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Q7RTS7

- K2C74_HUMAN

UniProt

Q7RTS7 - K2C74_HUMAN

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Protein

Keratin, type II cytoskeletal 74

Gene

KRT74

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Has a role in hair formation. Specific component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle (Probable).Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei391 – 3911Stutter

GO - Molecular functioni

  1. keratin filament binding Source: UniProt
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. intermediate filament cytoskeleton organization Source: UniProt
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cytoskeletal 74
Alternative name(s):
Cytokeratin-74
Short name:
CK-74
Keratin-5c
Short name:
K5C
Keratin-74
Short name:
K74
Type II inner root sheath-specific keratin-K6irs4
Type-II keratin Kb37
Gene namesi
Name:KRT74
Synonyms:K6IRS4, KB37, KRT5C, KRT6IRS4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:28929. KRT74.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProt
  2. extracellular vesicular exosome Source: UniProtKB
  3. keratin filament Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

Pathology & Biotechi

Involvement in diseasei

Woolly hair autosomal dominant (ADWH) [MIM:194300]: A hair shaft disorder characterized by fine and tightly curled hair. Compared to normal curly hair that is observed in some populations, woolly hair grows slowly and stops growing after a few inches. Under light microscopy, woolly hair shows some structural anomalies, including trichorrhexis nodosa and tapered ends.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti148 – 1481N → K in ADWH; results in disruption of keratin intermediate filament formation in cultured cells. 1 Publication
VAR_063587
Hypotrichosis 3 (HYPT3) [MIM:613981]: A condition characterized by the presence of less than the normal amount of hair. Affected individuals have normal hair in early childhood but experience progressive hair loss limited to the scalp beginning in the middle of the first decade and almost complete baldness by the third decade. Body hair, beard, eyebrows, axillary hair, teeth, and nails develop normally.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti482 – 4821D → N in HYPT3. 1 Publication
VAR_065951
Ectodermal dysplasia 7, hair/nail type (ECTD7) [MIM:614929]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures such as hair, teeth, nails and sweat glands, with or without any additional clinical sign. Each combination of clinical features represents a different type of ectodermal dysplasia. Ectodermal dysplasia of the hair/nail type is characterized by hypotrichosis and nail dystrophy without non-ectodermal or other ectodermal manifestations.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti274 – 2741F → S in ECTD7; autosomal recessive. 1 Publication
VAR_071383

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia, Hypotrichosis

Organism-specific databases

MIMi194300. phenotype.
613981. phenotype.
614929. phenotype.
Orphaneti90368. Hypotrichosis simplex of the scalp.
69084. Pure hair and nail ectodermal dysplasia.
170. Woolly hair.
PharmGKBiPA147357741.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Keratin, type II cytoskeletal 74PRO_0000314885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei513 – 5131Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ7RTS7.
PaxDbiQ7RTS7.
PRIDEiQ7RTS7.

PTM databases

PhosphoSiteiQ7RTS7.

Expressioni

Tissue specificityi

Highly expressed in hair follicles from scalp. In hair, it is specifically present in the inner root sheath (IRS) of the hair follicle. Present in the IRS Huxley layer, but not in Henle layer or cuticle of the IRS. In the IRS Huxley layer, it is expressed in specialized Huxley cells, termed 'Fluegelzellen, along the area of differentiated Henle cells (at protein level).3 Publications

Gene expression databases

BgeeiQ7RTS7.
CleanExiHS_KRT74.
ExpressionAtlasiQ7RTS7. baseline and differential.
GenevestigatoriQ7RTS7.

Organism-specific databases

HPAiHPA048596.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins.

Protein-protein interaction databases

BioGridi125727. 3 interactions.
STRINGi9606.ENSP00000307240.

