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Protein

Keratin, type II cuticular Hb5

Gene

Krt85

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cuticular Hb5
Alternative name(s):
Keratin-85
Short name:
K85
Type II hair keratin Hb5
Type-II keratin Kb25
Gene namesi
Name:Krt85
Synonyms:Krt2-18, Krthb5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1859268. Krt85.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507Keratin, type II cuticular Hb5PRO_0000063703Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki229 – 229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9Z2T6.
PeptideAtlasiQ9Z2T6.
PRIDEiQ9Z2T6.

PTM databases

iPTMnetiQ9Z2T6.
PhosphoSiteiQ9Z2T6.

Expressioni

Gene expression databases

CleanExiMM_KRT85.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2T6.
SMRiQ9Z2T6. Positions 123-271, 289-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 123123HeadAdd
BLAST
Regioni124 – 430307RodAdd
BLAST
Regioni124 – 15835Coil 1AAdd
BLAST
Regioni159 – 16810Linker 1
Regioni169 – 269101Coil 1BAdd
BLAST
Regioni270 – 28617Linker 12Add
BLAST
Regioni287 – 430144Coil 2Add
BLAST
Regioni431 – 50777TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOVERGENiHBG013015.
InParanoidiQ9Z2T6.
KOiK07605.
PhylomeDBiQ9Z2T6.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z2T6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCRSYRISP GCGVTRNFSS CSAVAPKTGN RCCISAAPFR GVSCYRGLTG
60 70 80 90 100
FSSRSLCNPS PCGPRMAVGG FRSGSCGRSF GYRSGGVCGP SPPCITTVSV
110 120 130 140 150
NESLLTPLNL EIDPNAQCVK YEEKEQIKCL NSKFAAFIDK VRFLEQQNKL
160 170 180 190 200
LETKWQFYQN RKCCESNLEP LFGGYIEALR REAECVEADS GRLAAELNHV
210 220 230 240 250
QEAMEGYKKK YEEEVALRAT AENEFVVLKK DVDCAYLRKS DLEANVEALV
260 270 280 290 300
EESSFLKRLY EEEVCVLQAH ISDTSVIVKM DNSRDLNMDC VVAEIKAQYD
310 320 330 340 350
DVASRSRAEA ESWYRTKCEE MKATVIRHGE TLRRTKEEIN ELNRMIQRLT
360 370 380 390 400
AEIENAKCQR AKLEAAVAEA EQQGEAALAD ARCKLAELEG ALQKAKQDMA
410 420 430 440 450
CLLKEYQEVM NSKLALDIEI ATYRRLLEGE EQRLCEGVGS VNVCVSSSRG
460 470 480 490 500
GVTCGGLTYG TTPGRQIVSG PSVTGGSITV MAPDSCSPCQ PRASSFTCGS

SRSVRFA
Length:507
Mass (Da):55,759
Last modified:March 29, 2004 - v2
Checksum:i602A27B0D36C3334
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371A → R in AAD01692 (Ref. 1) Curated
Sequence conflicti261 – 2611E → G in AAD01692 (Ref. 1) Curated
Sequence conflicti434 – 4341L → F in BAB26069 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021836 mRNA. Translation: AAD01692.1.
AK028825 mRNA. Translation: BAC26139.1.
AK009099 mRNA. Translation: BAB26069.1.
RefSeqiNP_058575.2. NM_016879.2.
UniGeneiMm.347934.

Genome annotation databases

GeneIDi53622.
KEGGimmu:53622.
UCSCiuc007xtf.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021836 mRNA. Translation: AAD01692.1.
AK028825 mRNA. Translation: BAC26139.1.
AK009099 mRNA. Translation: BAB26069.1.
RefSeqiNP_058575.2. NM_016879.2.
UniGeneiMm.347934.

3D structure databases

ProteinModelPortaliQ9Z2T6.
SMRiQ9Z2T6. Positions 123-271, 289-429.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ9Z2T6.
PhosphoSiteiQ9Z2T6.

Proteomic databases

MaxQBiQ9Z2T6.
PeptideAtlasiQ9Z2T6.
PRIDEiQ9Z2T6.

Protocols and materials databases

DNASUi53622.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi53622.
KEGGimmu:53622.
UCSCiuc007xtf.3. mouse.

Organism-specific databases

CTDi3891.
MGIiMGI:1859268. Krt85.

Phylogenomic databases

HOVERGENiHBG013015.
InParanoidiQ9Z2T6.
KOiK07605.
PhylomeDBiQ9Z2T6.

Miscellaneous databases

PROiQ9Z2T6.
SOURCEiSearch...

Gene expression databases

CleanExiMM_KRT85.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Inoue T., Kizawa K.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
    Tissue: Hair follicle and Skin.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin and Tongue.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Liver and Lung.

Entry informationi

Entry nameiKRT85_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2T6
Secondary accession number(s): Q8CE83, Q9D7M4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: July 6, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two types of hair/microfibrillar keratin, I (acidic) and II (neutral to basic).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.