P08729 (K2C7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	KRT7
Synonyms:	SCL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). Ref.3 Ref.9
Subunit structure	Heterotetramer of two type I and two type II keratins. Interacts with eukaryotic translation initiator factor 3 (eIF3) subunit EIF3S10 and with HPV16 E7. Ref.8 Ref.9
Subcellular location	Cytoplasm Ref.2.
Tissue specificity	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. Ref.1 Ref.4
Induction	Up-regulated by retinoic acid. Ref.2
Post-translational modification	Arg-20 is dimethylated, probably to asymmetric dimethylarginine. Ref.7 Ref.11
Miscellaneous	There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
Sequence similarities	Belongs to the intermediate filament family.
Mass spectrometry	Molecular mass is 51203.48 Da from positions 2 - 469. Determined by MALDI. Ref.10
Sequence caution	The sequence CAA26956.2 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Intermediate filament Keratin
Coding sequence diversity	Polymorphism
Domain	Coiled coil
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from direct assay Ref.3. Source: UniProtKB cytoskeleton organization Non-traceable author statement. Source: UniProtKB interphase Inferred from direct assay Ref.3. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of translation Inferred from direct assay Ref.9. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA keratin filament Inferred from electronic annotation. Source: InterPro nucleus Inferred from direct assay. Source: HPA
Molecular function	protein binding Inferred from physical interaction Ref.8Ref.9. Source: UniProtKB structural molecule activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF3A	Q14152	3	EBI-297833,EBI-366617

