P05787 (K2C8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Keratin, type II cytoskeletal 8

Alternative name(s):
Cytokeratin-8
Short name=CK-8
Keratin-8
Short name=K8
Type-II keratin Kb8

Gene names

Name:	KRT8
Synonyms:	CYK8

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	483 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	Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. Ref.20
Subunit structure	Heterotetramer of two type I and two type II keratins. KRT8 associates with KRT18. Associates with KRT20. Interacts with HCV core protein and PNN. When associated with KRT19, interacts with DMD. Interacts with TCHP. Interacts with APEX1. Ref.14 Ref.15 Ref.18 Ref.20 Ref.21 Ref.23 Ref.31
Subcellular location	Cytoplasm. Nucleus › nucleoplasm By similarity. Nucleus matrix By similarity Ref.14 Ref.31.
Tissue specificity	Observed in muscle fibers accumulating in the costameres of myoplasm at the sarcolemma membrane in structures that contain dystrophin and spectrin. Expressed in gingival mucosa and hard palate of the oral cavity. Ref.14 Ref.20
Post-translational modification	Phosphorylation on serine residues is enhanced during EGF stimulation and mitosis. Ser-74 phosphorylation plays an important role in keratin filament reorganization. O-glycosylated at multiple sites; glycans consist of single N-acetylglucosamine residues. Ref.12
Involvement in disease	Defects in KRT8 are a cause of cirrhosis (CIRRH) [MIM:215600]. Ref.35
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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Intermediate filament Keratin Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Coiled coil
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cytoskeleton organization Non-traceable author statement. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay Ref.31. Source: UniProtKB keratin filament Inferred from electronic annotation. Source: InterPro nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction Ref.23Ref.31. Source: UniProtKB structural molecule activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	3	EBI-297852,EBI-401755
IKBKG	Q9Y6K9	2	EBI-297852,EBI-81279
KRT18	P05783	8	EBI-297852,EBI-297888

