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P08729

- K2C7_HUMAN

UniProt

P08729 - K2C7_HUMAN

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Protein

Keratin, type II cytoskeletal 7

Gene

KRT7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Blocks interferon-dependent interphase and stimulates DNA synthesis in cells. Involved in the translational regulation of the human papillomavirus type 16 E7 mRNA (HPV16 E7).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei343 – 3431Stutter

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cytoskeletal 7
Alternative name(s):
Cytokeratin-7
Short name:
CK-7
Keratin-7
Short name:
K7
Sarcolectin
Type-II keratin Kb7
Gene namesi
Name:KRT7
Synonyms:SCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6445. KRT7.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. intermediate filament Source: UniProtKB
  4. keratin filament Source: InterPro
  5. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30233.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 469468Keratin, type II cytoskeletal 7PRO_0000063725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei20 – 201Dimethylated arginine; alternate1 Publication
Modified residuei20 – 201Omega-N-methylarginine; alternate1 Publication
Modified residuei179 – 1791N6-acetyllysine1 Publication
Modified residuei252 – 2521Phosphoserine1 Publication
Modified residuei254 – 2541Phosphoserine1 Publication

Post-translational modificationi

Arg-20 is dimethylated, probably to asymmetric dimethylarginine.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP08729.
PaxDbiP08729.
PRIDEiP08729.

2D gel databases

SWISS-2DPAGEP08729.

PTM databases

PhosphoSiteiP08729.

Expressioni

Tissue specificityi

Expressed in cultured epidermal, bronchial and mesothelial cells but absent in colon, ectocervix and liver. Observed throughout the glandular cells in the junction between stomach and esophagus but is absent in the esophagus.2 Publications

Inductioni

Up-regulated by retinoic acid.1 Publication

Gene expression databases

BgeeiP08729.
CleanExiHS_KRT7.
GenevestigatoriP08729.

Organism-specific databases

HPAiCAB000028.
HPA007272.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. Interacts with eukaryotic translation initiator factor 3 (eIF3) subunit EIF3S10 and with HPV16 E7. Interacts with GPER1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF3AQ141523EBI-297833,EBI-366617

Protein-protein interaction databases

BioGridi110053. 10 interactions.
IntActiP08729. 6 interactions.
MINTiMINT-256895.
STRINGi9606.ENSP00000329243.

