICNQFYTPGGTGLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIIFFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKNVSAGTQDMPPPPSDYAERVDSPMAYSSNGKVNGKRSYPESFYKSTPLVPEVAQEIPLTLSVDDFRQPRYSSNGNLETPSKRAPTKGKAGKGKRTDPDHYETDYTTGGESCEELEEDWVREYPPITSDQQRQLYKRNFDAGLQEYKSLQAELDDVNKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKRNYCKQLKSKLSHIKRMVGDYDRRKP
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------MSVRPFESP
------CCCCCCCCC
27.1723375375
8PhosphorylationMSVRPFESPPPYRPD
CCCCCCCCCCCCCCC
42.9823375375
40PhosphorylationMHVRPMLSQPAYSFY
CCCCCCCCCCCCCCC
28.0629472430
44PhosphorylationPMLSQPAYSFYPEDE
CCCCCCCCCCCCHHH
13.1429472430
45PhosphorylationMLSQPAYSFYPEDEI
CCCCCCCCCCCHHHH
22.0229472430
47PhosphorylationSQPAYSFYPEDEILH
CCCCCCCCCHHHHHE
10.3629472430
274UbiquitinationRKMDRYDKSNILWDK
HCCCCCCCCCCCCCH
36.15-
285PhosphorylationLWDKEHIYDEQPPNV
CCCHHHCCCCCCCCH
18.48-
297UbiquitinationPNVEEWVKNVSAGTQ
CCHHHHHHHHCCCCC
53.34-
300PhosphorylationEEWVKNVSAGTQDMP
HHHHHHHCCCCCCCC
30.3022817900
303PhosphorylationVKNVSAGTQDMPPPP
HHHHCCCCCCCCCCC
22.5522817900
311PhosphorylationQDMPPPPSDYAERVD
CCCCCCCCHHHHHCC
49.3722817900
313PhosphorylationMPPPPSDYAERVDSP
CCCCCCHHHHHCCCC
18.0721183079
319PhosphorylationDYAERVDSPMAYSSN
HHHHHCCCCCEECCC
17.4522817900
324PhosphorylationVDSPMAYSSNGKVNG
CCCCCEECCCCCCCC
14.0522817900
325PhosphorylationDSPMAYSSNGKVNGK
CCCCEECCCCCCCCC
36.6021082442
334PhosphorylationGKVNGKRSYPESFYK
CCCCCCCCCCHHHHC
48.8329472430
335PhosphorylationKVNGKRSYPESFYKS
CCCCCCCCCHHHHCC
18.3029472430
338PhosphorylationGKRSYPESFYKSTPL
CCCCCCHHHHCCCCC
29.4025521595
340PhosphorylationRSYPESFYKSTPLVP
CCCCHHHHCCCCCCH
17.2029472430
342PhosphorylationYPESFYKSTPLVPEV
CCHHHHCCCCCCHHH
24.7130352176
343PhosphorylationPESFYKSTPLVPEVA
CHHHHCCCCCCHHHH
19.2530352176
356PhosphorylationVAQEIPLTLSVDDFR
HHHHCCCEEEHHHCC
16.1926239621
358PhosphorylationQEIPLTLSVDDFRQP
HHCCCEEEHHHCCCC
20.4726239621
367PhosphorylationDDFRQPRYSSNGNLE
HHCCCCCCCCCCCCC
24.1225521595
368PhosphorylationDFRQPRYSSNGNLET
HCCCCCCCCCCCCCC
20.7122817900
369PhosphorylationFRQPRYSSNGNLETP
CCCCCCCCCCCCCCC
39.5625521595
375PhosphorylationSSNGNLETPSKRAPT
CCCCCCCCCCCCCCC
35.7122817900
377PhosphorylationNGNLETPSKRAPTKG
CCCCCCCCCCCCCCC
42.0423984901
382PhosphorylationTPSKRAPTKGKAGKG
CCCCCCCCCCCCCCC
51.9818187566
397PhosphorylationKRTDPDHYETDYTTG
CCCCCCCCCCCCCCC
28.09-
399PhosphorylationTDPDHYETDYTTGGE
CCCCCCCCCCCCCCC
27.4322871156
401PhosphorylationPDHYETDYTTGGESC
CCCCCCCCCCCCCCH
17.39-
402PhosphorylationDHYETDYTTGGESCE
CCCCCCCCCCCCCHH
23.0621183079
403PhosphorylationHYETDYTTGGESCEE
CCCCCCCCCCCCHHH
36.6422817900
407PhosphorylationDYTTGGESCEELEED
CCCCCCCCHHHHHHH
30.0622817900
466PhosphorylationLDKELDDYREESEEY
HHHHHHHHHHHHHHH
21.4222817900
470PhosphorylationLDDYREESEEYMAAA
HHHHHHHHHHHHHHH
30.8630482847
473PhosphorylationYREESEEYMAAADEY
HHHHHHHHHHHHHHH
6.4922817900
480PhosphorylationYMAAADEYNRLKQVK
HHHHHHHHHHHHHHC
13.2130482847
489PhosphorylationRLKQVKGSADYKSKR
HHHHHCCCCCHHHHH
16.55-
507PhosphorylationKQLKSKLSHIKRMVG
HHHHHHHHHHHHHHC
27.2318187566

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
338SPhosphorylationKinasePRKCAP17252
GPS
338SPhosphorylationKinasePKC-FAMILY-GPS
338SPhosphorylationKinasePKC-Uniprot
382TPhosphorylationKinaseGRK1Q15835
PSP
402TPhosphorylationKinasePRKCHP23298
Uniprot
507SPhosphorylationKinaseGRK1Q15835
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OCLN_MOUSE !!

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 OCLN_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFR1_MOUSETgfbr1physical
15761153
CLH1_MOUSECltcphysical
20682309

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OCLN_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein kinase C regulates the phosphorylation and cellularlocalization of occludin.";
Andreeva A.Y., Krause E., Mueller E.-C., Blasig I.E.,Utepbergenov D.I.;
J. Biol. Chem. 276:38480-38486(2001).
Cited for: PHOSPHORYLATION AT SER-338, AND MASS SPECTROMETRY.

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