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 483	482	Keratin, type II cytoskeletal 8		PRO_0000063740
Regions
	Region	2 – 90	89	Head
	Region	91 – 398	308	Rod
	Region	91 – 126	36	Coil 1A
	Region	127 – 143	17	Linker 1
	Region	144 – 235	92	Coil 1B
	Region	236 – 259	24	Linker 12
	Region	260 – 398	139	Coil 2
	Region	261 – 382	122	Necessary for interaction with PNN
	Region	399 – 483	85	Tail
	Compositional bias	9 – 49	41	Ser-rich
Sites
	Site	342	1	Stutter
Amino acid modifications
	Modified residue	9	1	Phosphoserine; by PKC/PRKCE Ref.13
	Modified residue	13	1	Phosphoserine Ref.28
	Modified residue	14	1	Phosphothreonine Ref.28
	Modified residue	21	1	Phosphoserine Ref.19 Ref.28 Ref.30
	Modified residue	22	1	Phosphoserine Ref.19 Ref.28
	Modified residue	24	1	Phosphoserine; by PKC/PRKCE Ref.4 Ref.13 Ref.19 Ref.27 Ref.28 Ref.30 Ref.32
	Modified residue	26	1	Phosphothreonine Ref.27 Ref.28
	Modified residue	27	1	Phosphoserine Ref.24 Ref.30
	Modified residue	34	1	Phosphoserine Ref.28 Ref.30
	Modified residue	36	1	Phosphoserine Ref.28 Ref.30
	Modified residue	37	1	Phosphoserine Ref.19 Ref.28 Ref.29 Ref.30
	Modified residue	39	1	Phosphoserine Ref.28
	Modified residue	43	1	Phosphoserine Ref.19 Ref.28 Ref.29 Ref.30 Ref.32
	Modified residue	44	1	Phosphoserine By similarity
	Modified residue	74	1	Phosphoserine; by MAPK Ref.16 Ref.17 Ref.28 Ref.29
	Modified residue	117	1	N6-acetyllysine Ref.33
	Modified residue	204	1	Phosphotyrosine Ref.26
	Modified residue	207	1	N6-acetyllysine Ref.33
	Modified residue	243	1	Phosphoserine Ref.28
	Modified residue	251	1	Phosphoserine Ref.30
	Modified residue	253	1	Phosphoserine Ref.22 Ref.29 Ref.30 Ref.32
	Modified residue	258	1	Phosphoserine Ref.28 Ref.29 Ref.30
	Modified residue	267	1	Phosphotyrosine Ref.26
	Modified residue	274	1	Phosphoserine Ref.29 Ref.30
	Modified residue	295	1	N6-acetyllysine Ref.33
	Modified residue	325	1	N6-acetyllysine Ref.33
	Modified residue	330	1	Phosphoserine Ref.22 Ref.28 Ref.30
	Modified residue	347	1	N6-acetyllysine Ref.33
	Modified residue	400	1	Phosphoserine Ref.28 Ref.30
	Modified residue	410	1	Phosphoserine Ref.28 Ref.30
	Modified residue	417	1	Phosphoserine By similarity
	Modified residue	424	1	Phosphoserine By similarity
	Modified residue	432	1	Phosphoserine; by CaMK2 and MAPK Ref.4 Ref.30 Ref.32
	Modified residue	438	1	Phosphoserine Ref.28
	Modified residue	441	1	Phosphoserine Ref.28
	Modified residue	442	1	Phosphoserine Ref.28
	Modified residue	451	1	Phosphoserine Ref.25
	Modified residue	456	1	Phosphoserine Ref.28
	Modified residue	475	1	Phosphoserine Ref.28 Ref.30 Ref.32
	Modified residue	478	1	Phosphoserine Ref.28 Ref.30
Natural variations
