Q04695 (K1C17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Keratin, type I cytoskeletal 17

Alternative name(s):
39.1
Cytokeratin-17
Short name=CK-17
Keratin-17
Short name=K17

Gene names

Name:

KRT17

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair. May be a marker of basal cell differentiation in complex epithelia and therefore indicative of a certain type of epithelial "stem cells". May act as an autoantigen in the immunopathogenesis of psoriasis, with certain peptide regions being a major target for autoreactive T-cells and hence causing their proliferation. Required for the correct growth of hair follicles, in particular for the persistence of the anagen (growth) state. Modulates the function of TNF-alpha in the specific context of hair cycling. Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway. Involved in tissue repair By similarity. Ref.10 Ref.11 Ref.14
Subunit structure	Heterodimer of a type I and a type II keratin. KRT17 associates with KRT6 isomers. Interacts with TRADD and SFN By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in the outer root sheath and medulla region of hair follicle specifically from eyebrow and beard, digital pulp, nail matrix and nail bed epithelium, mucosal stratified squamous epithelia and in basal cells of oral epithelium, palmoplantar epidermis and sweat and mammary glands. Also expressed in myoepithelium of prostate, basal layer of urinary bladder, cambial cells of sebaceous gland and in exocervix (at protein level). Ref.1 Ref.8 Ref.9 Ref.10
Induction	Induced in damaged or stressed epidermis. Induced by the cytokines interferon-gamma (IFN-gamma), tumor necrosis factor alpha (TNF-alpha) and transforming growth factor-alpha (TGF-alpha), and by the potent NF-kappa B inhibitor compounds Bay 11-7082 and Bay 11-7085. Down-regulated by the drug Imatinib. Ref.2 Ref.11 Ref.12 Ref.14
Involvement in disease	Pachyonychia congenita 2 (PC2) [MIM:167210]: An autosomal dominant ectodermal dysplasia characterized by hypertrophic nail dystrophy resulting in onchyogryposis (thickening and increase in curvature of the nail), palmoplantar keratoderma and hyperhidrosis, follicular hyperkeratosis, multiple epidermal cysts, absent/sparse eyebrow and body hair, and by the presence of natal teeth. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.6 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Steatocystoma multiplex (SM) [MIM:184500]: Disease characterized by round or oval cystic tumors widely distributed on the back, anterior trunk, arms, scrotum, and thighs. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.20 Ref.27 KRT16 and KRT17 are coexpressed only in pathological situations such as metaplasias and carcinomas of the uterine cervix and in psoriasis vulgaris.
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.
Sequence caution	The sequence AAH72018.1 differs from that shown. Reason: Frameshift at position 109.

Ontologies

Keywords
Cellular component	Cytoplasm Intermediate filament Keratin
Disease	Disease mutation Ectodermal dysplasia Palmoplantar keratoderma
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	epidermis development Traceable author statement Ref.6. Source: ProtInc intermediate filament organization Inferred from electronic annotation. Source: Compara keratinization Inferred from electronic annotation. Source: Compara morphogenesis of an epithelium Inferred from electronic annotation. Source: Compara positive regulation of cell growth Inferred from electronic annotation. Source: Compara positive regulation of hair follicle development Inferred from electronic annotation. Source: Compara positive regulation of translation Inferred from electronic annotation. Source: Compara
Cellular_component	cell periphery Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell intermediate filament Traceable author statement Ref.1. Source: ProtInc
Molecular_function	MHC class II receptor activity Inferred from direct assay Ref.11. Source: UniProtKB structural constituent of cytoskeleton Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCDC85B	Q15834	2	EBI-297873,EBI-739674

