Reviewed, UniProtKB/Swiss-Prot P08729 (K2C7_HUMAN)

Names and origin

Protein names

Recommended name:
    Keratin, type II cytoskeletal 7
Alternative name(s):
    Cytokeratin-7
      Short name=CK-7
      Short name=Keratin-7
      Short name=K7
    Sarcolectin

Gene names

Name:	KRT7
Synonyms:	SCL

Organism

Homo sapiens (Human) [Complete proteome]

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.8
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.7
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.6 Ref.10
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.9
Sequence caution	The sequence CAA26956.2 differs from that shown. Reason: Frameshift at position 22.

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
Gene Ontology (GO)
Biological process	DNA replication Ref.3 Inferred from direct assay. Source: UniProtKB cytoskeleton organization Non-traceable author statement. Source: UniProtKB interphase Ref.3 Inferred from direct assay. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of translation Ref.8 Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Ref.2 Inferred from direct assay. Source: UniProtKB keratin filament Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Ref.7 Ref.8 Inferred from physical interaction. Source: UniProtKB structural molecule activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF3A	Q14152	2	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.6
	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.6
	Modified residue	7	1	Phosphoserine Ref.15 Ref.16
	Modified residue	14	1	Phosphoserine By similarity
	Modified residue	20	1	Dimethylated arginine; alternate Ref.6 Ref.10
	Modified residue	20	1	Omega-N-methylarginine; alternate Ref.6 Ref.10
	Modified residue	36	1	Phosphoserine Ref.15
	Modified residue	38	1	Phosphoserine Ref.15
	Modified residue	40	1	Phosphotyrosine Ref.19
	Modified residue	45	1	Phosphoserine Ref.13
	Modified residue	53	1	Phosphoserine Ref.15
	Modified residue	55	1	Phosphotyrosine Ref.19
	Modified residue	199	1	N6-acetyllysine Ref.20
	Modified residue	205	1	Phosphotyrosine Ref.12
	Modified residue	252	1	Phosphoserine Ref.17
	Modified residue	254	1	Phosphoserine Ref.17 Ref.11
	Modified residue	296	1	N6-acetyllysine Ref.20
	Modified residue	375	1	Phosphotyrosine Ref.14
	Modified residue	380	1	Phosphoserine Ref.14
Natural variations
	Natural variant	364	1	A → G		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 – 165	2	QG → AE in AAN64031. Ref.4
	Sequence conflict	164 – 165	2	QG → AE in AAN64035. Ref.4
	Sequence conflict	164 – 165	2	QG → AE in AAH02700. Ref.5
	Sequence conflict	168	1	T → S in AAN64031. Ref.4
	Sequence conflict	168	1	T → S in AAN64035. Ref.4
	Sequence conflict	168	1	T → S in AAH02700. Ref.5
	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)
	P08729-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 26578B9D40DFF5CF	FASTA	469	51,418
	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 RLEQGLRTMQ DVVEDFKNKY 190 200 210 220 230 240 EDEINRRTAA 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 LQRAKQDMAR 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. 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.
[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. 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, VARIANT GLY-364. Tissue: Keratinocyte.
[5]	"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]. Tissue: Pancreas.
[6]	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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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.
[13]	"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: Epithelium.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"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.
[20]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X03212 mRNA. Translation: CAA26956.2. Frameshift. 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. BC002700 mRNA. Translation: AAH02700.1.
IPI	IPI00306959.
PIR	B24177. S05602.
RefSeq	NP_005547.3.
UniGene	Hs.411501 Hs.670221
3D structure databases
HSSP	HSSP built from PDB template 1GK7 based on UniProtKB P08670.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08729. 4 interactions.
STRING	P08729.
PTM databases
PhosphoSite	P08729.
2-D gel databases
SWISS-2DPAGE	P08729.
Proteomic databases
PRIDE	P08729.
Genome annotation databases
Ensembl	ENST00000331817; ENSP00000329243; ENSG00000135480; Homo sapiens. [Genome view] ENST00000422319; ENSP00000393966; ENSG00000135480; Homo sapiens. [Genome view]
GeneID	3855.
KEGG	hsa:3855.
UCSC	uc001saa.1. human.
Organism-specific databases
CTD	3855.
GeneCards	GC12P050913.
H-InvDB	HIX0037105. HIX0079487.
HGNC	HGNC:6445. KRT7.
HPA	CAB000028. HPA007272.
MIM	148059. gene.
PharmGKB	PA30233.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P08729.
HOVERGEN	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. [Graphical view]
PANTHER	PTHR23239. IF. 1 hit. PTHR23239:SF18. Keratin_II. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01276. TYPE2KERATIN.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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 23, 2007
Last modified:	November 3, 2009
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.