	Natural variant	53	1	G → V in CIRRH. Ref.35 Corresponds to variant rs61710484 [ dbSNP | Ensembl ].		VAR_023058
	Natural variant	54	1	Y → C in CIRRH. Ref.35		VAR_023059
	Natural variant	62	1	G → C in CIRRH. Ref.8 Ref.35 Corresponds to variant rs11554495 [ dbSNP | Ensembl ].		VAR_023060
	Natural variant	63	1	I → V. Ref.35 Corresponds to variant rs59536457 [ dbSNP | Ensembl ].		VAR_023061
	Natural variant	401	1	R → W. Corresponds to variant rs2277330 [ dbSNP | Ensembl ].		VAR_049805
Experimental info
	Mutagenesis	72	1	L → P: Increases phosphorylation. Ref.17
	Mutagenesis	74	1	S → A: Generates normal-appearing filaments, that remain stable after okadaic acid treatment. Ref.17
	Mutagenesis	74	1	S → D: Generates normal-appearing filaments, that are destabilized by okadaic acid. Ref.17
	Sequence conflict	56	1	G → V in BAF83627. Ref.5
	Sequence conflict	77	1	V → S in AAA35748. Ref.2
	Sequence conflict	201	1	D → DVD in CAA52882. Ref.3
	Sequence conflict	232	1	I → L in CAA67203. Ref.10
	Sequence conflict	257	1	D → E in AAA35748. Ref.2
	Sequence conflict	310	1	M → I in CAA31376. Ref.10
	Sequence conflict	324	1	L → F in BAD96661. Ref.6
	Sequence conflict	384	1	L → M in CAA67203. Ref.10
	Sequence conflict	387	1	E → D in AAA35748. Ref.2
	Sequence conflict	401	1	R → P in AAA35748. Ref.2
	Sequence conflict	417	1	S → G in AAA35763. Ref.1
	Sequence conflict	417	1	S → G in AAA35748. Ref.2
	Sequence conflict	417	1	S → G in CAA67203. Ref.10
	Sequence conflict	417	1	S → G in CAA31376. Ref.10
	Sequence conflict	429	1	G → D in AAA35748. Ref.2
	Sequence conflict	429	1	G → D in CAA31376. Ref.10
	Sequence conflict	430 – 433	4	LTSP → SQA in AAA35763. Ref.1
	Sequence conflict	431	1	T → A in CAA67203. Ref.10
	Sequence conflict	432	1	S → D in AAA35748. Ref.2
	Sequence conflict	432	1	S → D in CAA67203. Ref.10
	Sequence conflict	432	1	S → D in CAA31376. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P05787 [UniParc]. Last modified January 23, 2007. Version 7. Checksum: B0BC730B65929D37	FASTA	483	53,704
	10 20 30 40 50 60 MSIRVTQKSY KVSTSGPRAF SSRSYTSGPG SRISSSSFSR VGSSNFRGGL GGGYGGASGM 70 80 90 100 110 120 GGITAVTVNQ SLLSPLVLEV DPNIQAVRTQ EKEQIKTLNN KFASFIDKVR FLEQQNKMLE 130 140 150 160 170 180 TKWSLLQQQK TARSNMDNMF ESYINNLRRQ LETLGQEKLK LEAELGNMQG LVEDFKNKYE 190 200 210 220 230 240 DEINKRTEME NEFVLIKKDV DEAYMNKVEL ESRLEGLTDE INFLRQLYEE EIRELQSQIS 250 260 270 280 290 300 DTSVVLSMDN SRSLDMDSII AEVKAQYEDI ANRSRAEAES MYQIKYEELQ SLAGKHGDDL 310 320 330 340 350 360 RRTKTEISEM NRNISRLQAE IEGLKGQRAS LEAAIADAEQ RGELAIKDAN AKLSELEAAL 370 380 390 400 410 420 QRAKQDMARQ LREYQELMNV KLALDIEIAT YRKLLEGEES RLESGMQNMS IHTKTTSGYA 430 440 450 460 470 480 GGLSSAYGGL TSPGLSYSLG SSFGSGAGSS SFSRTSSSRA VVVKKIETRD GKLVSESSDV LPK

References

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[1]	"Organization and sequence of the human gene encoding cytokeratin 8." Krauss S., Franke W.W. Gene 86:241-249(1990) [PubMed: 1691124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and sequence of cDNA for human placental cytokeratin 8. Regulation of the mRNA in trophoblastic cells by cAMP." Yamamoto R., Kao L.C., McKnight C.E., Strauss J.F. III Mol. Endocrinol. 4:370-374(1990) [PubMed: 1692965] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Embryonic simple epithelial keratins 8 and 18: chromosomal location emphasizes difference from other keratin pairs." Waseem A., Alexander C.M., Steel J.B., Lane E.B. New Biol. 2:464-478(1990) [PubMed: 1705144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Placenta.
[4]	"Phosphorylation of human keratin 8 in vivo at conserved head domain serine 23 and at epidermal growth factor-stimulated tail domain serine 431." Ku N.-O., Omary M.B. J. Biol. Chem. 272:7556-7564(1997) [PubMed: 9054461] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-24 AND SER-432.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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], VARIANT CYS-62. Tissue: Colon, Liver, Lung and Placenta.
[9]	"Posttranslational regulation of keratins: degradation of mouse and human keratins 18 and 8." Kulesh D.A., Cecena G., Darmon Y.M., Vasseur M., Oshima R.G. Mol. Cell. Biol. 9:1553-1565(1989) [PubMed: 2471065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-231.
[10]	"Cytokeratin expression in simple epithelia. III. Detection of mRNAs encoding human cytokeratins nos. 8 and 18 in normal and tumor cells by hybridization with cDNA sequences in vitro and in situ." Leube R.E., Bosch F.X., Romano V., Zimbelmann R., Hofler H., Franke W.W. Differentiation 33:69-85(1986) [PubMed: 2434381] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 205-483.
[11]	"A two-dimensional gel database of human colon carcinoma proteins." Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J. Electrophoresis 18:605-613(1997) [PubMed: 9150948] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Colon carcinoma.
[12]	"Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18." Chou C.F., Smith A.J., Omary M.B. J. Biol. Chem. 267:3901-3906(1992) [PubMed: 1371281] [Abstract] Cited for: GLYCOSYLATION.
[13]	"PKC epsilon-related kinase associates with and phosphorylates cytokeratin 8 and 18." Omary M.B., Baxter G.T., Chou C.F., Riopel C.L., Lin W.Y., Strulovici B. J. Cell Biol. 117:583-593(1992) [PubMed: 1374067] [Abstract] Cited for: PHOSPHORYLATION AT SER-9 AND SER-24.
[14]	"An immunohistological study of cytokeratin 20 in human and mammalian oral epithelium." Barrett A.W., Cort E.M., Patel P., Berkovitz B.K.B. Arch. Oral Biol. 45:879-887(2000) [PubMed: 10973561] [Abstract] Cited for: INTERACTION WITH KRT20, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]	"Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus." Shi J., Sugrue S.P. J. Biol. Chem. 275:14910-14915(2000) [PubMed: 10809736] [Abstract] Cited for: INTERACTION WITH PNN.
[16]	"The intermediate filament protein keratin 8 is a novel cytoplasmic substrate for c-Jun N-terminal kinase." He T., Stepulak A., Holmstrom T.H., Omary M.B., Eriksson J.E. J. Biol. Chem. 277:10767-10774(2002) [PubMed: 11781324] [Abstract] Cited for: PHOSPHORYLATION AT SER-74.
[17]	"Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation." Ku N.O., Azhar S., Omary M.B. J. Biol. Chem. 277:10775-10782(2002) [PubMed: 11788583] [Abstract] Cited for: PHOSPHORYLATION AT SER-74, MUTAGENESIS OF LEU-72 AND SER-74.
[18]	"Identification of trichoplein, a novel keratin filament-binding protein." Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T., Usukura J., Inagaki M. J. Cell Sci. 118:1081-1090(2005) [PubMed: 15731013] [Abstract] Cited for: INTERACTION WITH TCHP.
[19]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-22; SER-24; SER-37 AND SER-43, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[20]	"Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19." Stone M.R., O'Neill A., Catino D., Bloch R.J. Mol. Biol. Cell 16:4280-4293(2005) [PubMed: 16000376] [Abstract] Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
[21]	"Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein." Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W. Proteomics 5:2227-2237(2005) [PubMed: 15846844] [Abstract] Cited for: INTERACTION WITH HCV CORE PROTEIN.
[22]	"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-253 AND SER-330, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Keratin 20 serine 13 phosphorylation is a stress and intestinal goblet cell marker." Zhou Q., Cadrin M., Herrmann H., Chen C.-H., Chalkley R.J., Burlingame A.L., Omary M.B. J. Biol. Chem. 281:16453-16461(2006) [PubMed: 16608857] [Abstract] Cited for: INTERACTION WITH KRT20.
[24]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[26]	"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-204 AND TYR-267, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[27]	"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-24 AND THR-26, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"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-13; THR-14; SER-21; SER-22; SER-24; THR-26; SER-34; SER-36; SER-37; SER-39; SER-43; SER-74; SER-243; SER-258; SER-330; SER-400; SER-410; SER-438; SER-441; SER-442; SER-456; SER-475 AND SER-478, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"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-37; SER-43; SER-74; SER-253; SER-258 AND SER-274, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"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-21; SER-24; SER-27; SER-34; SER-36; SER-37; SER-43; SER-251; SER-253; SER-258; SER-274; SER-330; SER-400; SER-410; SER-432; SER-475 AND SER-478, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[31]	"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process." Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G. Mol. Cell. Biol. 29:1834-1854(2009) [PubMed: 19188445] [Abstract] Cited for: INTERACTION WITH APEX1, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[32]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-43; SER-253; SER-432 AND SER-475, MASS SPECTROMETRY.
[33]	"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-117; LYS-207; LYS-295; LYS-325 AND LYS-347, MASS SPECTROMETRY.
[34]	"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].
[35]	"Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies." Ku N.-O., Darling J.M., Krams S.M., Esquivel C.O., Keeffe E.B., Sibley R.K., Lee Y.M., Wright T.L., Omary M.B. Proc. Natl. Acad. Sci. U.S.A. 100:6063-6068(2003) [PubMed: 12724528] [Abstract] Cited for: VARIANTS CIRRH VAL-53; CYS-54 AND CYS-62, VARIANT VAL-63.
+	Additional computationally mapped references.