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 432	432	Keratin, type I cytoskeletal 17		PRO_0000063664
Regions
	Region	1 – 83	83	Head
	Region	84 – 392	309	Rod
	Region	84 – 120	37	Coil 1A
	Region	102 – 116	15	Peptide epitope S1; induces T-cell and keratinocyte proliferation and IFN-gamma production
	Region	121 – 138	18	Linker 1
	Region	139 – 230	92	Coil 1B
	Region	153 – 167	15	Peptide epitope S2; induces T-cell proliferation and IFN-gamma production
	Region	231 – 250	20	Linker 12
	Region	251 – 392	142	Coil 2
	Region	332 – 346	15	Peptide epitope S4; induces T-cell and keratinocyte proliferation and IFN-gamma production
	Region	393 – 432	40	Tail
Amino acid modifications
	Modified residue	13	1	Phosphoserine Ref.16
	Modified residue	32	1	Phosphoserine Ref.15 Ref.16 Ref.17
	Modified residue	39	1	Phosphoserine Ref.16
	Modified residue	319	1	Phosphoserine By similarity
Natural variations
	Natural variant	88	1	M → T in PC2 and SM. Ref.21 Ref.27		VAR_010512
	Natural variant	92	1	N → D in PC2. Ref.6		VAR_003847
	Natural variant	92	1	N → H in SM. Ref.19		VAR_003848
	Natural variant	92	1	N → S in PC2. Ref.19 Ref.20		VAR_003849
	Natural variant	94 – 98	5	Missing in PC2.		VAR_017069
	Natural variant	94	1	R → C in PC2 and SM. Ref.20		VAR_010513
	Natural variant	94	1	R → H in SM. Ref.19		VAR_003850
	Natural variant	94	1	R → P in PC2. Ref.22		VAR_017068
	Natural variant	95	1	L → P in PC2. Ref.23		VAR_017071
	Natural variant	95	1	L → Q in PC2. Ref.22		VAR_017070
	Natural variant	97	1	Missing in PC2. Ref.23		VAR_017072
	Natural variant	98	1	Y → D in PC2. Ref.19		VAR_003851
	Natural variant	99	1	L → P in PC2. Ref.23		VAR_017073
	Natural variant	102	1	V → M in PC2. Ref.24 Ref.26		VAR_017074
	Natural variant	109	1	N → D in PC2. Ref.4 Ref.25		VAR_037083
Experimental info
	Mutagenesis	103	1	R → A: Down-regulates both proliferation of psoriatic T-cells and IFN-gamma production; suppresses keratinocyte growth when part of the altered peptide epitope S1. Ref.14
	Mutagenesis	106	1	E → A: Down-regulates proliferation of psoriatic T-cells and IFN-gamma production when part of the altered peptide epitope S1. Ref.14
	Mutagenesis	109	1	N → A: No significant effect on T-cell proliferation or IFN-gamma production when part of the altered peptide epitope S1. Ref.14
	Mutagenesis	154	1	N → A: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S2. Ref.14
	Mutagenesis	155	1	I → A: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S2. Ref.14
	Mutagenesis	157	1	L → A: Down-regulates proliferation of psoriatic T-cells and IFN-gamma production when part of the altered peptide epitope S2. Ref.14
	Mutagenesis	160	1	D → A: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S4. Ref.14
	Mutagenesis	333	1	N → A: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S4. Ref.14
	Mutagenesis	334	1	R → A: No significant effect on T-cell proliferation but can induce IFN-gamma production when part of the altered peptide epitope S2. Ref.14
	Mutagenesis	336	1	C → A: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S2. Ref.14
	Mutagenesis	339	1	L → A: Down-regulates both proliferation of psoriatic T-cells and IFN-gamma production; suppresses keratinocyte growth when part of the altered peptide epitope S4. Ref.14
	Sequence conflict	30	1	R → Q in AL353997. Ref.4
	Sequence conflict	30	1	R → Q in AC022596. Ref.4
	Sequence conflict	42	1	L → P in AL353997. Ref.4
	Sequence conflict	42	1	L → P in AC022596. Ref.4
	Sequence conflict	51 – 56	6	Missing in BAC04534. Ref.3
