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Q14678 (KANK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
KN motif and ankyrin repeat domain-containing protein 1
Alternative name(s):
Ankyrin repeat domain-containing protein 15
Kidney ankyrin repeat-containing protein
Gene names
Name:KANK1
Synonyms:ANKRD15, KANK, KIAA0172
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length1352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the control of cytoskeleton formation by regulating actin polymerization. Inhibits actin fiber formation and cell migration. Inhibits RhoA activity; the function involves phosphorylation through PI3K/Akt signaling and may depend on the competetive interaction with 14-3-3 adapter proteins to sequester them from active complexes. Inhibits the formation of lamellipodia but not of filopodia; the function may depend on the competetive interaction with BAIAP2 to block its association with activated RAC1. Inhibits fibronectin-mediated cell spreading; the function is partially mediated by BAIAP2. Inhibits neurite outgrowth. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. In the nucleus, is involved in beta-catenin-dependent activation of transcription. Potential tumor suppressor for renal cell carcinoma. Ref.5 Ref.8 Ref.9 Ref.12 Ref.15

Subunit structure

Interacts with YWHAQ; the interaction requires KANK1 phosphorylation at Ser-325 and is enhanced by growth factor stimulation. Interacts with YWHAB, YWHAG, YWHAE, YWHAH, YWHAZ and SFN; the interaction requires KANK1 phosphorylation at Ser-325. Interacts with ARFGEF1; however, colocalization cannot be experimentally confirmed. Interacts with BAIAP2. Interacts (via ANK repeats 1-5) with KIF21A (via coiled coil region); KIF21A enhances translocation of KANK1 to the plasma membrane. Interacts with CTNNB1. Ref.8 Ref.9 Ref.11 Ref.12 Ref.15

Subcellular location

Cell projection › ruffle membrane. Note: Colocalizes with KIF21A in membrane ruffles. Ref.5 Ref.8

Isoform 1: Cytoplasm. Nucleus. Note: Shuttles between the cytoplasm and nucleus. Ref.5 Ref.8

Isoform 2: Cytoplasm. Nucleus. Cell projection › ruffle membrane. Note: Shuttles between the cytoplasm and nucleus. Ref.5 Ref.8

Tissue specificity

Widely expressed. Isoform 1 is predominantly expressed in heart and kidney. Isoform 2 probably is widely expressed at basic levels. Ref.6

Involvement in disease

Cerebral palsy, spastic quadriplegic 2 (CPSQ2) [MIM:612900]: A non-progressive disorder of movement and/or posture resulting from defects in the developing central nervous system. Affected individuals manifest congenital hypotonia evolving over the first year to spastic quadriplegia with accompanying transient nystagmus and varying degrees of mental retardation. Neuroimaging shows brain atrophy and ventriculomegaly.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Contains 5 ANK repeats.

Sequence caution

The sequence BAA11489.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell membrane
Cell projection
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative promoter usage
Polymorphism
   DiseaseTumor suppressor
   DomainANK repeat
Coiled coil
Repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of Rho protein signal transduction

Inferred from mutant phenotype Ref.9. Source: UniProtKB

negative regulation of actin filament polymerization

Inferred from direct assay Ref.9. Source: UniProtKB

negative regulation of cell migration

Inferred from mutant phenotype Ref.9. Source: UniProtKB

negative regulation of insulin receptor signaling pathway

Inferred from mutant phenotype Ref.9. Source: UniProtKB

negative regulation of lamellipodium morphogenesis

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of neuron projection development

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of ruffle assembly

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of substrate adhesion-dependent cell spreading

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of Wnt receptor signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of catenin import into nucleus

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of wound healing

Inferred from mutant phenotype Ref.15. Source: UniProtKB

regulation of establishment of cell polarity

Inferred from mutant phenotype Ref.15. Source: UniProtKB

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.8. Source: UniProtKB

nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

ruffle membrane

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionbeta-catenin binding

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: Q14678-1)

Also known as: Kank-L;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14678-2)

Also known as: Kank-S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-158: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13521352KN motif and ankyrin repeat domain-containing protein 1
PRO_0000066911

Regions

Repeat1161 – 119131ANK 1
Repeat1195 – 122834ANK 2
Repeat1233 – 126230ANK 3
Repeat1266 – 129833ANK 4
Repeat1300 – 132930ANK 5
Region43 – 5210Nuclear export signal 1 (NES 1)
Region65 – 684Nuclear localization signal 1 (NLS 1)
Region125 – 13410Nuclear export signal 2 (NES 2)
Region291 – 467177Interaction with KIF21A
Region613 – 62210Nuclear export signal 3 (NES 3)
Region979 – 99214Nuclear localization signal 2 (NLS 2)
Region1156 – 1308153Interaction with KIF21A
Coiled coil258 – 31659 Potential
Coiled coil361 – 39535 Potential
Coiled coil446 – 50055 Potential