Structurei

3D structure databases

ProteinModelPortaliQ7RTS7.
SMRiQ7RTS7. Positions 137-287, 306-448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 139139HeadAdd
BLAST
Regioni140 – 449310RodAdd
BLAST
Regioni140 – 17536Coil 1AAdd
BLAST
Regioni176 – 19419Linker 1Add
BLAST
Regioni195 – 28692Coil 1BAdd
BLAST
Regioni287 – 31024Linker 12Add
BLAST
Regioni311 – 449139Coil 2Add
BLAST
Regioni450 – 52980TailAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 111102Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG266742.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiQ7RTS7.
KOiK07605.
PhylomeDBiQ7RTS7.
TreeFamiTF317854.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7RTS7 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRQLNIKSS GDKGNFSVHS AVVPRKAVGS LASYCAAGRG AGAGFGSRSL
60 70 80 90 100
YSLGGNRRIS FNVAGGGVRA GGYGFRPGSG YGGGRASGFA GSMFGSVALG
110 120 130 140 150
PACLSVCPPG GIHQVTVNKS LLAPLNVELD PEIQKVRAQE REQIKVLNDK
160 170 180 190 200
FASFIDKVRF LEQQNQVLET KWELLQQLDL NNCKKNLEPI LEGYISNLRK
210 220 230 240 250
QLETLSGDRV RLDSELRSMR DLVEDYKKRY EVEINRRTTA ENEFVVLKKD
260 270 280 290 300
ADAAYAVKVE LQAKVDSLDK EIKFLKCLYD AEIAQIQTHA SETSVILSMD
310 320 330 340 350
NNRDLDLDSI IAEVRMHYEE IALKSKAEAE ALYQTKIQEL QLAASRHGDD
360 370 380 390 400
LKHTRSEMVE LNRLIQRIRC EIGNVKKQRA SLETAIADAE QRGDNALKDA
410 420 430 440 450
QAKLDELEGA LHQAKEELAR MLREYQELMS LKLALDMEIA TYRKLLEGEE
460 470 480 490 500
CRMSGENPSS VSISVISSSS YSYHHPSSAG VDLGASAVAG SSGSTQSGQT
510 520
KTTEARGGDL KDTQGKSTPA SIPARKATR
Length:529
Mass (Da):57,865
Last modified:January 15, 2008 - v2
Checksum:iCE81527DD4825CBF
GO

Sequence cautioni

The sequence DAA00404.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti148 – 1481N → K in ADWH; results in disruption of keratin intermediate filament formation in cultured cells. 1 Publication
VAR_063587
Natural varianti165 – 1651N → K.
Corresponds to variant rs11170177 [ dbSNP | Ensembl ].
VAR_038096
Natural varianti178 – 1781L → Q.
Corresponds to variant rs11170176 [ dbSNP | Ensembl ].
VAR_049806
Natural varianti271 – 2711E → D.2 Publications
Corresponds to variant rs670741 [ dbSNP | Ensembl ].
VAR_038097
Natural varianti274 – 2741F → S in ECTD7; autosomal recessive. 1 Publication
VAR_071383
Natural varianti392 – 3921R → Q.
Corresponds to variant rs57387512 [ dbSNP | Ensembl ].
VAR_061299
Natural varianti424 – 4241E → K.
Corresponds to variant rs57711382 [ dbSNP | Ensembl ].
VAR_061300
Natural varianti482 – 4821D → N in HYPT3. 1 Publication
VAR_065951

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ508777 mRNA. Translation: CAD48514.1.
AC055715 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96637.1.
BK000977 Genomic DNA. Translation: DAA00404.1. Sequence problems.
CCDSiCCDS8832.1.
RefSeqiNP_778223.2. NM_175053.3.
UniGeneiHs.660125.

Genome annotation databases

EnsembliENST00000305620; ENSP00000307240; ENSG00000170484.
GeneIDi121391.
KEGGihsa:121391.
UCSCiuc001sap.1. human.

Polymorphism databases

DMDMi166218812.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ508777 mRNA. Translation: CAD48514.1 .
AC055715 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96637.1 .
BK000977 Genomic DNA. Translation: DAA00404.1 . Sequence problems.
CCDSi CCDS8832.1.
RefSeqi NP_778223.2. NM_175053.3.
UniGenei Hs.660125.

