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Q6TDP4 (KLH17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kelch-like protein 17
Alternative name(s):
Actinfilin
Gene names
Name:KLHL17
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Substrate-recognition component of some cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(KLHL17) mediates the ubiquitination and subsequenct degradation of GLUR6. May play a role in the actin-based neuronal function By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with F-actin; the interaction disruptes the F-actin structures and leads to marked changes of neuronal morphology. Component of a complex, composed of PDZK1, SYNGAP1, KLHL17 and NMDA receptors. Interacts directly with PDZK1 (via PDZ1 domain); the interaction is important for integrity of actin cytoskeleton structures in neurons. Interacts with DLG4 and SYNGAP1. Interacts (via kelch repeats) with GRIK2 (via C-terminus); the interaction targets GRIK2 for degradation via ubiquitin-proteasome pathway. Interacts with GRIK1. Interacts with (via BTB domain) CUL3; the interaction regulates surface GRIK2 expression By similarity.

Subcellular location

Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cell junctionsynapse By similarity. Note: Postsynaptic density By similarity.

Sequence similarities

Contains 1 BACK (BTB/Kelch associated) domain.

Contains 1 BTB (POZ) domain.

Contains 6 Kelch repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 642642Kelch-like protein 17
PRO_0000119119

Regions

Domain92 – 15968BTB
Domain194 – 296103BACK
Repeat343 – 38947Kelch 1
Repeat390 – 43647Kelch 2
Repeat438 – 48346Kelch 3
Repeat484 – 53047Kelch 4
Repeat532 – 57746Kelch 5
Repeat578 – 62447Kelch 6
Region289 – 641353Interaction with F-actin By similarity
Region640 – 6423Interaction with PDZK1 By similarity
Compositional bias15 – 5238Pro-rich

Sequences

Sequence LengthMass (Da)Tools
Q6TDP4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FE37BBCCD32131BF

FASTA64269,874
        10         20         30         40         50         60 
MQPRSERPAG RTQSPEHGSP GPGPEAPPPP PPQPPAPEAE RTRPRQARPA APMEGAVQLL 

        70         80         90        100        110        120 
SREGHSVAHN SKRHYHDAFV AMSRMRQRGL LCDIVLHVAA KEIRAHKVVL ASCSPYFHAM 

       130        140        150        160        170        180 
FTNEMSESRQ THVTLHDIDP QALDQLVQFA YTAEIVVGEG NVQTLLPAAS LLQLNGVRDA 

       190        200        210        220        230        240 
CCKFLLSQLD PSNCLGIRGF ADAHSCSDLL KAAHRYVLQH FVDVAKTEEF MLLPLKQVLE 

       250        260        270        280        290        300 
LVSSDSLNVP SEEEVYRAVL SWVKHDVDAR RQHVPRLMKC VRLPLLSRDF LLGHVDAESL 

       310        320        330        340        350        360 
VRHHPDCKDL LIEALKFHLL PEQRGVLGTS RTRPRRCEGA GPVLFAVGGG SLFAIHGDCE 

       370        380        390        400        410        420 
AYDTRTDRWH VVASMSTRRA RVGVAAVGNR LYAVGGYDGT SDLATVESYD PVTNTWQPEV 

       430        440        450        460        470        480 
SMGTRRSCLG VAALHGLLYS AGGYDGASCL NSAERYDPLT GTWTSVAAMS TRRRYVRVAT 

       490        500        510        520        530        540 
LDGNLYAVGG YDSSSHLATV EKYEPQVNVW SPVASMLSRR SSAGVAVLEG ALYVAGGNDG 

       550        560        570        580        590        600 
TSCLNSVERY SPKAGAWESV APMNIRRSTH DLVAMDGWLY AVGGNDGSSS LNSIEKYNPR 

       610        620        630        640 
TNKWVAASCM FTRRSSVGVA VLELLNFPPP SSPTLSVSST SL 

« Hide

References

« Hide 'large scale' references
[1]Huang C.Q., Wu S.L., Shan Y.X.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY423763 mRNA. Translation: AAR03710.1.
AL645608 Genomic DNA. Translation: CAI15569.1.
CCDSCCDS30550.1.
RefSeqNP_938073.1. NM_198317.2.
UniGeneHs.109212.

3D structure databases

ProteinModelPortalQ6TDP4.
SMRQ6TDP4. Positions 74-320, 343-622.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130885. 1 interaction.
STRING9606.ENSP00000343930.

PTM databases

PhosphoSiteQ6TDP4.

Polymorphism databases

DMDM52783052.

Proteomic databases

MaxQBQ6TDP4.
PaxDbQ6TDP4.
PRIDEQ6TDP4.

Protocols and materials databases

DNASU339451.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338591; ENSP00000343930; ENSG00000187961.
GeneID339451.
KEGGhsa:339451.
UCSCuc001aca.2. human.

Organism-specific databases

CTD339451.
GeneCardsGC01P000885.
HGNCHGNC:24023. KLHL17.
HPAHPA031251.
neXtProtNX_Q6TDP4.
PharmGKBPA134887396.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236397.
HOGENOMHOG000230814.
HOVERGENHBG014286.
InParanoidQ6TDP4.
KOK10454.
OMAMQLLNRD.
OrthoDBEOG7ZWD17.
PhylomeDBQ6TDP4.
TreeFamTF329218.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ6TDP4.
BgeeQ6TDP4.
CleanExHS_KLHL17.
GenevestigatorQ6TDP4.

Family and domain databases

Gene3D2.130.10.80. 1 hit.
3.30.710.10. 1 hit.
InterProIPR011705. BACK.
IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR011043. Gal_Oxase/kelch_b-propeller.
IPR015916. Gal_Oxidase_b-propeller.
IPR017096. Kelch-like_gigaxonin-typ.
IPR006652. Kelch_1.
[Graphical view]
PfamPF07707. BACK. 1 hit.
PF00651. BTB. 1 hit.
PF01344. Kelch_1. 5 hits.
[Graphical view]
PIRSFPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMARTSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view]
SUPFAMSSF50965. SSF50965. 1 hit.
SSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKLHL17. human.
GenomeRNAi339451.
NextBio97399.
PROQ6TDP4.

Entry information

Entry nameKLH17_HUMAN
AccessionPrimary (citable) accession number: Q6TDP4
Secondary accession number(s): Q5SV94
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM