Q8N1N4 (K2C78_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Keratin, type II cytoskeletal 78

Alternative name(s):
Cytokeratin-78
Short name=CK-78
Keratin-5b
Keratin-78
Short name=K78
Type-II keratin Kb40

Gene names

Name:	KRT78
Synonyms:	K5B, KB40

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	520 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Subunit structure	Heterotetramer of two type I and two type II keratins.
Tissue specificity	Expressed in tongue, but not in skin or in any other tissues or organs examined. Ref.6
Miscellaneous	There are two types of cytoskeletal and microfibrillar keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa, respectively).
Sequence similarities	Belongs to the intermediate filament family.
Sequence caution	The sequence DAA00377.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Intermediate filament Keratin
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	keratin filament Inferred from electronic annotation. Source: InterPro
Molecular function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8N1N4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8N1N4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-110: Missing.
     111-127: ETQEIRTLNNQFASFID → MEGHEASPAQVGQGDRG

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 520	520	Keratin, type II cytoskeletal 78		PRO_0000314891
Regions
	Region	1 – 110	110	Head
	Region	111 – 421	311	Rod
	Region	111 – 146	36	Coil 1A
	Region	147 – 165	19	Linker 1
	Region	166 – 258	93	Coil 1B
	Region	259 – 281	23	Linker 12
	Region	282 – 421	140	Coil 2
	Region	422 – 520	99	Tail
	Compositional bias	7 – 82	76	Gly-rich
	Compositional bias	430 – 507	78	Ser-rich
Sites
	Site	362	1	Stutter
Natural variations
	Alternative sequence	1 – 110	110	Missing in isoform 2.		VSP_030419
	Alternative sequence	111 – 127	17	ETQEI…ASFID → MEGHEASPAQVGQGDRG in isoform 2.		VSP_030420
	Natural variant	25	1	R → H. Corresponds to variant rs11170289 [ dbSNP | Ensembl ].		VAR_038109
	Natural variant	92	1	L → P. Ref.1 Corresponds to variant rs2013335 [ dbSNP | Ensembl ].		VAR_038110
	Natural variant	224	1	G → A. Corresponds to variant rs2682343 [ dbSNP | Ensembl ].		VAR_038111
	Natural variant	238	1	A → T. Corresponds to variant rs10876360 [ dbSNP | Ensembl ].		VAR_038112
Experimental info
	Sequence conflict	250	1	N → S in CAI46001. Ref.2
	Sequence conflict	259	1	T → A in BAC04782. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: 4502110AAA408E86	FASTA	520	56,866
	10 20 30 40 50 60 MSLSPCRAQR GFSARSACSA RSRGRSRGGF SSRGGFSSRS LNSFGGCLEG SRGSTWGSGG 70 80 90 100 110 120 RLGVRFGEWS GGPGLSLCPP GGIQEVTINQ NLLTPLKIEI DPQFQVVRTQ ETQEIRTLNN 130 140 150 160 170 180 QFASFIDKVR FLEQQNKVLE TKWHLLQQQG LSGSQQGLEP VFEACLDQLR KQLEQLQGER 190 200 210 220 230 240 GALDAELKAC RDQEEEYKSK YEEEAHRRAT LENDFVVLKK DVDGVFLSKM ELEGKLEALR 250 260 270 280 290 300 EYLYFLKHLN EEELGQLQTQ ASDTSVVLSM DNNRYLDFSS IITEVRARYE EIARSSKAEA 310 320 330 340 350 360 EALYQTKYQE LQVSAQLHGD RMQETKVQIS QLHQEIQRLQ SQTENLKKQN ASLQAAITDA 370 380 390 400 410 420 EQRGELALKD AQAKVDELEA ALRMAKQNLA RLLCEYQELT STKLSLDVEI ATYRRLLEGE 430 440 450 460 470 480 ECRMSGECTS QVTISSVGGS AVMSGGVGGG LGSTCGLGSG KGSPGSCCTS IVTGGSNIIL 490 500 510 520 GSGKDPVLDS CSVSGSSAGS SCHTILKKTV ESSLKTSITY