3D structure databases

ProteinModelPortali Q7RTS7.
SMRi Q7RTS7. Positions 137-287, 306-448.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125727. 3 interactions.
STRINGi 9606.ENSP00000307240.

PTM databases

PhosphoSitei Q7RTS7.

Polymorphism databases

DMDMi 166218812.

Proteomic databases

MaxQBi Q7RTS7.
PaxDbi Q7RTS7.
PRIDEi Q7RTS7.

Protocols and materials databases

DNASUi 121391.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305620 ; ENSP00000307240 ; ENSG00000170484 .
GeneIDi 121391.
KEGGi hsa:121391.
UCSCi uc001sap.1. human.

Organism-specific databases

CTDi 121391.
GeneCardsi GC12M052959.
H-InvDB HIX0036697.
HGNCi HGNC:28929. KRT74.
HPAi HPA048596.
MIMi 194300. phenotype.
608248. gene.
613981. phenotype.
614929. phenotype.
neXtProti NX_Q7RTS7.
Orphaneti 90368. Hypotrichosis simplex of the scalp.
69084. Pure hair and nail ectodermal dysplasia.
170. Woolly hair.
PharmGKBi PA147357741.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266742.
GeneTreei ENSGT00760000118796.
HOGENOMi HOG000230976.
HOVERGENi HBG013015.
InParanoidi Q7RTS7.
KOi K07605.
PhylomeDBi Q7RTS7.
TreeFami TF317854.

Miscellaneous databases

GenomeRNAii 121391.
NextBioi 80732.
PROi Q7RTS7.
SOURCEi Search...

Gene expression databases

Bgeei Q7RTS7.
CleanExi HS_KRT74.
ExpressionAtlasi Q7RTS7. baseline and differential.
Genevestigatori Q7RTS7.

Family and domain databases

InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
Pfami PF00038. Filament. 1 hit.
[Graphical view ]
PRINTSi PR01276. TYPE2KERATIN.
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "K6irs1, K6irs2, K6irs3, and K6irs4 represent the inner-root-sheath-specific type II epithelial keratins of the human hair follicle."
    Langbein L., Rogers M.A., Praetzel S., Winter H., Schweizer J.
    J. Invest. Dermatol. 120:512-522(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT ASP-271.
    Tissue: Scalp.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, VARIANT ASP-271.
  5. "K25 (K25irs1), K26 (K25irs2), K27 (K25irs3), and K28 (K25irs4) represent the type I inner root sheath keratins of the human hair follicle."
    Langbein L., Rogers M.A., Praetzel-Wunder S., Helmke B., Schirmacher P., Schweizer J.
    J. Invest. Dermatol. 126:2377-2386(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "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 THR-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Autosomal-dominant woolly hair resulting from disruption of keratin 74 (KRT74), a potential determinant of human hair texture."
    Shimomura Y., Wajid M., Petukhova L., Kurban M., Christiano A.M.
    Am. J. Hum. Genet. 86:632-638(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ADWH LYS-148, CHARACTERIZATION OF VARIANT ADWH LYS-148.
  8. "Novel mutations in the keratin-74 (KRT74) gene underlie autosomal dominant woolly hair/hypotrichosis in Pakistani families."
    Wasif N., Naqvi S.K., Basit S., Ali N., Ansar M., Ahmad W.
    Hum. Genet. 129:419-424(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HYPT3 ASN-482.
  9. "Autosomal recessive transmission of a rare KRT74 variant causes hair and nail ectodermal dysplasia: allelism with dominant woolly hair/hypotrichosis."
    Raykova D., Klar J., Azhar A., Khan T.N., Malik N.A., Iqbal M., Tariq M., Baig S.M., Dahl N.
    PLoS ONE 9:E93607-E93607(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ECTD7, VARIANT ECTD7 SER-274, TISSUE SPECIFICITY.

Entry informationi

Entry nameiK2C74_HUMAN
AccessioniPrimary (citable) accession number: Q7RTS7
Secondary accession number(s): B5MD61, Q86Y45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: October 29, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa, respectively).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3