Structurei

3D structure databases

ProteinModelPortaliP08729.
SMRiP08729. Positions 88-240, 256-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9089HeadAdd
BLAST
Regioni90 – 12637Coil 1AAdd
BLAST
Regioni91 – 399309RodAdd
BLAST
Regioni92 – 976Interaction with HPV16 E7
Regioni127 – 14418Linker 1Add
BLAST
Regioni145 – 23692Coil 1BAdd
BLAST
Regioni237 – 26024Linker 12Add
BLAST
Regioni261 – 399139Coil 2Add
BLAST
Regioni400 – 46970TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG145985.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP08729.
KOiK07605.
OMAiMSIHFSS.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP08729.
TreeFamiTF317854.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08729-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIHFSSPVF TSRSAAFSGR GAQVRLSSAR PGGLGSSSLY GLGASRPRVA
60 70 80 90 100
VRSAYGGPVG AGIREVTINQ SLLAPLRLDA DPSLQRVRQE ESEQIKTLNN
110 120 130 140 150
KFASFIDKVR FLEQQNKLLE TKWTLLQEQK SAKSSRLPDI FEAQIAGLRG
160 170 180 190 200
QLEALQVDGG RLEAELRSMQ DVVEDFKNKY EDEINHRTAA ENEFVVLKKD
210 220 230 240 250
VDAAYMSKVE LEAKVDALND EINFLRTLNE TELTELQSQI SDTSVVLSMD
260 270 280 290 300
NSRSLDLDGI IAEVKAQYEE MAKCSRAEAE AWYQTKFETL QAQAGKHGDD
310 320 330 340 350
LRNTRNEISE MNRAIQRLQA EIDNIKNQRA KLEAAIAEAE ERGELALKDA
360 370 380 390 400
RAKQEELEAA LQRGKQDMAR QLREYQELMS VKLALDIEIA TYRKLLEGEE
410 420 430 440 450
SRLAGDGVGA VNISVMNSTG GSSSGGGIGL TLGGTMGSNA LSFSSSAGPG
460
LLKAYSIRTA SASRRSARD
Length:469
Mass (Da):51,386
Last modified:January 11, 2011 - v5
Checksum:i070CBE8F66A62497
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791D → G in CAB41416. (PubMed:10492017)Curated
Sequence conflicti83 – 842SL → FS in CAB41416. (PubMed:10492017)Curated
Sequence conflicti97 – 971T → A in CAA26956. (PubMed:2415537)Curated
Sequence conflicti97 – 971T → A in CAA31695. (PubMed:2459129)Curated
Sequence conflicti155 – 1551L → M in CAB41416. (PubMed:10492017)Curated
Sequence conflicti164 – 1641A → Q in CAA26956. (PubMed:2415537)Curated
Sequence conflicti164 – 1641A → Q in CAA31695. (PubMed:2459129)Curated
Sequence conflicti164 – 1641A → Q in CAB41416. (PubMed:10492017)Curated
Sequence conflicti165 – 1651E → G in CAA26956. (PubMed:2415537)Curated
Sequence conflicti165 – 1651E → G in CAA31695. (PubMed:2459129)Curated
Sequence conflicti165 – 1651E → G in CAB41416. (PubMed:10492017)Curated
Sequence conflicti168 – 1681S → T in CAA26956. (PubMed:2415537)Curated
Sequence conflicti168 – 1681S → T in CAA31695. (PubMed:2459129)Curated
Sequence conflicti168 – 1681S → T in CAB41416. (PubMed:10492017)Curated
Sequence conflicti342 – 3421R → C in CAA26956. (PubMed:2415537)Curated
Sequence conflicti342 – 3421R → C in CAA31695. (PubMed:2459129)Curated
Sequence conflicti411 – 4111V → A in CAB41416. (PubMed:10492017)Curated
Sequence conflicti467 – 4671A → T in CAB41416. (PubMed:10492017)Curated

Mass spectrometryi

Molecular mass is 51203.48 Da from positions 2 - 469. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti186 – 1861H → R.6 Publications
Corresponds to variant rs6580870 [ dbSNP | Ensembl ].
VAR_060731
Natural varianti364 – 3641G → A.5 Publications
Corresponds to variant rs2608009 [ dbSNP | Ensembl ].
VAR_016321

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03212 mRNA. Translation: CAA26956.2. Sequence problems.
X13320
, X13346, X13347, X13348, X13349, X13350, X13351, X13352, X13353 Genomic DNA. Translation: CAA31695.1.
AJ238246 mRNA. Translation: CAB41416.1.
AF509887 mRNA. Translation: AAN64031.1.
AF509892, AF509891 Genomic DNA. Translation: AAN64035.1.
AC007338 Genomic DNA. No translation available.
AC007494 Genomic DNA. No translation available.
BC002700 mRNA. Translation: AAH02700.1.
CCDSiCCDS8822.1.
PIRiB24177.
S05602.
RefSeqiNP_005547.3. NM_005556.3.
UniGeneiHs.411501.
Hs.670221.

Genome annotation databases

EnsembliENST00000331817; ENSP00000329243; ENSG00000135480.
GeneIDi3855.
KEGGihsa:3855.
UCSCiuc001saa.1. human.

Polymorphism databases

DMDMi317373583.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03212 mRNA. Translation: CAA26956.2 . Sequence problems.
X13320
, X13346 , X13347 , X13348 , X13349 , X13350 , X13351 , X13352 , X13353 Genomic DNA. Translation: CAA31695.1 .
AJ238246 mRNA. Translation: CAB41416.1 .
AF509887 mRNA. Translation: AAN64031.1 .
AF509892 , AF509891 Genomic DNA. Translation: AAN64035.1 .
AC007338 Genomic DNA. No translation available.
AC007494 Genomic DNA. No translation available.
BC002700 mRNA. Translation: AAH02700.1 .
CCDSi CCDS8822.1.
PIRi B24177.
S05602.
RefSeqi NP_005547.3. NM_005556.3.
UniGenei Hs.411501.
Hs.670221.

3D structure databases

ProteinModelPortali P08729.
SMRi P08729. Positions 88-240, 256-398.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110053. 10 interactions.
IntActi P08729. 6 interactions.
MINTi MINT-256895.
STRINGi 9606.ENSP00000329243.