	Sequence conflict	51	1	T → A in AL353997. Ref.4
	Sequence conflict	51	1	T → A in AC022596. Ref.4
	Sequence conflict	72	1	S → SS in AL353997. Ref.4
	Sequence conflict	73 – 74	2	FG → SFE in AC022596. Ref.4
	Sequence conflict	74	1	G → E in AL353997. Ref.4
	Sequence conflict	81	1	A → V in AL353997. Ref.4
	Sequence conflict	81	1	A → V in AC022596. Ref.4
	Sequence conflict	94 – 108	15	Missing in AAH72018. Ref.5
	Sequence conflict	137	1	T → I in AL353997. Ref.4
	Sequence conflict	137	1	T → I in AC022596. Ref.4
	Sequence conflict	145 – 147	3	ILT → VGPA in AL353997. Ref.4
	Sequence conflict	158	1	Q → H in AC022596. Ref.4
	Sequence conflict	159	1	I → N in AL353997. Ref.4
	Sequence conflict	163	1	R → H in AL353997. Ref.4
	Sequence conflict	163	1	R → H in AC022596. Ref.4
	Sequence conflict	167	1	D → A in AL353997. Ref.4
	Sequence conflict	167	1	D → A in AC022596. Ref.4
	Sequence conflict	180	1	R → C in AL353997. Ref.4
	Sequence conflict	180	1	R → C in AC022596. Ref.4
	Sequence conflict	190 – 191	2	LR → PC in AL353997. Ref.4
	Sequence conflict	190 – 191	2	LR → PC in AC022596. Ref.4
	Sequence conflict	204	1	L → P in AL353997. Ref.4
	Sequence conflict	207	1	Q → H in AL353997. Ref.4
	Sequence conflict	207	1	Q → H in AC022596. Ref.4
	Sequence conflict	225	1	Missing in AL353997. Ref.4
	Sequence conflict	225	1	Missing in AC022596. Ref.4
	Sequence conflict	229	1	L → P in AL353997. Ref.4
	Sequence conflict	229	1	L → P in AC022596. Ref.4
	Sequence conflict	242	1	D → G in AL353997. Ref.4
	Sequence conflict	242	1	D → G in AC022596. Ref.4
	Sequence conflict	258	1	D → E in AL353997. Ref.4
	Sequence conflict	258	1	D → E in AC022596. Ref.4
	Sequence conflict	305	1	R → C in AL353997. Ref.4
	Sequence conflict	305	1	R → C in AC022596. Ref.4
	Sequence conflict	337	1	V → M in AL353997. Ref.4
	Sequence conflict	337	1	V → M in AC022596. Ref.4
	Sequence conflict	352	1	Q → R in AL353997. Ref.4
	Sequence conflict	352	1	Q → R in AC022596. Ref.4
	Sequence conflict	357	1	R → L in AL353997. Ref.4
	Sequence conflict	357	1	R → L in AC022596. Ref.4
	Sequence conflict	373 – 375	3	VKT → MKM in AL353997. Ref.4
	Sequence conflict	373 – 375	3	VKT → MKM in AC022596. Ref.4
	Sequence conflict	379	1	Q → L in AL353997. Ref.4
	Sequence conflict	379	1	Q → L in AC022596. Ref.4
	Sequence conflict	382	1	A → T in AL353997. Ref.4
	Sequence conflict	382	1	A → T in AC022596. Ref.4
	Sequence conflict	385	1	R → H in AL353997. Ref.4
	Sequence conflict	385	1	R → H in AC022596. Ref.4
	Sequence conflict	395 – 404	10	LTQYKKEPVT → FRMSESSPVS in AC022596. Ref.4
	Sequence conflict	406	1	R → C in AL353997. Ref.4
	Sequence conflict	409	1	R → P in AL353997. Ref.4
	Sequence conflict	428	1	H → R in AL353997. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q04695 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 35B429243F47EB5C	FASTA	432	48,106
	10 20 30 40 50 60 MTTSIRQFTS SSSIKGSSGL GGGSSRTSCR LSGGLGAGSC RLGSAGGLGS TLGGSSYSSC 70 80 90 100 110 120 YSFGSGGGYG SSFGGVDGLL AGGEKATMQN LNDRLASYLD KVRALEEANT ELEVKIRDWY 130 140 150 160 170 180 QRQAPGPARD YSQYYRTIEE LQNKILTATV DNANILLQID NARLAADDFR TKFETEQALR 190 200 210 220 230 240 LSVEADINGL RRVLDELTLA RADLEMQIEN LKEELAYLKK NHEEEMNALR GQVGGEINVE 250 260 270 280 290 300 MDAAPGVDLS RILNEMRDQY EKMAEKNRKD AEDWFFSKTE ELNREVATNS ELVQSGKSEI 310 320 330 340 350 360 SELRRTMQAL EIELQSQLSM KASLEGNLAE TENRYCVQLS QIQGLIGSVE EQLAQLRCEM 370 380 390 400 410 420 EQQNQEYKIL LDVKTRLEQE IATYRRLLEG EDAHLTQYKK EPVTTRQVRT IVEEVQDGKV 430 ISSREQVHQT TR

References

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[1]	"Characterization of the human gene encoding cytokeratin 17 and its expression pattern." Troyanovsky S.M., Leube R.E., Franke W.W. Eur. J. Cell Biol. 59:127-137(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[2]	"Interferon-gamma regulates expression of a novel keratin class I gene." Flohr T., Buwitt U., Bonnekoh B., Decker T., Boettger E.C. Eur. J. Immunol. 22:975-979(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[4]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PC2 ASP-109.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Cervix and Muscle.
[6]	"Keratin 16 and keratin 17 mutations cause pachyonychia congenita." McLean W.H.I., Rugg E.L., Lunny D.P., Morley S.M., Lane E.B., Swensson O., Dopping-Hepenstal P.J.C., Griffiths W.A.D., Eady R.A.J., Higgins C., Navsaria H.A., Leigh I.M., Strachan T., Kunkeler L., Munro C.S. Nat. Genet. 9:273-278(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-101, VARIANT PC2 ASP-92.
[7]	Shen Z., Chen L., Wang G., Liu Y.-F. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-117; 152-168; 306-322 AND 331-347.
[8]	"Patterns of expression of keratin 17 in human epithelia: dependency on cell position." Troyanovsky S.M., Guelstein V.I., Tchipysheva T.A., Krutovskikh V.A., Bannikov G.A. J. Cell Sci. 93:419-426(1989) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Keratin expression in the normal nail unit: markers of regional differentiation." De Berker D., Wojnarowska F., Sviland L., Westgate G.E., Dawber R.P., Leigh I.M. Br. J. Dermatol. 142:89-96(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"Keratin 17 expression in the hard epithelial context of the hair and nail, and its relevance for the pachyonychia congenita phenotype." McGowan K.M., Coulombe P.A. J. Invest. Dermatol. 114:1101-1107(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[11]	"HLA DR B1*04, *07-restricted epitopes on Keratin 17 for autoreactive T cells in psoriasis." Shen Z., Wang G., Fan J.-Y., Li W., Liu Y.-F. J. Dermatol. Sci. 38:25-39(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[12]	"Interferon-gamma-dependent in vitro model for the putative keratin 17 autoimmune loop in psoriasis: exploration of pharmaco- and gene-therapeutic effects." Bockelmann R., Horn T., Gollnick H., Bonnekoh B. Skin Pharmacol. Physiol. 18:42-54(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[13]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"Altered keratin 17 peptide ligands inhibit in vitro proliferation of keratinocytes and T cells isolated from patients with psoriasis." Shen Z., Chen L., Liu Y.-F., Gao T.-W., Wang G., Fan X.-L., Fan J.-Y., Fan P.-S., Li C.-Y., Liu B., Dang Y.-P., Li C.-X. J. Am. Acad. Dermatol. 54:992-1002(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION, MUTAGENESIS OF ARG-103; GLU-106; ASN-109; ASN-154; ILE-155; LEU-157; ASP-160; ASN-333; ARG-334; CYS-336 AND LEU-339.
[15]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-32 AND SER-39, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Missense mutations in keratin 17 cause either pachyonychia congenita type 2 or a phenotype resembling steatocystoma multiplex." Smith F.J.D., Corden L.D., Rugg E.L., Ratnavel R., Leigh I.M., Moss C., Tidman M.J., Hohl D., Huber M., Kunkeler L., Munro C.S., Lane E.B., McLean W.H.I. J. Invest. Dermatol. 108:220-223(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PC2 SER-92 AND ASP-98, VARIANTS SM HIS-92 AND HIS-94.
[20]	"Keratin 17 mutations cause either steatocystoma multiplex or pachyonychia congenita type 2." Covello S.P., Smith F.J.D., Sillevis Smitt J.H., Paller A.S., Munro C.S., Jonkman M.F., Uitto J., McLean W.H.I. Br. J. Dermatol. 139:475-480(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PC2 SER-92 AND CYS-94, VARIANT SM CYS-94.
[21]	"Mutation report: identification of a germline mutation in keratin 17 in a family with pachyonychia congenita type 2." Celebi J.T., Tanzi E.L., Yao Y.J., Michael E.J., Peacocke M. J. Invest. Dermatol. 113:848-850(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PC2 THR-88.
[22]	"Novel keratin 17 mutations in pachyonychia congenita type 2." Smith F.J.D., Coleman C.M., Bayoumy N.M., Tenconi R., Nelson J., David A., McLean W.H.I. J. Invest. Dermatol. 116:806-808(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PC2 94-PRO--TYR-98 DEL; PRO-94 AND GLN-95.
[23]	"Novel and recurrent mutations in the genes encoding keratins K6a, K16 and K17 in 13 cases of pachyonychia congenita." Terrinoni A., Smith F.J.D., Didona B., Canzona F., Paradisi M., Huber M., Hohl D., David A., Verloes A., Leigh I.M., Munro C.S., Melino G., McLean W.H.I. J. Invest. Dermatol. 117:1391-1396(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PC2 PRO-95; SER-97 DEL AND PRO-99.
[24]	"A novel point mutation in the keratin 17 gene in a Japanese case of pachyonychia congenita type 2." Hashiguchi T., Yotsumoto S., Shimada H., Terasaki K., Setoyama M., Kobayashi K., Saheki T., Kanzaki T. J. Invest. Dermatol. 118:545-547(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PC2 MET-102.
[25]	"A novel mutation in the second half of the keratin 17 1A domain in a large pedigree with delayed-onset pachyonychia congenita type 2." Xiao S.-X., Feng Y.-G., Ren X.-R., Tan S.-S., Li L., Wang J.-M., Shi Y.-Z. J. Invest. Dermatol. 122:892-895(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PC2 ASP-109.
[26]	"Identification of a recurrent mutation in keratin 17 in a Japanese family with pachyonychia congenita type 2." Uchida T., Inaoki M., Makino E., Fujimoto W. J. Dermatol. Sci. 38:60-63(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PC2 MET-102.
[27]	"Keratin 17 mutation in pachyonychia congenita type 2 patient with early onset steatocystoma multiplex and Hutchinson-like tooth deformity." Oh S.-W., Kim M.Y., Lee J.S., Kim S.-C. J. Dermatol. 33:161-164(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PC2 THR-88, VARIANT SM THR-88.
+	Additional computationally mapped references.