	Isoform 2 [UniParc]. Checksum: AF958D13D971A4A8	FASTA	410	45,017
	10 20 30 40 50 60 MEGHEASPAQ VGQGDRGKVR FLEQQNKVLE TKWHLLQQQG LSGSQQGLEP VFEACLDQLR 70 80 90 100 110 120 KQLEQLQGER GALDAELKAC RDQEEEYKSK YEEEAHRRAT LENDFVVLKK DVDGVFLSKM 130 140 150 160 170 180 ELEGKLEALR EYLYFLKHLN EEELGQLQTQ ASDTSVVLSM DNNRYLDFSS IITEVRARYE 190 200 210 220 230 240 EIARSSKAEA EALYQTKYQE LQVSAQLHGD RMQETKVQIS QLHQEIQRLQ SQTENLKKQN 250 260 270 280 290 300 ASLQAAITDA EQRGELALKD AQAKVDELEA ALRMAKQNLA RLLCEYQELT STKLSLDVEI 310 320 330 340 350 360 ATYRRLLEGE ECRMSGECTS QVTISSVGGS AVMSGGVGGG LGSTCGLGSG KGSPGSCCTS 370 380 390 400 410 IVTGGSNIIL GSGKDPVLDS CSVSGSSAGS SCHTILKKTV ESSLKTSITY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORM 1), VARIANT PRO-92. Tissue: Oesophagus and Tongue.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Oesophageal carcinoma.
[3]	"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].
[4]	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].
[5]	"Genes for intermediate filament proteins and the draft sequence of the human genome: novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18." Hesse M., Magin T.M., Weber K. J. Cell Sci. 114:2569-2575(2001) [PubMed: 11683385] [Abstract] Cited for: IDENTIFICATION.
[6]	"Characterization of new members of the human type II keratin gene family and a general evaluation of the keratin gene domain on chromosome 12q13.13." Rogers M.A., Edler L., Winter H., Langbein L., Beckmann I., Schweizer J. J. Invest. Dermatol. 124:536-544(2005) [PubMed: 15737194] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK096419 mRNA. Translation: BAC04782.1. AK290901 mRNA. Translation: BAF83590.1. BX647095 mRNA. Translation: CAI46001.1. AC107016 Genomic DNA. No translation available. BK000646 Genomic DNA. Translation: DAA00377.1. Sequence problems. CH471054 Genomic DNA. Translation: EAW96650.1.
IPI	IPI00166205. IPI00477227.
RefSeq	NP_775487.2. NM_173352.2.
UniGene	Hs.665267.
3D structure databases
HSSP	HSSP built from PDB template 1GK7 based on UniProtKB P08670.
ProteinModelPortal	Q8N1N4.
SMR	Q8N1N4. Positions 109-146, 154-260, 277-422.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8N1N4. 3 interactions.
STRING	Q8N1N4.
Polymorphism databases
DMDM	166218809.
Proteomic databases
PRIDE	Q8N1N4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000304620; ENSP00000306261; ENSG00000170423.
GeneID	196374.
KEGG	hsa:196374.
UCSC	uc001sbc.1. human.
Organism-specific databases
CTD	196374.
GeneCards	GC12M053232.
H-InvDB	HIX0010660.
HGNC	HGNC:28926. KRT78.
HPA	HPA039724.
MIM	611159. gene.
neXtProt	NX_Q8N1N4.
PharmGKB	PA147357807.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08573.
GeneTree	ENSGT00550000074491.
HOGENOM	HBG715391.
HOVERGEN	HBG013015.
OMA	CRDQEEE.
OrthoDB	EOG4M65HV.
PhylomeDB	Q8N1N4.
Gene expression databases
ArrayExpress	Q8N1N4.
Bgee	Q8N1N4.
CleanEx	HS_KRT78.
Genevestigator	Q8N1N4.
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
NextBio	89444.
SOURCE	Search...

Entry information

Entry name

K2C78_HUMAN

Accession

Primary (citable) accession number: Q8N1N4
Secondary accession number(s): A8K4D6, Q5HYM7, Q7RTT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	January 25, 2012
This is version 79 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.