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Protein

Ankyrin repeat and SAM domain-containing protein 6

Gene

Anks6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for renal function.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ankyrin repeat and SAM domain-containing protein 6
Alternative name(s):
Polycystic kidney disease protein 1
SamCystin
Sterile alpha motif domain-containing protein 6
Short name:
SAM domain-containing protein 6
Gene namesi
Name:Anks6
Synonyms:Pkdr1, Samd6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3334. Anks6.

Subcellular locationi

  • Cell projectioncilium By similarity
  • Cytoplasm 1 Publication

  • Note: Localizes to the proximal region of the primary cilium in the presence of INVS.By similarity

GO - Cellular componenti

  • cilium Source: UniProtKB-SubCell
  • cytoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Defects in Anks6 are the cause of polycystic kidney disease (cy). Heterozygous cy rats are characterized by progressive formation and enlargement of cysts in kidneys.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi129N → A: Decreased NEK8-binding, but no effect on INVS-binding; when associated with A-209. 1 Publication1
Mutagenesisi209N → A: Decreased NEK8-binding, but no effect on INVS-binding; when associated with A-129. 1 Publication1
Mutagenesisi433Q → R: No effect on interaction with INVS, NEK8 AND NPHP3, nor on ciliary localization. Unable to rescue ANKS6 knockout in a heterologous system. 1 Publication1

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000670671 – 885Ankyrin repeat and SAM domain-containing protein 6Add BLAST885

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1293-hydroxyasparagine1 Publication1
Modified residuei650PhosphoserineBy similarity1
Modified residuei734PhosphoserineBy similarity1
Modified residuei742PhosphoserineBy similarity1

Post-translational modificationi

Hydroxylated at Asn-129, most probably by HIF1AN. This hydroxylation results in decreased NEK8-binding.1 Publication

Keywords - PTMi

Hydroxylation, Phosphoprotein

Proteomic databases

PaxDbiP0C0T2.
PRIDEiP0C0T2.

Expressioni

Tissue specificityi

Widely expressed with moderate level in brain, skeletal muscle and testis. Expressed in renal tubules.1 Publication

Gene expression databases

BgeeiENSRNOG00000023309.

Interactioni

Subunit structurei

Homooligomer (PubMed:19324013). Central component of a complex containing at least ANKS6, INVS, NEK8 and NPHP3. ANKS6 may organize complex assembly by linking INVS and NPHP3 to NEK8 and INVS may target the complex to the proximal ciliary axoneme (PubMed:23793029). Interacts (via SAM domain) with BICC1 (via KH domains) in an RNA-dependent manner (PubMed:19324013). Interacts with ANKS3 (PubMed:25671767).3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000056754.

Structurei

3D structure databases

ProteinModelPortaliP0C0T2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati8 – 37ANK 1Add BLAST30
Repeati68 – 97ANK 2Add BLAST30
Repeati101 – 130ANK 3Add BLAST30
Repeati134 – 163ANK 4Add BLAST30
Repeati181 – 210ANK 5Add BLAST30
Repeati215 – 244ANK 6Add BLAST30
Repeati282 – 312ANK 7Add BLAST31
Repeati316 – 345ANK 8Add BLAST30
Repeati350 – 379ANK 9Add BLAST30
Repeati383 – 414ANK 10Add BLAST32
Domaini773 – 836SAMPROSITE-ProRule annotationAdd BLAST64

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi609 – 769Ser-richAdd BLAST161

Domaini

The ankyrin repeats are necessary and sufficient for NEK8-binding.1 Publication
The SAM domain mediates interaction with the SAM domain of ANKS3.1 Publication