Web resources

Human Intermediate Filament Mutation Database

Cross-references

Sequence databases
EMBL GenBank DDBJ	M34482 Genomic DNA. Translation: AAA35763.1. M34225 mRNA. Translation: AAA35748.1. X74929 mRNA. Translation: CAA52882.1. X74981 Genomic DNA. Translation: CAA52916.1. U76549 mRNA. Translation: AAB18966.1. AK222941 mRNA. Translation: BAD96661.1. AK290938 mRNA. Translation: BAF83627.1. AK315826 mRNA. Translation: BAF98717.1. CH471054 Genomic DNA. Translation: EAW96653.1. BC000654 mRNA. Translation: AAH00654.3. BC063513 mRNA. Translation: AAH63513.2. BC073760 mRNA. Translation: AAH73760.1. BC075839 mRNA. Translation: AAH75839.1. M26512 mRNA. Translation: AAA51542.1. X12882 mRNA. Translation: CAA31376.1. X98614 mRNA. Translation: CAA67203.1.
IPI	IPI00554648.
PIR	A34720.
RefSeq	NP_002264.1. NM_002273.3.
UniGene	Hs.533782. Hs.708445.
3D structure databases
ProteinModelPortal	P05787.
SMR	P05787. Positions 89-126, 131-238, 255-400.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-424N.
IntAct	P05787. 11 interactions.
MINT	MINT-256526.
STRING	P05787.
PTM databases
GlycoSuiteDB	P05787.
PhosphoSite	P05787.
Polymorphism databases
DMDM	90110027.
2D gel databases
SWISS-2DPAGE	P05787.
Siena-2DPAGE	P05787.
Proteomic databases
PeptideAtlas	P05787.
PRIDE	P05787.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000293308; ENSP00000293308; ENSG00000170421.
GeneID	3856.
KEGG	hsa:3856.
UCSC	uc001sbd.1. human.
Organism-specific databases
CTD	3856.
GeneCards	GC12M053290.
H-InvDB	HIX0010658. HIX0026255. HIX0034365.
HGNC	HGNC:6446. KRT8.
HPA	CAB000131. CAB001696.
MIM	148060. gene. 215600. phenotype.
neXtProt	NX_P05787.
PharmGKB	PA30234.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14428.
HOVERGEN	HBG013015.
InParanoid	P05787.
OMA	TDMENEF.
OrthoDB	EOG4XKV78.
PhylomeDB	P05787.
Enzyme and pathway databases
Pathway_Interaction_DB	p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.
Gene expression databases
ArrayExpress	P05787.
Bgee	P05787.
Genevestigator	P05787.
GermOnline	ENSG00000170421. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR003054. Keratin_II. [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.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00009. Alteplase. DB00029. Anistreplase. DB00015. Reteplase. DB00031. Tenecteplase.
NextBio	15173.
PMAP-CutDB	P05787.
SOURCE	Search...

Entry information

Entry name

K2C8_HUMAN

Accession

Primary (citable) accession number: P05787
Secondary accession number(s): A8K4H3 , B0AZN5, Q14099, Q14716, Q14717, Q53GJ0, Q6DHW5, Q6GMY0, Q6P4C7, Q96J60

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 151 of the entry and version 7 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.