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Protein

Keratin, type II cytoskeletal 1b

Gene

KRT77

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei418 – 4181Stutter

GO - Molecular functioni

  1. structural molecule activity Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cytoskeletal 1b
Alternative name(s):
Cytokeratin-1B
Short name:
CK-1B
Keratin-77
Short name:
K77
Type-II keratin Kb39
Gene namesi
Name:KRT77
Synonyms:KRT1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:20411. KRT77.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 578578Keratin, type II cytoskeletal 1bPRO_0000063711Add
BLAST

Post-translational modificationi

Undergoes deimination of some arginine residues (citrullination).By similarity

Keywords - PTMi

Citrullination

Proteomic databases

MaxQBiQ7Z794.
PaxDbiQ7Z794.
PRIDEiQ7Z794.

PTM databases

PhosphoSiteiQ7Z794.

Expressioni

Tissue specificityi

Expressed exclusively in skin.1 Publication

Gene expression databases

BgeeiQ7Z794.
CleanExiHS_KRT77.
ExpressionAtlasiQ7Z794. baseline and differential.
GenevestigatoriQ7Z794.

Organism-specific databases

HPAiHPA045934.

Interactioni

Protein-protein interaction databases

BioGridi131903. 14 interactions.
IntActiQ7Z794. 4 interactions.
STRINGi9606.ENSP00000342710.

Structurei

3D structure databases

ProteinModelPortaliQ7Z794.
SMRiQ7Z794. Positions 161-302, 330-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 163163HeadAdd
BLAST
Regioni164 – 474311RodAdd
BLAST
Regioni164 – 20037Coil 1AAdd
BLAST
Regioni201 – 21919Linker 1Add
BLAST
Regioni220 – 31192Coil 1BAdd
BLAST
Regioni312 – 33524Linker 12Add
BLAST
Regioni336 – 474139Coil 2Add
BLAST
Regioni475 – 578104TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Sequence Analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG146126.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiQ7Z794.
KOiK07605.
OMAiNTSHRRI.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ7Z794.
TreeFamiTF317854.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM00150. SPEC. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7Z794-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHQFSSQSA FSSMSRRVYS TSSSAGSGGG SPAVGSVCYA RGRCGGGGYG
60 70 80 90 100
IHGRGFGSRS LYNLGGSRSI SINLMGRSTS GFCQGGGVGG FGGGRGFGVG
110 120 130 140 150
STGAGGFGGG GFGGAGFGTS NFGLGGFGPY CPPGGIQEVT INQSLLEPLH
160 170 180 190 200
LEVDPEIQRI KTQEREQIMV LNNKFASFID KVRFLEQQNQ VLQTKWELLQ
210 220 230 240 250
QVNTSTGTNN LEPLLENYIG DLRRQVDLLS AEQMRQNAEV RSMQDVVEDY
260 270 280 290 300
KSKYEDEINK RTGSENDFVV LKKDVDAAYV SKVDLESRVD TLTGEVNFLK
310 320 330 340 350
YLFLTELSQV QTHISDTNVI LSMDNNRSLD LDSIIDAVRT QYELIAQRSK
360 370 380 390 400
DEAEALYQTK YQELQITAGR HGDDLKNSKM EIAELNRTVQ RLQAEISNVK
410 420 430 440 450
KQIEQMQSLI SDAEERGEQA LQDAWQKLQD LEEALQQSKE ELARLLRDYQ
460 470 480 490 500
AMLGVKLSLD VEIATYRQLL EGEESRMSGE LQSHVSISVQ NSQVSVNGGA
510 520 530 540 550
GGGGSYGSGG YGGGSGGGYG GGRSYRGGGA RGRSGGGYGS GCGGGGGSYG
560 570
GSGRSGRGSS RVQIIQTSTN TSHRRILE
Length:578
Mass (Da):61,901
Last modified:October 4, 2010 - v3
Checksum:i232F92351DF0FDCA
GO

Sequence cautioni

The sequence DAA00402.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti336 – 3361D → N in CAD91892 (PubMed:15737194).Curated
Sequence conflicti533 – 5331R → G in CAD91892 (PubMed:15737194).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101A → T.
Corresponds to variant rs17118224 [ dbSNP | Ensembl ].
VAR_056022

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ564104 mRNA. Translation: CAD91892.1.
AC055716 Genomic DNA. No translation available.
BK000975 Genomic DNA. Translation: DAA00402.1. Sequence problems.
CCDSiCCDS8837.1.
RefSeqiNP_778253.2. NM_175078.2.
UniGeneiHs.334989.

Genome annotation databases

EnsembliENST00000341809; ENSP00000342710; ENSG00000189182.
GeneIDi374454.
KEGGihsa:374454.
UCSCiuc001saw.3. human.

Polymorphism databases

DMDMi308153590.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ564104 mRNA. Translation: CAD91892.1.
AC055716 Genomic DNA. No translation available.
BK000975 Genomic DNA. Translation: DAA00402.1. Sequence problems.
CCDSiCCDS8837.1.
RefSeqiNP_778253.2. NM_175078.2.
UniGeneiHs.334989.

3D structure databases

ProteinModelPortaliQ7Z794.
SMRiQ7Z794. Positions 161-302, 330-472.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131903. 14 interactions.
IntActiQ7Z794. 4 interactions.
STRINGi9606.ENSP00000342710.

PTM databases

PhosphoSiteiQ7Z794.

Polymorphism databases

DMDMi308153590.

Proteomic databases

MaxQBiQ7Z794.
PaxDbiQ7Z794.
PRIDEiQ7Z794.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341809; ENSP00000342710; ENSG00000189182.
GeneIDi374454.
KEGGihsa:374454.
UCSCiuc001saw.3. human.

Organism-specific databases

CTDi374454.
GeneCardsiGC12M053083.
H-InvDBHIX0036740.
HGNCiHGNC:20411. KRT77.
HPAiHPA045934.
MIMi611158. gene.
neXtProtiNX_Q7Z794.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG146126.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiQ7Z794.
KOiK07605.
OMAiNTSHRRI.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ7Z794.
TreeFamiTF317854.

Miscellaneous databases

GenomeRNAii374454.
NextBioi100191.
PROiQ7Z794.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z794.
CleanExiHS_KRT77.
ExpressionAtlasiQ7Z794. baseline and differential.
GenevestigatoriQ7Z794.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM00150. SPEC. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: SkinImported.
  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiK2C1B_HUMAN
AccessioniPrimary (citable) accession number: Q7Z794
Secondary accession number(s): Q7RTS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2005
Last sequence update: October 4, 2010
Last modified: March 3, 2015
This is version 102 of the entry and version 3 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; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.