Sequence similaritiesi

Contains 10 ANK repeats.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG4369. Eukaryota.
KOG4374. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000231711.
HOVERGENiHBG059049.
InParanoidiP0C0T2.
PhylomeDBiP0C0T2.
TreeFamiTF328552.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF12796. Ank_2. 3 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 10 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 7 hits.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C0T2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEGALAPGL QLLLRACEQG DTDTARRLLE PGGEPVAGSE AGAEPAGPEA
60 70 80 90 100
ARAVEAGTPV PVDCSDEAGN SALQLAAAGG HEPLVRFLLR RGASVNSRNH
110 120 130 140 150
YGWSALMQAA RCGHASVAHL LLDHGADVNA QNRLGASVLT VASRGGHLGV
160 170 180 190 200
VKLLLEAGAT VDHRNPSGES TASGGSRDEL LGITALMAAV QHGHEAVVRL
210 220 230 240 250
LMEWGADPNH TARTVGWSPL MLAALLGKLS VVQQLVEKGA NPDHLGVLEK
260 270 280 290 300
TAFEVALDRK HRDLADYLDP LTTVRPKTDE EKRRPDIFHA LKMGNFQLVK
310 320 330 340 350
EIADEDPNHV NLVNGDGATP LMLAAVTGQL PLVQLLVEKH ADMNKQDSVH
360 370 380 390 400
GWTALMQATY HGNKEIVKYL LNQGADVTLR AKNGYTAFDL VMLLNDPDTE
410 420 430 440 450
LVRLLASVCM QVNKDRGGRP SHRPPLPHSK ARQPWSIPML PDDKGGLKSW
460 470 480 490 500
WSRMSNRFRK LKLMQTLPRG LAANQPLPFS DEPELALDST MRAPPQDRTN
510 520 530 540 550
HLGPPEAAHA AKDSGPGNPR REKDDVLLTT MLRNGAPFPR LPSDKLKAVI
560 570 580 590 600
PPFLPPSSFE LWSSDRSRTC PNGKADPMKT VLPPRASRAH PVGCVGTDGA
610 620 630 640 650
AGRPVKFPSI SRSPTSPASS GNFNHSPHSS GGASGVGSMS RLGGELHNRS
660 670 680 690 700
GGSVDSVLSQ IAAQRKKAAG LCEQKPPCQQ SSPVGPATGS SPPELPASLL
710 720 730 740 750
GSGSGSSNVT SSSKKLDPGK RPPSGTSATS KSTSPTLTPS PSPKGHTAES
760 770 780 790 800
SVSSSSSHRQ SKSSGGSSSG TITDEDELTG ILKKLSLEKY QPIFEEQEVD
810 820 830 840 850
MEAFLTLTDG DLQELGIKTD GSRQQILAAI SELNAGKGRE RQILQETIHN
860 870 880
FHSSFESSAS NTRAPGNSPC MAGWVRPEET VSSRR
Length:885
Mass (Da):93,809
Last modified:November 14, 2006 - v2
Checksum:iB4F91C5DFCD2D35E
GO

Sequence cautioni

The sequence AAH91436 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti870C → S in AAT76432 (PubMed:16207829).Curated1
Sequence conflicti870C → S in AAH91436 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti823R → W in cy; loss of ability to self-associate, does not affect interaction with Bicc1. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY661303 mRNA. Translation: AAT76432.1.
AABR03040311 Genomic DNA. No translation available.
BC091436 mRNA. Translation: AAH91436.1. Sequence problems.
RefSeqiNP_001015028.2. NM_001015028.2.
UniGeneiRn.101322.

Genome annotation databases

GeneIDi362515.
KEGGirno:362515.
UCSCiRGD:3334. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY661303 mRNA. Translation: AAT76432.1.
AABR03040311 Genomic DNA. No translation available.
BC091436 mRNA. Translation: AAH91436.1. Sequence problems.
RefSeqiNP_001015028.2. NM_001015028.2.
UniGeneiRn.101322.

3D structure databases

ProteinModelPortaliP0C0T2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000056754.

Proteomic databases

PaxDbiP0C0T2.
PRIDEiP0C0T2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi362515.
KEGGirno:362515.
UCSCiRGD:3334. rat.

Organism-specific databases

CTDi203286.
RGDi3334. Anks6.

Phylogenomic databases

eggNOGiKOG4369. Eukaryota.
KOG4374. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000231711.
HOVERGENiHBG059049.
InParanoidiP0C0T2.
PhylomeDBiP0C0T2.
TreeFamiTF328552.

Miscellaneous databases

PROiP0C0T2.

Gene expression databases

BgeeiENSRNOG00000023309.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF12796. Ank_2. 3 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 10 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 7 hits.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANKS6_RAT
AccessioniPrimary (citable) accession number: P0C0T2
Secondary accession number(s): Q2VWC0, Q5BJL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: November 14, 2006
Last modified: November 30, 2016
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.