SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02535

- K1C10_MOUSE

UniProt

P02535 - K1C10_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Keratin, type I cytoskeletal 10

Gene
Krt10, Krt1-10
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei396 – 3961Stutter

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. cellular response to calcium ion Source: MGI
  2. epithelial cell differentiation Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 10
Alternative name(s):
56 kDa cytokeratin
Cytokeratin-10
Short name:
CK-10
Keratin, type I cytoskeletal 59 kDa
Keratin-10
Short name:
K10
Gene namesi
Name:Krt10
Synonyms:Krt1-10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:96685. Krt10.

Subcellular locationi

GO - Cellular componenti

  1. keratin filament Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 570570Keratin, type I cytoskeletal 10PRO_0000063643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphoserine By similarity
Modified residuei34 – 341Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP02535.
PaxDbiP02535.
PRIDEiP02535.

PTM databases

PhosphoSiteiP02535.

Expressioni

Gene expression databases

CleanExiMM_KRT10.
GenevestigatoriP02535.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. keratin-10 is generally associated with keratin-1.

Binary interactionsi

WithEntry#Exp.IntActNotes
ChukQ60680-16EBI-646288,EBI-646260

Protein-protein interaction databases

BioGridi201017. 8 interactions.
IntActiP02535. 2 interactions.
MINTiMINT-1859130.

Structurei

3D structure databases

ProteinModelPortaliP02535.
SMRiP02535. Positions 143-293, 311-453.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 143143HeadAdd
BLAST
Regioni144 – 454311RodAdd
BLAST
Regioni144 – 17936Coil 1AAdd
BLAST
Regioni180 – 20021Linker 1Add
BLAST
Regioni201 – 29292Coil 1BAdd
BLAST
Regioni293 – 31523Linker 12Add
BLAST
Regioni316 – 454139Coil 2Add
BLAST
Regioni455 – 570116TailAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi453 – 565113Gly/Ser-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG147548.
HOVERGENiHBG013015.
InParanoidiP02535.
KOiK07604.
PhylomeDBiP02535.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P02535-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSVLYSSSSK QFSSSRSGGG GGGGSVRVSS TRGSLGGGYS SGGFSGGSFS    50
RGSSGGGCFG GSSGGYGGFG GGGSFGGGYG GSSFGGGYGG SSFGGGYGGS 100
SFGGAGFGGG GSFGGGSFGG GSYGGGFGGG GFGGDGGSLL SGNGRVTMQN 150
LNDRLASYMD KVRALEESNY ELEGKIKEWY EKHGNSSQRE PRDYSKYYKT 200
IEDLKGQILT LTTDNANVLL QIDNARLAAD DFRLKYENEV TLRQSVEADI 250
NGLRRVLDEL TLSKSDLEMQ IESLNEELAY LKKNHEEEMR DLQNVSTGDV 300
NVEMNAAPGV DLTQLLNNMR NQYEQLAEKN RKDAEEWFNQ KSKELTTEID 350
SNIEQMSSHK SEITELRRTV QGLEIELQSQ LALKQSLEAS LAETEGRYCV 400
QLSQIQSQIS ALEEQLQQIR AETECQNAEY QQLLDIKTRL ENEIQTYRSL 450
LEGEGSSSGG GGGRRGGSGG GSYGGSSGGG SYGGSSGGGG SYGGSSGGGG 500
SYGGGSSGGG SHGGSSGGGY GGGSSSGGAG GHGGSSGGGY GGGSSSGGQG 550
GSGGFKSSGG GDQSSKGPRY 570
Length:570
Mass (Da):57,770
Last modified:January 23, 2007 - v3
Checksum:iEE60EA87DE7770E0
GO
Isoform 2 (identifier: P02535-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     97-106: YGGSSFGGAG → S
     144-145: GR → EK

Note: No experimental confirmation available.

Show »
Length:561
Mass (Da):57,060
Checksum:i8EEF036A0FA03831
GO
Isoform 3 (identifier: P02535-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     97-106: YGGSSFGGAG → S
     144-145: GR → EK
     465-471: RGGSGGG → PRRQPRR
     472-570: Missing.

Note: No experimental confirmation available.