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 469	468	Keratin, type II cytoskeletal 7		PRO_0000063725
Regions
	Region	2 – 90	89	Head
	Region	90 – 126	37	Coil 1A
	Region	91 – 399	309	Rod
	Region	92 – 97	6	Interaction with HPV16 E7
	Region	127 – 144	18	Linker 1
	Region	145 – 236	92	Coil 1B
	Region	237 – 260	24	Linker 12
	Region	261 – 399	139	Coil 2
	Region	400 – 469	70	Tail
Sites
	Site	343	1	Stutter
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.7
	Modified residue	7	1	Phosphoserine Ref.17 Ref.18
	Modified residue	14	1	Phosphoserine By similarity
	Modified residue	20	1	Dimethylated arginine; alternate Ref.7 Ref.11
	Modified residue	20	1	Omega-N-methylarginine; alternate Ref.7 Ref.11
	Modified residue	36	1	Phosphoserine Ref.17
	Modified residue	38	1	Phosphoserine Ref.16 Ref.17
	Modified residue	40	1	Phosphotyrosine Ref.16 Ref.20
	Modified residue	45	1	Phosphoserine Ref.14
	Modified residue	53	1	Phosphoserine Ref.17
	Modified residue	55	1	Phosphotyrosine Ref.20
	Modified residue	199	1	N6-acetyllysine Ref.21
	Modified residue	205	1	Phosphotyrosine Ref.13
	Modified residue	252	1	Phosphoserine Ref.19
	Modified residue	254	1	Phosphoserine Ref.12 Ref.19
	Modified residue	296	1	N6-acetyllysine Ref.21
	Modified residue	375	1	Phosphotyrosine Ref.15
	Modified residue	380	1	Phosphoserine Ref.15
Natural variations
	Natural variant	186	1	H → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Corresponds to variant rs6580870 [ dbSNP | Ensembl ].		VAR_060731
	Natural variant	364	1	G → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Corresponds to variant rs2608009 [ dbSNP | Ensembl ].		VAR_016321
Experimental info
	Sequence conflict	79	1	D → G in CAB41416. Ref.3
	Sequence conflict	83 – 84	2	SL → FS in CAB41416. Ref.3
	Sequence conflict	97	1	T → A in CAA26956. Ref.1
	Sequence conflict	97	1	T → A in CAA31695. Ref.2
	Sequence conflict	155	1	L → M in CAB41416. Ref.3
	Sequence conflict	164	1	A → Q in CAA26956. Ref.1
	Sequence conflict	164	1	A → Q in CAA31695. Ref.2
	Sequence conflict	164	1	A → Q in CAB41416. Ref.3
	Sequence conflict	165	1	E → G in CAA26956. Ref.1
	Sequence conflict	165	1	E → G in CAA31695. Ref.2
	Sequence conflict	165	1	E → G in CAB41416. Ref.3
	Sequence conflict	168	1	S → T in CAA26956. Ref.1
	Sequence conflict	168	1	S → T in CAA31695. Ref.2
	Sequence conflict	168	1	S → T in CAB41416. Ref.3
	Sequence conflict	342	1	R → C in CAA26956. Ref.1
	Sequence conflict	342	1	R → C in CAA31695. Ref.2
	Sequence conflict	411	1	V → A in CAB41416. Ref.3
	Sequence conflict	467	1	A → T in CAB41416. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P08729 [UniParc]. Last modified January 11, 2011. Version 5. Checksum: 070CBE8F66A62497	FASTA	469	51,386
	10 20 30 40 50 60 MSIHFSSPVF TSRSAAFSGR GAQVRLSSAR PGGLGSSSLY GLGASRPRVA VRSAYGGPVG 70 80 90 100 110 120 AGIREVTINQ SLLAPLRLDA DPSLQRVRQE ESEQIKTLNN KFASFIDKVR FLEQQNKLLE 130 140 150 160 170 180 TKWTLLQEQK SAKSSRLPDI FEAQIAGLRG QLEALQVDGG RLEAELRSMQ DVVEDFKNKY 190 200 210 220 230 240 EDEINHRTAA ENEFVVLKKD VDAAYMSKVE LEAKVDALND EINFLRTLNE TELTELQSQI 250 260 270 280 290 300 SDTSVVLSMD NSRSLDLDGI IAEVKAQYEE MAKCSRAEAE AWYQTKFETL QAQAGKHGDD 310 320 330 340 350 360 LRNTRNEISE MNRAIQRLQA EIDNIKNQRA KLEAAIAEAE ERGELALKDA RAKQEELEAA 370 380 390 400 410 420 LQRGKQDMAR QLREYQELMS VKLALDIEIA TYRKLLEGEE SRLAGDGVGA VNISVMNSTG 430 440 450 460 GSSSGGGIGL TLGGTMGSNA LSFSSSAGPG LLKAYSIRTA SASRRSARD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2415537] [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: 2459129] [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: 10492017] [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: 12359226] [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: 16541075] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-186 AND ALA-364. Tissue: Pancreas.
[7]	Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB 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, 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: 11169732] [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: 12072504] [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: 11840567] [Abstract] Cited for: MASS SPECTROMETRY. Tissue: Mammary cancer.
[11]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-20, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-205, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[14]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation 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) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-375 AND SER-380, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND TYR-40, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[17]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-36; SER-38 AND SER-53, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND SER-254, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40 AND TYR-55, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[21]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-296, MASS SPECTROMETRY.
[22]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00306959.
PIR	B24177. S05602.
RefSeq	NP_005547.3. NM_005556.3.
UniGene	Hs.411501. Hs.670221.
3D structure databases
ProteinModelPortal	P08729.
SMR	P08729. Positions 89-126, 132-239, 256-401.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08729. 3 interactions.
MINT	MINT-256895.
STRING	P08729.
PTM databases
PhosphoSite	P08729.
Polymorphism databases
DMDM	281185511.
2D gel databases
SWISS-2DPAGE	P08729.
Proteomic databases
PRIDE	P08729.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000331817; ENSP00000329243; ENSG00000135480.
GeneID	3855.
KEGG	hsa:3855.
UCSC	uc001saa.1. human.
Organism-specific databases
CTD	3855.
GeneCards	GC12P052626.
H-InvDB	HIX0037105. HIX0079487. HIX0194260.
HGNC	HGNC:6445. KRT7.
HPA	CAB000028. HPA007272.
MIM	148059. gene.
neXtProt	NX_P08729.
PharmGKB	PA30233.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15294.
HOGENOM	HBG715391.
HOVERGEN	HBG013015.
InParanoid	P08729.
OMA	MSIHFSS.
OrthoDB	EOG4TMR28.
PhylomeDB	P08729.
Gene expression databases
ArrayExpress	P08729.
Bgee	P08729.
CleanEx	HS_KRT7.
Genevestigator	P08729.
GermOnline	ENSG00000135480. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR003054. Keratin_II. IPR009053. Prefoldin. [Graphical view]
KO	K07605.
PANTHER	PTHR23239. IF. 1 hit. PTHR23239:SF18. Keratin_II. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01276. TYPE2KERATIN.
SUPFAM	SSF46579. Prefoldin. 1 hit.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	15169.
SOURCE	Search...

Entry information

Entry name

K2C7_HUMAN

Accession

Primary (citable) accession number: P08729
Secondary accession number(s): Q92676, Q9BUD8, Q9Y3R7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 137 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.