Reviewed, UniProtKB/Swiss-Prot P04264 (K2C1_HUMAN)

Names and origin

Protein names

Recommended name:
    Keratin, type II cytoskeletal 1
Alternative name(s):
    Cytokeratin-1
      Short name=CK-1
    Keratin-1
      Short name=K1
    67 kDa cytokeratin
    Hair alpha protein

Gene names

Name:	KRT1
Synonyms:	KRTA

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	644 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	May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein kinase C (RACK1/GNB2L1). Ref.16
Subunit structure	Heterotetramer of two type I and two type II keratins. Keratin-1 is generally associated with keratin-10. Interacts with ITGB1 in the presence of GNB2L1 and SRC, and with GNB2L1. Ref.16
Subcellular location	Cell membrane. Note: Located on plasma membrane of neuroblastoma NMB7 cells. Ref.16
Tissue specificity	The source of this protein is neonatal foreskin. The 67-kDa type II keratins are expressed in terminally differentiating epidermis.
Post-translational modification	Undergoes deimination of some arginine residues (citrullination).
Polymorphism	There are two size variants of KRT1, termed allele 1A and allele 1B with allelic frequencies of 0.61 and 0.39. Allele 1B lacks 7 residues compared to allele 1A.
Involvement in disease	Defects in KRT1 are a cause of bullous congenital ichthyosiform erythroderma (BCIE) [MIM:113800]; also known as epidermolytic hyperkeratosis (EHK) or bullous erythroderma ichthyosiformis congenita of Brocq. BCIE is an autosomal dominant skin disorder characterized by widespread blistering and an ichthyotic erythroderma at birth that persist into adulthood. Histologically there is a diffuse epidermolytic degeneration in the lower spinous layer of the epidermis. Within a few weeks from birth, erythroderma and blister formation diminish and hyperkeratoses develop. Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.29 Ref.31 Ref.32 Ref.33 Ref.35 Defects in KRT1 are the cause of ichthyosis hystrix Curth-Macklin type (IHCM) [MIM:146590]. IHCM is a genodermatosis with severe verrucous hyperkeratosis. Affected individuals manifest congenital verrucous black scale on the scalp, neck, and limbs with truncal erythema, palmoplantar keratoderma and keratoses on the lips, ears, nipples and buttocks. Ref.12 Defects in KRT1 are a cause of palmoplantar keratoderma non-epidermolytic (NEPPK) [MIM:600962]. NEPKK is a dermatological disorder characterized by focal palmoplantar keratoderma with oral, genital, and follicular lesions. Ref.3 Ref.26 Defects in KRT1 are a cause of ichthyosis annular epidermolytic (AEI) [MIM:607602]; also known as cyclic ichthyosis with epidermolytic hyperkeratosis. AEI is a skin disorder resembling bullous congenital ichthyosiform erythroderma. Affected individuals present with bullous ichthyosis in early childhood and hyperkeratotic lichenified plaques in the flexural areas and extensor surfaces at later ages. The feature that distinguishes AEI from BCIE is dramatic episodes of flares of annular polycyclic plaques with scale, which coalesce to involve most of the body surface and can persist for several weeks or even months. Ref.28 Ref.30 Defects in KRT1 are the cause of palmoplantar keratoderma striate type 3 (SPPK3) [MIM:607654]; also known as keratosis palmoplantaris striata III. SPPK3 is a dermatological disorder affecting palm and sole skin where stratum corneum and epidermal layers are thickened. There is no involvement of non-palmoplantar skin, and both hair and nails are normal. Ref.14
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
Cellular component	Cell membrane Intermediate filament Keratin Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Ichthyosis Palmoplantar keratoderma
Domain	Coiled coil
PTM	Citrullination Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	complement activation, lectin pathway Inferred from physical interaction. Source: UniProtKB epidermis development Ref.22 Traceable author statement. Source: ProtInc fibrinolysis Non-traceable author statement. Source: UniProtKB regulation of angiogenesis Non-traceable author statement. Source: UniProtKB response to oxidative stress Non-traceable author statement. Source: UniProtKB
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from mutant phenotype. Source: UniProtKB receptor activity Non-traceable author statement. Source: UniProtKB structural constituent of cytoskeleton Ref.22 Traceable author statement. Source: ProtInc sugar binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDM2	Q00987	1	EBI-298429,EBI-389668

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 644	643	Keratin, type II cytoskeletal 1		PRO_0000063709
Regions
	Region	2 – 179	178	Head
	Region	180 – 489	310	Rod
	Region	180 – 215	36	Coil 1A
	Region	216 – 234	19	Linker 1
	Region	235 – 326	92	Coil 1B
	Region	327 – 350	24	Linker 12
	Region	351 – 489	139	Coil 2
	Region	490 – 644	155	Tail
	Compositional bias	2 – 151	150	Gly/Phe/Ser-rich
	Compositional bias	502 – 641	140	Gly/Ser-rich
Sites
	Site	433	1	Stutter
Amino acid modifications
	Modified residue	21	1	Phosphoserine Ref.15 Ref.18
	Modified residue	66	1	Phosphoserine Ref.18
	Modified residue	82	1	Omega-N-methylarginine Ref.7
	Modified residue	276	1	N6,N6-dimethyllysine Ref.7
	Modified residue	295	1	Phosphotyrosine Ref.17
	Modified residue	297	1	Phosphothreonine Ref.17
Natural variations
	Natural variant	74	1	K → I in NEPPK. Ref.26		VAR_017819
	Natural variant	155	1	V → D in BCIE. Ref.24 Ref.33		VAR_017820
	Natural variant	155	1	V → G in BCIE. Ref.24 Ref.33		VAR_003853
	Natural variant	161	1	L → P in BCIE. Ref.20		VAR_003854
	Natural variant	176 – 197	22	Missing in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas. Ref.34		VAR_038627
	Natural variant	186	1	S → P in BCIE. Ref.25		VAR_003855
	Natural variant	188	1	N → K in BCIE. Ref.24 Ref.25 Ref.29 Ref.35		VAR_017821
	Natural variant	188	1	N → S in BCIE. Ref.24 Ref.25 Ref.29 Ref.35		VAR_003856
	Natural variant	188	1	N → T in BCIE; severe. Ref.24 Ref.25 Ref.29 Ref.35		VAR_017822
	Natural variant	193	1	S → P in BCIE. Ref.24		VAR_003857
	Natural variant	214	1	L → P in BCIE. Ref.31		VAR_017823
	Natural variant	312	1	I → V		VAR_003858
	Natural variant	330	1	I → T		VAR_003859
	Natural variant	340	1	D → V in BCIE. Ref.27		VAR_017824
	Natural variant	358	1	Y → N: dbSNP rs1050872.		VAR_003860
	Natural variant	454	1	A → S: dbSNP rs17678945.		VAR_038628
	Natural variant	459 – 466	8	Missing in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas. Ref.34		VAR_038629
	Natural variant	479	1	I → F in AEI. Ref.28 Ref.30		VAR_017825
	Natural variant	479	1	I → T in AEI and BCIE.		VAR_017826
	Natural variant	482	1	Y → C in BCIE. Ref.23		VAR_017827
