K1C18_MOUSE - dbPTM
K1C18_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K1C18_MOUSE
UniProt AC P05784
Protein Name Keratin, type I cytoskeletal 18
Gene Name Krt18
Organism Mus musculus (Mouse).
Sequence Length 423
Subcellular Localization Nucleus matrix. Nucleus, nucleolus. Cytoplasm.
Protein Description When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection..
Protein Sequence MSFTTRSTTFSTNYRSLGSVRTPSQRVRPASSAASVYAGAGGSGSRISVSRSVWGGSVGSAGLAGMGGIQTEKETMQDLNDRLASYLDKVKSLETENRRLESKIREHLEKKGPQGVRDWGHYFKIIEDLRAQIFANSVDNARIVLQIDNARLAADDFRVKYETELAMRQSVESDIHGLRKVVDDTNITRLQLETEIEALKEELLFMKKNHEEEVQGLEAQIASSGLTVEVDAPKSQDLSKIMADIRAQYEALAQKNREELDKYWSQQIEESTTVVTTKSAEIRDAETTLTELRRTLQTLEIDLDSMKNQNINLENSLGDVEARYKAQMEQLNGVLLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFSLNDALDSSNSMQTVQKTTTRKIVDGRVVSETNDTRVLRH
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------MSFTTRSTT
------CCCCCCCCC		31.1629472430
2Acetylation------MSFTTRSTT
------CCCCCCCCC		31.16-
4Phosphorylation----MSFTTRSTTFS
----CCCCCCCCCCC		17.6229472430
5Phosphorylation---MSFTTRSTTFST
---CCCCCCCCCCCC		22.1729472430
7Phosphorylation-MSFTTRSTTFSTNY
-CCCCCCCCCCCCCC		29.7027087446
8PhosphorylationMSFTTRSTTFSTNYR
CCCCCCCCCCCCCCC		28.6821082442
9PhosphorylationSFTTRSTTFSTNYRS
CCCCCCCCCCCCCCC		19.4820139300
11PhosphorylationTTRSTTFSTNYRSLG
CCCCCCCCCCCCCCC		17.4122817900
12PhosphorylationTRSTTFSTNYRSLGS
CCCCCCCCCCCCCCC		31.8826239621
14PhosphorylationSTTFSTNYRSLGSVR
CCCCCCCCCCCCCCC		11.1526239621
16PhosphorylationTFSTNYRSLGSVRTP
CCCCCCCCCCCCCCC		27.0726239621
19PhosphorylationTNYRSLGSVRTPSQR
CCCCCCCCCCCCCCC		17.4527087446
22PhosphorylationRSLGSVRTPSQRVRP
CCCCCCCCCCCCCCC		25.7422817900
24PhosphorylationLGSVRTPSQRVRPAS
CCCCCCCCCCCCCCC		29.9718846507
28MethylationRTPSQRVRPASSAAS
CCCCCCCCCCCCCCE		24.2116188877
31O-linked_GlycosylationSQRVRPASSAASVYA
CCCCCCCCCCCEECC		24.16-
31PhosphorylationSQRVRPASSAASVYA
CCCCCCCCCCCEECC		24.1625521595
32O-linked_GlycosylationQRVRPASSAASVYAG
CCCCCCCCCCEECCC		29.93-
32PhosphorylationQRVRPASSAASVYAG
CCCCCCCCCCEECCC		29.9325521595
35PhosphorylationRPASSAASVYAGAGG
CCCCCCCEECCCCCC		18.5125521595
37PhosphorylationASSAASVYAGAGGSG
CCCCCEECCCCCCCC		9.2325521595
43PhosphorylationVYAGAGGSGSRISVS
ECCCCCCCCCCEEEE		32.4525521595
45PhosphorylationAGAGGSGSRISVSRS
CCCCCCCCCEEEEEC		28.3025521595
46MethylationGAGGSGSRISVSRSV
CCCCCCCCEEEEECC		28.8230760143
48PhosphorylationGGSGSRISVSRSVWG
CCCCCCEEEEECCCC		16.9627087446
50PhosphorylationSGSRISVSRSVWGGS
CCCCEEEEECCCCCC		16.4323984901
50O-linked_GlycosylationSGSRISVSRSVWGGS
CCCCEEEEECCCCCC		16.43-
52PhosphorylationSRISVSRSVWGGSVG
CCEEEEECCCCCCCC		18.0826239621
57PhosphorylationSRSVWGGSVGSAGLA
EECCCCCCCCHHHHC		21.2626239621
60PhosphorylationVWGGSVGSAGLAGMG
CCCCCCCHHHHCCCC		19.6026239621
85PhosphorylationDLNDRLASYLDKVKS
HHHHHHHHHHHHHHC		30.7124719451
89UbiquitinationRLASYLDKVKSLETE
HHHHHHHHHHCHHHH		49.3022790023
92PhosphorylationSYLDKVKSLETENRR
HHHHHHHCHHHHHHH		34.13-
102PhosphorylationTENRRLESKIREHLE
HHHHHHHHHHHHHHH		37.66-
103AcetylationENRRLESKIREHLEK
