K1C13_HUMAN - dbPTM
K1C13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K1C13_HUMAN
UniProt AC P13646
Protein Name Keratin, type I cytoskeletal 13
Gene Name KRT13
Organism Homo sapiens (Human).
Sequence Length 458
Subcellular Localization
Protein Description
Protein Sequence MSLRLQSSSASYGGGFGGGSCQLGGGRGVSTCSTRFVSGGSAGGYGGGVSCGFGGGAGSGFGGGYGGGLGGGYGGGLGGGFGGGFAGGFVDFGACDGGLLTGNEKITMQNLNDRLASYLEKVRALEEANADLEVKIRDWHLKQSPASPERDYSPYYKTIEELRDKILTATIENNRVILEIDNARLAADDFRLKYENELALRQSVEADINGLRRVLDELTLSKTDLEMQIESLNEELAYMKKNHEEEMKEFSNQVVGQVNVEMDATPGIDLTRVLAEMREQYEAMAERNRRDAEEWFHTKSAELNKEVSTNTAMIQTSKTEITELRRTLQGLEIELQSQLSMKAGLENTVAETECRYALQLQQIQGLISSIEAQLSELRSEMECQNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMIGFPSSAGSVSPRSTSVTTTSSASVTTTSNASGRRTSDVRRP
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
7Phosphorylation-MSLRLQSSSASYGG
-CCCCCCCCCCCCCC
30.7425394399
8PhosphorylationMSLRLQSSSASYGGG
CCCCCCCCCCCCCCC
19.57-
11PhosphorylationRLQSSSASYGGGFGG
CCCCCCCCCCCCCCC
26.6825394399
12PhosphorylationLQSSSASYGGGFGGG
CCCCCCCCCCCCCCC
21.3622817900
27MethylationSCQLGGGRGVSTCST
CCCCCCCCCCCCCEE
45.6924129315
27 (in isoform 3)Methylation-45.69-
35MethylationGVSTCSTRFVSGGSA
CCCCCEEEEECCCCC
17.4224129315
50PhosphorylationGGYGGGVSCGFGGGA
CCCCCCCCCCCCCCC
16.28-
118PhosphorylationLNDRLASYLEKVRAL
HHHHHHHHHHHHHHH
17.17-
144PhosphorylationRDWHLKQSPASPERD
EHHHHCCCCCCCCCC
22.3528290473
147PhosphorylationHLKQSPASPERDYSP
HHCCCCCCCCCCCCC
30.5828355574
152PhosphorylationPASPERDYSPYYKTI
CCCCCCCCCCHHHHH
20.1223312004
153PhosphorylationASPERDYSPYYKTIE
CCCCCCCCCHHHHHH
15.6623312004
155PhosphorylationPERDYSPYYKTIEEL
CCCCCCCHHHHHHHH
16.2023312004
156PhosphorylationERDYSPYYKTIEELR
CCCCCCHHHHHHHHH
12.6823312004
168PhosphorylationELRDKILTATIENNR
HHHHHHHEEEEECCE
25.8120860994
170PhosphorylationRDKILTATIENNRVI
HHHHHEEEEECCEEE
24.4820860994
194PhosphorylationADDFRLKYENELALR
CHHHHHHHHCHHHHH
28.6922817900
238PhosphorylationSLNEELAYMKKNHEE
HHHHHHHHHHHCCHH
23.30-
281PhosphorylationLAEMREQYEAMAERN
HHHHHHHHHHHHHHH
10.82-
308PhosphorylationAELNKEVSTNTAMIQ
HHHCHHCCCCCEEEE
19.6121406692
309PhosphorylationELNKEVSTNTAMIQT
HHCHHCCCCCEEEEC
41.5921406692
311PhosphorylationNKEVSTNTAMIQTSK
CHHCCCCCEEEECCH
20.0721406692
316PhosphorylationTNTAMIQTSKTEITE
CCCEEEECCHHHHHH
22.6721406692
317PhosphorylationNTAMIQTSKTEITEL
CCEEEECCHHHHHHH
22.6221406692
327PhosphorylationEITELRRTLQGLEIE
HHHHHHHHHHHHHHH
19.5920068231
337PhosphorylationGLEIELQSQLSMKAG
HHHHHHHHHHHHHHC
45.7920068231
340PhosphorylationIELQSQLSMKAGLEN
HHHHHHHHHHHCCCC
15.5930278072
404PhosphorylationRLEQEIATYRSLLEG
HHHHHHHHHHHHHCC
25.73-
405PhosphorylationLEQEIATYRSLLEGQ
HHHHHHHHHHHHCCC
6.81-
416 (in isoform 3)Acetylation-3.77-
421PhosphorylationAKMIGFPSSAGSVSP
CEEECCCCCCCCCCC
30.4728176443
422PhosphorylationKMIGFPSSAGSVSPR
EEECCCCCCCCCCCC
36.5728355574
425PhosphorylationGFPSSAGSVSPRSTS
CCCCCCCCCCCCCCE
21.0928176443
427PhosphorylationPSSAGSVSPRSTSVT
CCCCCCCCCCCCEEE
19.127493031
432PhosphorylationSVSPRSTSVTTTSSA
CCCCCCCEEEECCCC
20.79-
434PhosphorylationSPRSTSVTTTSSASV
CCCCCEEEECCCCEE
24.91-
438PhosphorylationTSVTTTSSASVTTTS
CEEEECCCCEEEECC
23.5930576142
444PhosphorylationSSASVTTTSNASGRR
CCCEEEECCCCCCCC
15.6030576142
452PhosphorylationSNASGRRTSDVRRP-
CCCCCCCCCCCCCC-
28.1120363803
453PhosphorylationNASGRRTSDVRRP--
CCCCCCCCCCCCC--
32.0920363803

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 K1C13_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K1C13_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 K1C13_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MOS_HUMANMOSphysical
25416956
MYH1_HUMANMYH1physical
25416956
PSB1_HUMANPSMB1physical
25416956
PSB2_HUMANPSMB2physical
25416956
TYB4_HUMANTMSB4Xphysical
25416956
TS101_HUMANTSG101physical
25416956
IF4E2_HUMANEIF4E2physical
25416956
CEP57_HUMANCEP57physical
25416956
ABI2_HUMANABI2physical
25416956
SYFM_HUMANFARS2physical
25416956
BL1S6_HUMANBLOC1S6physical
25416956
ABI3_HUMANABI3physical
25416956
AMOL2_HUMANAMOTL2physical
25416956
K1C20_HUMANKRT20physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
CA109_HUMANC1orf109physical
25416956
EXOS5_HUMANEXOSC5physical
25416956
LSM2_HUMANLSM2physical
25416956
FBF1_HUMANFBF1physical
25416956
KLC4_HUMANKLC4physical
25416956
IFT20_HUMANIFT20physical
25416956
K2C71_HUMANKRT71physical
25416956
SGF29_HUMANCCDC101physical
25416956
CA216_HUMANC1orf216physical
25416956
KLC3_HUMANKLC3physical
25416956
C2CD6_HUMANALS2CR11physical
25416956
PPR18_HUMANPPP1R18physical
25416956
TXLNA_HUMANTXLNAphysical
25416956
CE57L_HUMANCEP57L1physical
25416956
K2C6C_HUMANKRT6Cphysical
25416956
TRI42_HUMANTRIM42physical
25416956
K2C79_HUMANKRT79physical
25416956
RTL8B_HUMANFAM127Cphysical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615785White sponge nevus 2 (WSN2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K1C13_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-427, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND MASSSPECTROMETRY.

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