Chemistry

DrugBanki DB01087. Primaquine.

PTM databases

PhosphoSitei P08729.

Polymorphism databases

DMDMi 317373583.

2D gel databases

SWISS-2DPAGE P08729.

Proteomic databases

MaxQBi P08729.
PaxDbi P08729.
PRIDEi P08729.

Protocols and materials databases

DNASUi 3855.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331817 ; ENSP00000329243 ; ENSG00000135480 .
GeneIDi 3855.
KEGGi hsa:3855.
UCSCi uc001saa.1. human.

Organism-specific databases

CTDi 3855.
GeneCardsi GC12P052626.
H-InvDB HIX0010643.
HIX0079487.
HGNCi HGNC:6445. KRT7.
HPAi CAB000028.
HPA007272.
MIMi 148059. gene.
neXtProti NX_P08729.
PharmGKBi PA30233.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG145985.
GeneTreei ENSGT00760000118796.
HOGENOMi HOG000230976.
HOVERGENi HBG013015.
InParanoidi P08729.
KOi K07605.
OMAi MSIHFSS.
OrthoDBi EOG7FV3Q8.
PhylomeDBi P08729.
TreeFami TF317854.

Miscellaneous databases

ChiTaRSi KRT7. human.
GeneWikii Keratin_7.
GenomeRNAii 3855.
NextBioi 15169.
PROi P08729.
SOURCEi Search...

Gene expression databases

Bgeei P08729.
CleanExi HS_KRT7.
Genevestigatori P08729.

Family and domain databases

InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
IPR009053. Prefoldin.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
Pfami PF00038. Filament. 1 hit.
[Graphical view ]
PRINTSi PR01276. TYPE2KERATIN.
SUPFAMi SSF46579. SSF46579. 1 hit.
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and expression of a human type II mesothelial keratin."
    Glass C., Kim K.H., Fuchs E.
    J. Cell Biol. 101:2366-2373(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS ARG-186 AND ALA-364.
    Tissue: Mesothelium.
  2. "Isolation, sequence, and differential expression of a human K7 gene in simple epithelial cells."
    Glass C., Fuchs E.
    J. Cell Biol. 107:1337-1350(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION, VARIANTS ARG-186 AND ALA-364.
  3. "Sarcolectin (SCL): structure and expression of the recombinant molecule."
    Kaba A., Jiang P., Chany-Fournier F., Chany C.
    Biochimie 81:709-715(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS ARG-186 AND ALA-364.
    Tissue: Placenta.
  4. "Cloning of human, murine, and marsupial keratin 7 and a survey of K7 expression in the mouse."
    Smith F.J.D., Porter R.M., Corden L.D., Lunny D.P., Lane E.B., McLean W.H.I.
    Biochem. Biophys. Res. Commun. 297:818-827(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, VARIANTS ARG-186 AND ALA-364.
    Tissue: Keratinocyte.
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-186 AND ALA-364.
    Tissue: Pancreas.
  7. Cited for: PROTEIN SEQUENCE OF 2-48; 53-96; 102-110; 123-130; 137-161; 178-208; 215-273; 277-296; 306-313; 318-326; 330-348; 352-363 AND 374-402, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT ARG-20, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma and Ovarian carcinoma.
  8. "Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7."
    Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.
    J. Cell. Biochem. 80:483-490(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF3S10.
  9. "Translational regulation of human papillomavirus type 16 E7 mRNA by the peptide SEQIKA, shared by rabbit alpha(1)-globin and human cytokeratin 7."
    Kanduc D.
    J. Virol. 76:7040-7048(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HPV16 E7.
  10. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
    Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
    Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Tissue: Mammary cancer.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "G protein-coupled estrogen receptor 1/G protein-coupled receptor 30 localizes in the plasma membrane and traffics intracellularly on cytokeratin intermediate filaments."
    Sanden C., Broselid S., Cornmark L., Andersson K., Daszkiewicz-Nilsson J., Martensson U.E., Olde B., Leeb-Lundberg L.M.
    Mol. Pharmacol. 79:400-410(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPER1.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiK2C7_HUMAN
AccessioniPrimary (citable) accession number: P08729
Secondary accession number(s): Q92676, Q9BUD8, Q9Y3R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 164 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3