	Natural variant	486	1	L → P in BCIE. Ref.35		VAR_017828
	Natural variant	490	1	E → Q in BCIE. Ref.22		VAR_003861
	Natural variant	537	1	G → C Ref.9		VAR_003862
	Natural variant	560 – 566	7	Missing in allele 1B. Ref.21		VAR_003864
	Natural variant	633	1	K → R: dbSNP rs14024.		VAR_003863
Experimental info
	Sequence conflict	201	1	L → M in AAA36153. Ref.9
	Sequence conflict	206	1	Q → K in AAA36153. Ref.9
	Sequence conflict	238	1	L → S in AAA36153. Ref.9
	Sequence conflict	344 – 345	2	SL → QF in AAA36153. Ref.9
	Sequence conflict	403	1	R → H in BAG36698. Ref.4
	Sequence conflict	404	1	V → M in AAA36153. Ref.9
	Sequence conflict	447	1	L → M in AAA36153. Ref.9
	Sequence conflict	463	1	R → C in AAA36153. Ref.9
	Sequence conflict	466	1	Q → H in AAA36153. Ref.9
	Sequence conflict	504	1	S → T in AAA36153. Ref.9
	Sequence conflict	511 – 512	2	TI → SM in AAA36153. Ref.9
	Sequence conflict	564	1	G → S in AAA36153. Ref.9
	Sequence conflict	613	1	I → S in AAA36153. Ref.9
	Sequence conflict	638	1	T → S in AAA36153. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P04264-1 [UniParc]. Last modified May 26, 2009. Version 6. Checksum: CE5DDE97388F5017	FASTA	644	66,039
	10 20 30 40 50 60 MSRQFSSRSG YRSGGGFSSG SAGIINYQRR TTSSSTRRSG GGGGRFSSCG GGGGSFGAGG 70 80 90 100 110 120 GFGSRSLVNL GGSKSISISV ARGGGRGSGF GGGYGGGGFG GGGFGGGGFG GGGIGGGGFG 130 140 150 160 170 180 GFGSGGGGFG GGGFGGGGYG GGYGPVCPPG GIQEVTINQS LLQPLNVEID PEIQKVKSRE 190 200 210 220 230 240 REQIKSLNNQ FASFIDKVRF LEQQNQVLQT KWELLQQVDT STRTHNLEPY FESFINNLRR 250 260 270 280 290 300 RVDQLKSDQS RLDSELKNMQ DMVEDYRNKY EDEINKRTNA ENEFVTIKKD VDGAYMTKVD 310 320 330 340 350 360 LQAKLDNLQQ EIDFLTALYQ AELSQMQTQI SETNVILSMD NNRSLDLDSI IAEVKAQYED 370 380 390 400 410 420 IAQKSKAEAE SLYQSKYEEL QITAGRHGDS VRNSKIEISE LNRVIQRLRS EIDNVKKQIS 430 440 450 460 470 480 NLQQSISDAE QRGENALKDA KNKLNDLEDA LQQAKEDLAR LLRDYQELMN TKLALDLEIA 490 500 510 520 530 540 TYRTLLEGEE SRMSGECAPN VSVSVSTSHT TISGGGSRGG GGGGYGSGGS SYGSGGGSYG 550 560 570 580 590 600 SGGGGGGGRG SYGSGGSSYG SGGGSYGSGG GGGGHGSYGS GSSSGGYRGG SGGGGGGSSG 610 620 630 640 GRGSGGGSSG GSIGGRGSSS GGVKSSGGSS SVKFVSTTYS GVTR