Show »
Length:462
Mass (Da):49,501
Checksum:iD7A0BC767157B99D
GO

Sequence cautioni

The sequence BAB29296.1 differs from that shown. Reason: Frameshift at positions 96 and 122.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei97 – 10610YGGSSFGGAG → S in isoform 2 and isoform 3. VSP_021100
Alternative sequencei144 – 1452GR → EK in isoform 2 and isoform 3. VSP_021101
Alternative sequencei465 – 4717RGGSGGG → PRRQPRR in isoform 3. VSP_021102
Alternative sequencei472 – 57099Missing in isoform 3. VSP_021103Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41L → R in AAF65456. 1 Publication
Sequence conflicti6 – 61S → C in CAA24214. 1 Publication
Sequence conflicti23 – 231G → GGG1 Publication
Sequence conflicti25 – 251S → F in CAA24214. 1 Publication
Sequence conflicti29 – 291S → F in CAA24214. 1 Publication
Sequence conflicti39 – 391Y → L in CAA24214. 1 Publication
Sequence conflicti42 – 421G → E in AAA39391. 1 Publication
Sequence conflicti46 – 461G → R in BAB29296. 1 Publication
Sequence conflicti94 – 941G → V in BAB29296. 1 Publication
Sequence conflicti105 – 1062AG → GS in CAA24214. 1 Publication
Sequence conflicti111 – 1111Missing1 Publication
Sequence conflicti122 – 1232SY → GC in CAA24214. 1 Publication
Sequence conflicti138 – 1381S → G in CAA24214. 1 Publication
Sequence conflicti149 – 1491Q → R in CAA24214. 1 Publication
Sequence conflicti179 – 18810WYEKHGNSSQ → VVREARQLKP in CAA24214. 1 Publication
Sequence conflicti264 – 2696KSDLEM → QSVLEL in CAA24214. 1 Publication
Sequence conflicti277 – 2771E → G in BAC38210. 1 Publication
Sequence conflicti285 – 2851H → L in CAA24214. 1 Publication
Sequence conflicti354 – 3541E → A in CAA24214. 1 Publication
Sequence conflicti395 – 4006EGRYCV → VESLLR in CAA24214. 1 Publication
Sequence conflicti465 – 4651R → G in BAB29296. 1 Publication
Sequence conflicti465 – 4651R → G in BAC36371. 1 Publication
Sequence conflicti465 – 4651R → G in BAC38210. 1 Publication
Sequence conflicti466 – 4672GG → AD in BAB29296. 1 Publication
Sequence conflicti469 – 4691G → H in BAB29296. 1 Publication
Sequence conflicti469 – 4691G → H in BAC36371. 1 Publication
Sequence conflicti469 – 4691G → H in BAC38210. 1 Publication
Sequence conflicti509 – 5157GGSHGGS → CGGRGGG in CAA24214. 1 Publication
Sequence conflicti524 – 5241S → G in CAA24214. 1 Publication
Sequence conflicti532 – 5321H → R in CAA24214. 1 Publication
Sequence conflicti535 – 5351S → G in CAA24214. 1 Publication
Sequence conflicti544 – 5441S → G in CAA24214. 1 Publication
Sequence conflicti548 – 5492GQ → RR in CAA24214. 1 Publication
Sequence conflicti556 – 5572KS → SGT in CAA24214. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L00193, M10081 Genomic DNA. Translation: AAA39391.1.
V00830 mRNA. Translation: CAA24214.1.
AK014360 mRNA. Translation: BAB29296.1. Frameshift.
AK076508 mRNA. Translation: BAC36371.1.
AK081402 mRNA. Translation: BAC38210.1.
AK081914 mRNA. Translation: BAC38369.1.
AF245658 Genomic DNA. Translation: AAF65456.1.
CCDSiCCDS25380.1. [P02535-2]
PIRiA02940. KRMSE1.
S07330.
RefSeqiNP_034790.2. NM_010660.2.
UniGeneiMm.22662.

Genome annotation databases

GeneIDi16661.
KEGGimmu:16661.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L00193 , M10081 Genomic DNA. Translation: AAA39391.1 .
V00830 mRNA. Translation: CAA24214.1 .
AK014360 mRNA. Translation: BAB29296.1 . Frameshift.
AK076508 mRNA. Translation: BAC36371.1 .
AK081402 mRNA. Translation: BAC38210.1 .
AK081914 mRNA. Translation: BAC38369.1 .
AF245658 Genomic DNA. Translation: AAF65456.1 .
CCDSi CCDS25380.1. [P02535-2 ]
PIRi A02940. KRMSE1.
S07330.
RefSeqi NP_034790.2. NM_010660.2.
UniGenei Mm.22662.

3D structure databases

ProteinModelPortali P02535.
SMRi P02535. Positions 143-293, 311-453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201017. 8 interactions.
IntActi P02535. 2 interactions.
MINTi MINT-1859130.

PTM databases

PhosphoSitei P02535.

Proteomic databases

MaxQBi P02535.
PaxDbi P02535.
PRIDEi P02535.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 16661.
KEGGi mmu:16661.

Organism-specific databases

CTDi 3858.
MGIi MGI:96685. Krt10.

Phylogenomic databases

eggNOGi NOG147548.
HOVERGENi HBG013015.
InParanoidi P02535.
KOi K07604.
PhylomeDBi P02535.

Miscellaneous databases

ChiTaRSi KRT10. mouse.
NextBioi 290363.
PROi P02535.
SOURCEi Search...

Gene expression databases

CleanExi MM_KRT10.
Genevestigatori P02535.

Family and domain databases

InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
Pfami PF00038. Filament. 1 hit.
[Graphical view ]
PRINTSi PR01248. TYPE1KERATIN.
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Organization of a type I keratin gene. Evidence for evolution of intermediate filaments from a common ancestral gene."
    Krieg T.M., Schafer M.P., Cheng C.K., Filpula D., Flaherty P., Steinert P.M., Roop D.R.
    J. Biol. Chem. 260:5867-5870(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  2. "Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments."
    Steinert P.M., Rice R.H., Roop D.R., Trus B.L., Steven A.C.
    Nature 302:794-800(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Head.
  4. Reichelt J., Magin T.M.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-341 (ISOFORMS 2/3).
    Strain: 129/SvJ.
    Tissue: Liver.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 146-154; 164-175; 227-233; 244-254; 361-367; 385-397 AND 440-448, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.

Entry informationi

Entry nameiK1C10_MOUSE
AccessioniPrimary (citable) accession number: P02535
Secondary accession number(s): P08731
, Q8BUX3, Q8BV09, Q8BVU3, Q9CXH6, Q9JKB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi