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P02535

- K1C10_MOUSE

UniProt

P02535 - K1C10_MOUSE

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Protein

Keratin, type I cytoskeletal 10

Gene

Krt10

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. 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 – 171PhosphoserineBy similarity
Modified residuei34 – 341PhosphoserineBy 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.
ModBaseiSearch...
MobiDBiSearch...

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

Belongs to the intermediate filament family.Curated

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) [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

        10         20         30         40         50
MSVLYSSSSK QFSSSRSGGG GGGGSVRVSS TRGSLGGGYS SGGFSGGSFS
60 70 80 90 100
RGSSGGGCFG GSSGGYGGFG GGGSFGGGYG GSSFGGGYGG SSFGGGYGGS
110 120 130 140 150
SFGGAGFGGG GSFGGGSFGG GSYGGGFGGG GFGGDGGSLL SGNGRVTMQN
160 170 180 190 200
LNDRLASYMD KVRALEESNY ELEGKIKEWY EKHGNSSQRE PRDYSKYYKT
210 220 230 240 250
IEDLKGQILT LTTDNANVLL QIDNARLAAD DFRLKYENEV TLRQSVEADI
260 270 280 290 300
NGLRRVLDEL TLSKSDLEMQ IESLNEELAY LKKNHEEEMR DLQNVSTGDV
310 320 330 340 350
NVEMNAAPGV DLTQLLNNMR NQYEQLAEKN RKDAEEWFNQ KSKELTTEID
360 370 380 390 400
SNIEQMSSHK SEITELRRTV QGLEIELQSQ LALKQSLEAS LAETEGRYCV
410 420 430 440 450
QLSQIQSQIS ALEEQLQQIR AETECQNAEY QQLLDIKTRL ENEIQTYRSL
460 470 480 490 500
LEGEGSSSGG GGGRRGGSGG GSYGGSSGGG SYGGSSGGGG SYGGSSGGGG
510 520 530 540 550
SYGGGSSGGG SHGGSSGGGY GGGSSSGGAG GHGGSSGGGY GGGSSSGGQG
560 570
GSGGFKSSGG GDQSSKGPRY
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41L → R in AAF65456. 1 PublicationCurated
Sequence conflicti6 – 61S → C in CAA24214. (PubMed:6188955)Curated
Sequence conflicti23 – 231G → GGG1 PublicationCurated
Sequence conflicti25 – 251S → F in CAA24214. (PubMed:6188955)Curated
Sequence conflicti29 – 291S → F in CAA24214. (PubMed:6188955)Curated
Sequence conflicti39 – 391Y → L in CAA24214. (PubMed:6188955)Curated
Sequence conflicti42 – 421G → E in AAA39391. (PubMed:2581944)Curated
Sequence conflicti46 – 461G → R in BAB29296. (PubMed:16141072)Curated
Sequence conflicti94 – 941G → V in BAB29296. (PubMed:16141072)Curated
Sequence conflicti105 – 1062AG → GS in CAA24214. (PubMed:6188955)Curated
Sequence conflicti111 – 1111Missing(PubMed:6188955)Curated
Sequence conflicti122 – 1232SY → GC in CAA24214. (PubMed:6188955)Curated
Sequence conflicti138 – 1381S → G in CAA24214. (PubMed:6188955)Curated
Sequence conflicti149 – 1491Q → R in CAA24214. (PubMed:6188955)Curated
Sequence conflicti179 – 18810WYEKHGNSSQ → VVREARQLKP in CAA24214. (PubMed:6188955)Curated
Sequence conflicti264 – 2696KSDLEM → QSVLEL in CAA24214. (PubMed:6188955)Curated
Sequence conflicti277 – 2771E → G in BAC38210. (PubMed:16141072)Curated
Sequence conflicti285 – 2851H → L in CAA24214. (PubMed:6188955)Curated
Sequence conflicti354 – 3541E → A in CAA24214. (PubMed:6188955)Curated
Sequence conflicti395 – 4006EGRYCV → VESLLR in CAA24214. (PubMed:6188955)Curated
Sequence conflicti465 – 4651R → G in BAB29296. (PubMed:16141072)Curated
Sequence conflicti465 – 4651R → G in BAC36371. (PubMed:16141072)Curated
Sequence conflicti465 – 4651R → G in BAC38210. (PubMed:16141072)Curated
Sequence conflicti466 – 4672GG → AD in BAB29296. (PubMed:16141072)Curated
Sequence conflicti469 – 4691G → H in BAB29296. (PubMed:16141072)Curated
Sequence conflicti469 – 4691G → H in BAC36371. (PubMed:16141072)Curated
Sequence conflicti469 – 4691G → H in BAC38210. (PubMed:16141072)Curated
Sequence conflicti509 – 5157GGSHGGS → CGGRGGG in CAA24214. (PubMed:6188955)Curated
Sequence conflicti524 – 5241S → G in CAA24214. (PubMed:6188955)Curated
Sequence conflicti532 – 5321H → R in CAA24214. (PubMed:6188955)Curated
Sequence conflicti535 – 5351S → G in CAA24214. (PubMed:6188955)Curated
Sequence conflicti544 – 5441S → G in CAA24214. (PubMed:6188955)Curated
Sequence conflicti548 – 5492GQ → RR in CAA24214. (PubMed:6188955)Curated
Sequence conflicti556 – 5572KS → SGT in CAA24214. (PubMed:6188955)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei97 – 10610YGGSSFGGAG → S in isoform 2 and isoform 3. 1 PublicationVSP_021100
Alternative sequencei144 – 1452GR → EK in isoform 2 and isoform 3. 1 PublicationVSP_021101
Alternative sequencei465 – 4717RGGSGGG → PRRQPRR in isoform 3. 1 PublicationVSP_021102
Alternative sequencei472 – 57099Missing in isoform 3. 1 PublicationVSP_021103Add
BLAST

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: October 29, 2014
This is version 118 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