References

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[1]	"Structure of a gene for the human epidermal 67-kDa keratin." Johnson L.D., Idler W.W., Zhou X.-M., Roop D.R., Steinert P.M. Proc. Natl. Acad. Sci. U.S.A. 82:1896-1900(1985) [PubMed: 2580302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-358 AND ARG-633.
[2]	"Genomic organization and amplification of the human epidermal type II keratin genes K1 and K5." Whittock N.V., Eady R.A.J., McGrath J.A. Biochem. Biophys. Res. Commun. 274:149-152(2000) [PubMed: 10903910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-358 AND ARG-633.
[3]	"Novel splice site mutation in keratin 1 underlies mild epidermolytic palmoplantar keratoderma in three kindreds." Hatsell S.J., Eady R.A.J., Wennerstrand L., Dopping-Hepenstal P.J., Leigh I.M., Munro C., Kelsell D.P. J. Invest. Dermatol. 116:606-609(2001) [PubMed: 11286630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN NEPPK, VARIANT ARG-633.
[4]	"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]. Tissue: Tongue.
[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], VARIANT ARG-633. Tissue: Skin.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8. Tissue: Platelet.
[8]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 13-30; 66-82; 186-240; 258-276; 278-298; 344-355; 365-386; 396-403; 408-416; 418-432; 442-455 AND 461-588, METHYLATION AT ARG-82 AND LYS-276, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[9]	"Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits." Steinert P.M., Parry D.A.D., Idler W.W., Johnson L.D., Steven A.C., Roop D.R. J. Biol. Chem. 260:7142-7149(1985) [PubMed: 2581964] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 152-644, VARIANTS CYS-537 AND ARG-633.
[10]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 377-386, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[11]	"Preferential deimination of keratin K1 and filaggrin during the terminal differentiation of human epidermis." Senshu T., Kan S., Ogawa H., Manabe M., Asaga H. Biochem. Biophys. Res. Commun. 225:712-719(1996) [PubMed: 8780679] [Abstract] Cited for: CITRULLINATION.
[12]	"Evidence for novel functions of the keratin tail emerging from a mutation causing ichthyosis hystrix." Sprecher E., Ishida-Yamamoto A., Becker O.M., Marekov L.N., Miller C.J., Steinert P.M., Neldner K., Richard G. J. Invest. Dermatol. 116:511-519(2001) [PubMed: 11286616] [Abstract] Cited for: INVOLVEMENT IN IHCM.
[13]	"Sequential reorganization of cornified cell keratin filaments involving filaggrin-mediated compaction and keratin 1 deimination." Ishida-Yamamoto A., Senshu T., Eady R.A.J., Takahashi H., Shimizu H., Akiyama M., Iizuka H. J. Invest. Dermatol. 118:282-287(2002) [PubMed: 11841545] [Abstract] Cited for: CITRULLINATION.
[14]	"Frameshift mutation in the V2 domain of human keratin 1 results in striate palmoplantar keratoderma." Whittock N.V., Smith F.J., Wan H., Mallipeddi R., Griffiths W.A.D., Dopping-Hepenstal P.J., Ashton G.H.S., Eady R.A.J., McLean W.H.I., McGrath J.A. J. Invest. Dermatol. 118:838-844(2002) [PubMed: 11982762] [Abstract] Cited for: INVOLVEMENT IN SPPK3.
[15]	"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-21, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 cells." Chuang N.N., Huang C.C. Biochem. Soc. Trans. 35:1292-1294(2007) [PubMed: 17956333] [Abstract] Cited for: FUNCTION, INTERACTION WITH GNB2L1 AND ITGB1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[17]	"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 TYR-295 AND THR-297, MASS SPECTROMETRY. Tissue: Epithelium.
[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-21 AND SER-66, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"A leucine-->proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis." Chipev C.C., Korge B.P., Markova N., Bale S.J., Digiovanna J.J., Compton J.G., Steinert P.M. Cell 70:821-828(1992) [PubMed: 1381288] [Abstract] Cited for: VARIANT BCIE PRO-161.
[21]	"The two size alleles of human keratin 1 are due to a deletion in the glycine-rich carboxyl-terminal V2 subdomain." Korge B.P., Compton J.G., Steinert P.M., Mischke D. J. Invest. Dermatol. 99:697-702(1992) [PubMed: 1281859] [Abstract] Cited for: VARIANT ALLELE 1B 560-GLY--TYR-566 DEL.
