P78385 (KRT83_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Keratin, type II cuticular Hb3

Alternative name(s):
Hair keratin K2.10
Keratin-83
Short name=K83
Type II hair keratin Hb3
Type-II keratin Kb23

Gene names

Name:	KRT83
Synonyms:	KRTHB3

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	493 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Heterotetramer of two type I and two type II keratins.
Tissue specificity	Synthesis begins in the cortex 10-15 cell layers above the apex of the dermal papilla and ends abruptly in the middle of the cortex. Ref.1
Involvement in disease	Monilethrix (MLTRX) [MIM:158000]: Autosomal dominant hair disorder characterized clinically by alopecia and follicular papules. Affected hairs have uniform elliptical nodes of normal thickness and intermittent constrictions, internodes at which the hair easily breaks. Usually only the scalp is involved, but in severe forms, the secondary sexual hair, eyebrows, eyelashes, and nails may also be affected. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5
Miscellaneous	There are two types of hair/microfibrillar keratin, I (acidic) and II (neutral to basic).
Sequence similarities	Belongs to the intermediate filament family.

Ontologies

Keywords
Cellular component	Intermediate filament Keratin
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Coiled coil
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	epidermis development Traceable author statement Ref.1. Source: ProtInc
Cellular_component	keratin filament Inferred from electronic annotation. Source: InterPro
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 493	493	Keratin, type II cuticular Hb3		PRO_0000063699
Regions
	Region	1 – 111	111	Head
	Region	112 – 418	307	Rod
	Region	112 – 146	35	Coil 1A
	Region	147 – 156	10	Linker 1
	Region	157 – 257	101	Coil 1B
	Region	258 – 274	17	Linker 12
	Region	275 – 418	144	Coil 2
	Region	419 – 493	75	Tail
Natural variations
	Natural variant	149	1	R → C. Ref.1 Ref.4 Corresponds to variant rs2857663 [ dbSNP | Ensembl ].		VAR_018119
	Natural variant	279	1	I → M. Ref.1 Ref.4 Corresponds to variant rs2852464 [ dbSNP | Ensembl ].		VAR_018120
	Natural variant	407	1	E → K in MLTRX. Ref.5		VAR_023052
	Natural variant	493	1	H → Y. Ref.1 Ref.3 Ref.4 Corresponds to variant rs2857671 [ dbSNP | Ensembl ].		VAR_018121
Experimental info
	Sequence conflict	67	1	S → D in CAA67578. Ref.1
	Sequence conflict	314	1	I → V in BAG37418. Ref.3
	Sequence conflict	473	1	C → R in BAG37418. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P78385 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 73BE2DA2C93F3EB6	FASTA	493	54,195
	10 20 30 40 50 60 MTCGFNSIGC GFRPGNFSCV SACGPRPSRC CITAAPYRGI SCYRGLTGGF GSHSVCGGFR 70 80 90 100 110 120 AGSCGRSFGY RSGGVCGPSP PCITTVSVNE SLLTPLNLEI DPNAQCVKQE EKEQIKSLNS 130 140 150 160 170 180 RFAAFIDKVR FLEQQNKLLE TKLQFYQNRE CCQSNLEPLF AGYIETLRRE AECVEADSGR 190 200 210 220 230 240 LASELNHVQE VLEGYKKKYE EEVALRATAE NEFVALKKDV DCAYLRKSDL EANVEALIQE 250 260 270 280 290 300 IDFLRRLYEE EIRILQSHIS DTSVVVKLDN SRDLNMDCIV AEIKAQYDDI ATRSRAEAES 310 320 330 340 350 360 WYRSKCEEMK ATVIRHGETL RRTKEEINEL NRMIQRLTAE VENAKCQNSK LEAAVAQSEQ 370 380 390 400 410 420 QGEAALSDAR CKLAELEGAL QKAKQDMACL IREYQEVMNS KLGLDIEIAT YRRLLEGEEQ 430 440 450 460 470 480 RLCEGVEAVN VCVSSSRGGV VCGDLCVSGS RPVTGSVCSA PCNGNLVVST GLCKPCGQLN 490 TTCGGGSCGQ GRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequences and differential expression of three novel human type-II hair keratins." Rogers M.A., Langbein L., Praetzel S., Krieg T., Winter H., Schweizer J. Differentiation 61:187-194(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS CYS-149; MET-279 AND TYR-493. Tissue: Scalp.
[2]	"Characterization of a 300 kbp region of human DNA containing the type II hair keratin." Rogers M.A., Winter H., Langbein L., Wolf C., Schweizer J. J. Invest. Dermatol. 114:464-472(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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], VARIANT TYR-493. Tissue: Cerebellum.
[4]	"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], VARIANTS CYS-149; MET-279 AND TYR-493.
[5]	"A missense mutation in the type II hair keratin hHb3 is associated with monilethrix." van Steensel M.A., Steijlen P.M., Bladergroen R.S., Vermeer M., van Geel M. J. Med. Genet. 42:E19-E19(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MLTRX LYS-407.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	X99141 mRNA. Translation: CAA67578.1. Y19208 Genomic DNA. Translation: CAB76828.1. AK314904 mRNA. Translation: BAG37418.1. BC069546 mRNA. Translation: AAH69546.1. BC128063 mRNA. Translation: AAI28064.1.
IPI	IPI00297795.
RefSeq	NP_002273.3. NM_002282.3.
UniGene	Hs.720768.
3D structure databases
ProteinModelPortal	P78385.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000293670.
PTM databases
PhosphoSite	P78385.
Polymorphism databases
DMDM	218511666.
Proteomic databases
PaxDb	P78385.
PeptideAtlas	P78385.
PRIDE	P78385.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000293670; ENSP00000293670; ENSG00000170523.
GeneID	3889.
KEGG	hsa:3889.
UCSC	uc001saf.2. human.
Organism-specific databases
CTD	3889.
GeneCards	GC12M052708.
H-InvDB	HIX0036826. HIX0037211.
HGNC	HGNC:6460. KRT83.
HPA	CAB004987.
MIM	158000. phenotype. 602765. gene.
neXtProt	NX_P78385.
Orphanet	573. Monilethrix.
PharmGKB	PA30249.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG149039.
HOGENOM	HOG000230976.
HOVERGEN	HBG013015.
InParanoid	P78385.
KO	K07605.
OMA	SCGQGRC.
OrthoDB	EOG4B2SX3.
PhylomeDB	P78385.
Gene expression databases
ArrayExpress	P78385.
Bgee	P78385.
Genevestigator	P78385.
GermOnline	ENSG00000170523. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR003054. Keratin_II. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit. PTHR23239:SF18. PTHR23239:SF18. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01276. TYPE2KERATIN.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	3889.
NextBio	15267.
SOURCE	Search...

Entry information

Entry name

KRT83_HUMAN

Accession

Primary (citable) accession number: P78385
Secondary accession number(s): A1A4S9 , B2RC21, Q6NT21, Q9NSB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 106 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.