Web resources

Human Intermediate Filament Mutation Database

GeneReviews

Wikipedia

Keratin-17 entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z19574 Genomic DNA. Translation: CAA79626.1. X62571 mRNA. Translation: CAA44451.1. AK095342 mRNA. Translation: BAC04534.1. AC022596 Genomic DNA. No translation available. AL353997 Genomic DNA. No translation available. BC000159 mRNA. Translation: AAH00159.2. BC011901 mRNA. Translation: AAH11901.1. BC056421 mRNA. Translation: AAH56421.1. BC072018 mRNA. Translation: AAH72018.1. Frameshift. BC072019 mRNA. Translation: AAH72019.1. S78515 Genomic DNA. Translation: AAB34565.1. EF608068 mRNA. Translation: ABQ96595.1. EF608069 mRNA. Translation: ABQ96596.1. EF608070 mRNA. Translation: ABQ96597.1. EF608071 mRNA. Translation: ABQ96598.1.
IPI	IPI00450768.
PIR	S30433.
RefSeq	NP_000413.1. NM_000422.2.
UniGene	Hs.2785.
3D structure databases
ProteinModelPortal	Q04695.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q04695. 9 interactions.
MINT	MINT-256746.
PTM databases
PhosphoSite	Q04695.
Polymorphism databases
DMDM	547751.
2D gel databases
SWISS-2DPAGE	Q04695.
Proteomic databases
PaxDb	Q04695.
PRIDE	Q04695.
Protocols and materials databases
DNASU	3872.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000311208; ENSP00000308452; ENSG00000128422.
GeneID	3872.
KEGG	hsa:3872.
UCSC	uc002hxh.2. human.
Organism-specific databases
CTD	3872.
GeneCards	GC17M039775.
H-InvDB	HIX0059686.
HGNC	HGNC:6427. KRT17.
HPA	CAB000029. HPA000452. HPA000453.
MIM	148069. gene. 167210. phenotype. 184500. phenotype.
neXtProt	NX_Q04695.
Orphanet	2309. Pachyonychia congenita. 841. Sebocystomatosis.
PharmGKB	PA30214.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG148784.
HOVERGEN	HBG013015.
InParanoid	Q04695.
KO	K07604.
OMA	YYHTIED.
OrthoDB	EOG483D4W.
PhylomeDB	Q04695.
Gene expression databases
ArrayExpress	Q04695.
Bgee	Q04695.
Genevestigator	Q04695.
GermOnline	ENSG00000186831. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR002957. Keratin_I. IPR009053. Prefoldin. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01248. TYPE1KERATIN.
SUPFAM	SSF46579. Prefoldin. 1 hit.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	3872.
NextBio	15209.
PMAP-CutDB	Q04695.
SOURCE	Search...

Entry information

Entry name

K1C17_HUMAN

Accession

Primary (citable) accession number: Q04695
Secondary accession number(s): A5Z1M9 , A5Z1N0, A5Z1N1, A5Z1N2, A6NDV6, A6NKQ2, Q6IP98, Q8N1P6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 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.