[22]	"Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis." Rothnagel J.A., Dominey A.M., Dempsey L.D., Longley M.A., Greenhalgh D.A., Gagne T.A., Huber M., Frenk E., Hohl D., Roop D.R. Science 257:1128-1130(1992) [PubMed: 1380725] [Abstract] Cited for: VARIANT BCIE GLN-490.
[23]	"Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity." Syder A.J., Yu Q.-C., Paller A.S., Giudice G., Pearson R., Fuchs E. J. Clin. Invest. 93:1533-1542(1994) [PubMed: 7512983] [Abstract] Cited for: VARIANT BCIE CYS-482.
[24]	"Mutations in the H1 and 1A domains in the keratin 1 gene in epidermolytic hyperkeratosis." Yang J.-M., Chipev C.C., Digiovanna J.J., Bale S.J., Marekov L.N., Steinert P.M., Compton J.G. J. Invest. Dermatol. 102:17-23(1994) [PubMed: 7507151] [Abstract] Cited for: VARIANTS BCIE GLY-155; SER-188 AND PRO-193.
[25]	"Mutations in the rod 1A domain of keratins 1 and 10 in bullous congenital ichthyosiform erythroderma (BCIE)." McLean W.H.I., Eady R.A.J., Dopping-Hepenstal P.J.C., McMillan J.R., Leigh I.M., Navsaria H.A., Higgins C., Harper J.I., Paige D.G., Morley S.M. J. Invest. Dermatol. 102:24-30(1994) [PubMed: 7507152] [Abstract] Cited for: VARIANTS BCIE PRO-186 AND SER-188.
[26]	"A mutation in the V1 end domain of keratin 1 in non-epidermolytic palmar-plantar keratoderma." Kimonis V., DiGiovanna J.J., Yang J.-M., Doyle S.Z., Bale S.J., Compton J.G. J. Invest. Dermatol. 103:764-769(1994) [PubMed: 7528239] [Abstract] Cited for: VARIANT NEPPK ILE-74.
[27]	"An atypical form of bullous congenital ichthyosiform erythroderma is caused by a mutation in the L12 linker region of keratin 1." Kremer H., Lavrijsen A.P., McLean W.H.I., Lane E.B., Melchers D., Ruiter D.J., Mariman E.C., Steijlen P.M. J. Invest. Dermatol. 111:1224-1226(1998) [PubMed: 9856846] [Abstract] Cited for: VARIANT BCIE VAL-340.
[28]	"Cyclic ichthyosis with epidermolytic hyperkeratosis: a phenotype conferred by mutations in the 2B domain of keratin K1." Sybert V.P., Francis J.S., Corden L.D., Smith L.T., Weaver M., Stephens K., McLean W.H.I. Am. J. Hum. Genet. 64:732-738(1999) [PubMed: 10053007] [Abstract] Cited for: VARIANTS AEI PHE-479 AND THR-479.
[29]	"An asparagine to threonine substitution in the 1A domain of keratin 1: a novel mutation that causes epidermolytic hyperkeratosis." Arin M.J., Longley M.A., Kuster W., Huber M., Hohl D., Rothnagel J.A., Roop D.R. Exp. Dermatol. 8:124-127(1999) [PubMed: 10232403] [Abstract] Cited for: VARIANT BCIE THR-188.
[30]	"Epidermolytic hyperkeratosis with polycyclic psoriasiform plaques resulting from a mutation in the keratin 1 gene." Michael E.J., Schneiderman P., Grossman M.E., Christiano A.M. Exp. Dermatol. 8:501-503(1999) [PubMed: 10597140] [Abstract] Cited for: VARIANT AEI PHE-479.
[31]	"Epidermolytic hyperkeratosis in a Hispanic family resulting from a mutation in the keratin 1 gene." Cserhalmi-Friedman P.B., Squeo R., Gordon D., Garzon M., Schneiderman P., Grossman M.E., Christiano A.M. Clin. Exp. Dermatol. 25:241-243(2000) [PubMed: 10844506] [Abstract] Cited for: VARIANT BCIE PRO-214.
[32]	"Identification of a novel mutation in keratin 1 in a family with epidermolytic hyperkeratosis." Arin M.J., Longley M.A., Epstein E.H. Jr., Rothnagel J.A., Roop D.R. Exp. Dermatol. 9:16-19(2000) [PubMed: 10688370] [Abstract] Cited for: VARIANT BCIE THR-479.
[33]	"New mutations in keratin 1 that cause bullous congenital ichthyosiform erythroderma and keratin 2e that cause ichthyosis bullosa of Siemens." Whittock N.V., Ashton G.H.S., Griffiths W.A.D., Eady R.A.J., McGrath J.A. Br. J. Dermatol. 145:330-335(2001) [PubMed: 11531804] [Abstract] Cited for: VARIANT BCIE ASP-155.
[34]	"Two cases of primarily palmoplantar keratoderma associated with novel mutations in keratin 1." Terron-Kwiatkowski A., Paller A.S., Compton J., Atherton D.J., McLean W.H., Irvine A.D. J. Invest. Dermatol. 119:966-971(2002) [PubMed: 12406346] [Abstract] Cited for: VARIANTS PALMOPLANTAR KERATODERMA VAL-176--LYS-197 DEL AND ALA-459--466-GLN DEL.
[35]	"Two novel mutations in the keratin 1 gene in epidermolytic hyperkeratosis." Lee D.-Y., Ahn K.-S., Lee C.-H., Rho N.-K., Lee J.-H., Lee E.-S., Steinert P.M., Yang J.-M. J. Invest. Dermatol. 119:976-977(2002) [PubMed: 12406348] [Abstract] Cited for: VARIANTS BCIE LYS-188 AND PRO-486.
+	Additional computationally mapped references.