HHHHHHHHHHHHHHH		36.0923201123
124AcetylationRDWGHYFKIIEDLRA
HHHHHHHHHHHHHHH		35.2923864654
124UbiquitinationRDWGHYFKIIEDLRA
HHHHHHHHHHHHHHH		35.2922790023
137PhosphorylationRAQIFANSVDNARIV
HHHHHHCCCCCEEEE		27.6722817900
160AcetylationAADDFRVKYETELAM
CCCCCHHHHHHHHHH		32.8723201123
160UbiquitinationAADDFRVKYETELAM
CCCCCHHHHHHHHHH		32.8722790023
161PhosphorylationADDFRVKYETELAMR
CCCCHHHHHHHHHHH		25.8122871156
170PhosphorylationTELAMRQSVESDIHG
HHHHHHHHHHHHHCH		19.9320139300
180UbiquitinationSDIHGLRKVVDDTNI
HHHCHHHHHCCCCCC		52.2122790023
180AcetylationSDIHGLRKVVDDTNI
HHHCHHHHHCCCCCC		52.2122733758
200AcetylationETEIEALKEELLFMK
HHHHHHHHHHHHHHC		57.0722733758
234UbiquitinationTVEVDAPKSQDLSKI
EEEEECCCCCCHHHH		63.5722790023
235PhosphorylationVEVDAPKSQDLSKIM
EEEECCCCCCHHHHH		28.0621454597
240UbiquitinationPKSQDLSKIMADIRA
CCCCCHHHHHHHHHH		43.7427667366
240MalonylationPKSQDLSKIMADIRA
CCCCCHHHHHHHHHH		43.7425418362
240AcetylationPKSQDLSKIMADIRA
CCCCCHHHHHHHHHH		43.7422733758
255UbiquitinationQYEALAQKNREELDK
HHHHHHHCCHHHHHH		52.9822790023
262UbiquitinationKNREELDKYWSQQIE
CCHHHHHHHHHHHHH		62.3322790023
278UbiquitinationSTTVVTTKSAEIRDA
CCEEEEECCHHHHCH		38.0022790023
279PhosphorylationTTVVTTKSAEIRDAE
CEEEEECCHHHHCHH		29.1023984901
295PhosphorylationTLTELRRTLQTLEID
HHHHHHHHHHHEEEC		19.45-
305PhosphorylationTLEIDLDSMKNQNIN
HEEECHHHHHCCCCC		38.6728973931
316PhosphorylationQNINLENSLGDVEAR
CCCCCCCCCHHHHHH		25.1025521595
324PhosphorylationLGDVEARYKAQMEQL
CHHHHHHHHHHHHHH		20.0923984901
363UbiquitinationYEALLNIKVKLEAEI
HHHHHCCCHHHHHHH		32.0422790023
384PhosphorylationLEDGEDFSLNDALDS
HHCCCCCCHHHHCCC		38.2927087446
391PhosphorylationSLNDALDSSNSMQTV
CHHHHCCCCCCCCCC		32.0622817900
392PhosphorylationLNDALDSSNSMQTVQ
HHHHCCCCCCCCCCC		32.3727087446
394PhosphorylationDALDSSNSMQTVQKT
HHCCCCCCCCCCCCC		17.7627087446
395OxidationALDSSNSMQTVQKTT
HCCCCCCCCCCCCCC		4.5317203969
397PhosphorylationDSSNSMQTVQKTTTR
CCCCCCCCCCCCCCC		19.0917203969
400UbiquitinationNSMQTVQKTTTRKIV
CCCCCCCCCCCCEEE		43.4322790023
413PhosphorylationIVDGRVVSETNDTRV
EECCEEEEECCCCCC		35.5325521595
415PhosphorylationDGRVVSETNDTRVLR
CCEEEEECCCCCCCC		30.7818846507
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
52SPhosphorylationKinaseMAPKAPK2P49138
Uniprot
52SPhosphorylationKinaseMAPKAPK3Q3UMW7
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K1C18_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 K1C18_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of K1C18_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K1C18_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylateepithelial keratins.";
Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O.,Seidler U., Omary M.B., Kotlyarov A., Gaestel M.;
J. Biol. Chem. 285:33242-33251(2010).
Cited for: PHOSPHORYLATION AT SER-52 BY MAPKAPK2 AND MAPKAPK3.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; THR-12; SER-31;SER-32 AND SER-35, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND THR-397, ANDMASS SPECTROMETRY.

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