Web resources

Human Intermediate Filament Mutation Database

GeneReviews

Wikipedia

Keratin-1 entry

Cross-references

Sequence databases
EMBLGenBankDDBJ	M98776 Genomic DNA. Translation: AAB47721.1. AF237621 Genomic DNA. Translation: AAF60327.1. AF304164 Genomic DNA. Translation: AAG41947.1. AK313986 mRNA. Translation: BAG36698.1. AC055716 Genomic DNA. No translation available. BC063697 mRNA. Translation: AAH63697.1. M10938 mRNA. Translation: AAA36153.1.
IPI	IPI00220327.
PIR	KRHU2. A22940.
RefSeq	NP_006112.3.
UniGene	Hs.80828
3D structure databases
HSSP	HSSP built from PDB template 1GK7 based on UniProtKB P08670.
ModBase	Search...
Protein-protein interaction databases
IntAct	P04264. 12 interactions.
PTM databases
PhosphoSite	P04264.
2-D gel databases
SWISS-2DPAGE	P04264.
Aarhus/Ghent-2DPAGE	4606. NEPHGE.
REPRODUCTION-2DPAGE	P04264.
Proteomic databases
PRIDE	P04264.
Genome annotation databases
Ensembl	ENSG00000167768. Homo sapiens. [Contig view]
GeneID	3848.
KEGG	hsa:3848.
Organism-specific databases
GeneCards	GC12M051354.
HGNC	HGNC:6412. KRT1.
HPA	CAB002153. HPA017917.
MIM	113800. phenotype. 139350. gene. 146590. phenotype. 600962. phenotype. 607602. phenotype. 607654. phenotype.
Orphanet	312. Erythroderma, congenital ichthyosiform, bullous. 458. Ichthyosis hystrix. 79503. Ichthyosis hystrix, Curth-Macklin type. 313. Ichthyosis, lamellar. 50942. Keratosis palmoplantaris striata. 496. Thost-Unna palmoplantar keratoderma.
PharmGKB	PA30199.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P04264.
HOVERGEN	P04264.
Gene expression databases
ArrayExpress	P04264.
Bgee	P04264.
CleanEx	HS_KRT1.
GermOnline	ENSG00000167768. Homo sapiens.
Family and domain databases
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	15141.
SOURCE	Search...

Entry information

Entry name

K2C1_HUMAN

Accession

Primary (citable) accession number: P04264
Secondary accession number(s): B2RA01 , Q14720, Q6GSJ0, Q9H298

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	May 26, 2009
Last modified:	July 7, 2009
This is version 125 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)