Amino acid modifications

Modified residue3251Phosphoserine; by PKB Ref.9 Ref.13 Ref.16

Natural variations

Alternative sequence1 – 158158Missing in isoform 2.
VSP_043958
Natural variant2061N → K. Ref.4
Corresponds to variant rs17857145 [ dbSNP | Ensembl ].
VAR_026212
Natural variant2101H → Q.
Corresponds to variant rs28374506 [ dbSNP | Ensembl ].
VAR_048298
Natural variant3211K → R.
Corresponds to variant rs17857159 [ dbSNP | Ensembl ].
VAR_048299
Natural variant4321E → Q. Ref.3 Ref.4
Corresponds to variant rs4465020 [ dbSNP | Ensembl ].
VAR_026213
Natural variant4641S → A. Ref.1
Corresponds to variant rs912174 [ dbSNP | Ensembl ].
VAR_016697
Natural variant6641A → V.
Corresponds to variant rs3824421 [ dbSNP | Ensembl ].
VAR_048300
Natural variant6671R → H.
Corresponds to variant rs3824420 [ dbSNP | Ensembl ].
VAR_048301
Natural variant9011N → S.
Corresponds to variant rs12352313 [ dbSNP | Ensembl ].
VAR_048302
Natural variant10551I → T.
Corresponds to variant rs34832656 [ dbSNP | Ensembl ].
VAR_048303

Experimental info

Mutagenesis431L → A: Nuclear localization; when associated A-52; A-125; A-129; A-134; A-613; A-616; A-620 and A-622. Ref.8
Mutagenesis521I → A: Nuclear localization; when associated A-43; A-125; A-129; A-134; A-613; A-616; A-620 and A-622. Ref.8
Mutagenesis65 – 684KRRK → AAAA: Enhanced cytoplasmic localization; when associated with 979-A--A-981 and 991-A-A-992. Ref.8
Mutagenesis1251L → A: Nuclear localization; when associated A-43; A-52; A-129; A-134; A-613; A-616; A-620 and A-622. Ref.8
Mutagenesis1291L → A: Nuclear localization; when associated A-43; A-52; A-125; A-134; A-613; A-616; A-620 and A-622. Ref.8
Mutagenesis1341I → A: Nuclear localization; when associated A-43; A-52; A-125; A-129; A-613; A-616; A-620 and A-622. Ref.8
Mutagenesis3251S → A: Abolishes phosphorylation by PKB. Abolishes interaction with YWHAB; YWHAG; YWHAE; YWHAH; YWHAQ; YWHAZ and SFN. Ref.9
Mutagenesis6131L → A: Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-616; A-620 and A-622. Ref.8
Mutagenesis6161L → A: Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-613; A-620 and A-622. Ref.8
Mutagenesis6201L → A: Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-613; A-616 and A-622. Ref.8
Mutagenesis6221L → A: Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-613; A-616 and A-620. Ref.8
Mutagenesis979 – 9813KKK → AAA: Enhanced cytoplasmic localization; when associated with 65-A--A-68 and 991-A-A-992. Ref.8
Mutagenesis991 – 9922KK → AA: Enhanced cytoplasmic localization; when associated with 65-A--68 and 979-A--A-981.

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Kank-L) [UniParc].

Last modified August 30, 2005. Version 3.
Checksum: 0C3993143391363B

FASTA1,352147,289
        10         20         30         40         50         60 
MAHTTKVNGS ASGKAGDILS GDQDKEQKDP YFVETPYGYQ LDLDFLKYVD DIQKGNTIKR 

        70         80         90        100        110        120 
LNIQKRRKPS VPCPEPRTTS GQQGIWTSTE SLSSSNSDDN KQCPNFLIAR SQVTSTPISK 

       130        140        150        160        170        180 
PPPPLETSLP FLTIPENRQL PPPSPQLPKH NLHVTKTLME TRRRLEQERA TMQMTPGEFR 

       190        200        210        220        230        240 
RPRLASFGGM GTTSSLPSFV GSGNHNPAKH QLQNGYQGNG DYGSYAPAAP TTSSMGSSIR 

       250        260        270        280        290        300 
HSPLSSGIST PVTNVSPMHL QHIREQMAIA LKRLKELEEQ VRTIPVLQVK ISVLQEEKRQ 

       310        320        330        340        350        360 
LVSQLKNQRA ASQINVCGVR KRSYSAGNAS QLEQLSRARR SGGELYIDYE EEEMETVEQS 

       370        380        390        400        410        420 
TQRIKEFRQL TADMQALEQK IQDSSCEASS ELRENGECRS VAVGAEENMN DIVVYHRGSR 

       430        440        450        460        470        480 
SCKDAAVGTL VEMRNCGVSV TEAMLGVMTE ADKEIELQQQ TIESLKEKIY RLEVQLRETT 

       490        500        510        520        530        540 
HDREMTKLKQ ELQAAGSRKK VDKATMAQPL VFSKVVEAVV QTRDQMVGSH MDLVDTCVGT 

       550        560        570        580        590        600 
SVETNSVGIS CQPECKNKVV GPELPMNWWI VKERVEMHDR CAGRSVEMCD KSVSVEVSVC 

       610        620        630        640        650        660 
ETGSNTEESV NDLTLLKTNL NLKEVRSIGC GDCSVDVTVC SPKECASRGV NTEAVSQVEA 

       670        680        690        700        710        720 
AVMAVPRTAD QDTSTDLEQV HQFTNTETAT LIESCTNTCL STLDKQTSTQ TVETRTVAVG 

       730        740        750        760        770        780 
EGRVKDINSS TKTRSIGVGT LLSGHSGFDR PSAVKTKESG VGQININDNY LVGLKMRTIA 

       790        800        810        820        830        840 
CGPPQLTVGL TASRRSVGVG DDPVGESLEN PQPQAPLGMM TGLDHYIERI QKLLAEQQTL 

       850        860        870        880        890        900 
LAENYSELAE AFGEPHSQMG SLNSQLISTL SSINSVMKSA STEELRNPDF QKTSLGKITG 

       910        920        930        940        950        960 
NYLGYTCKCG GLQSGSPLSS QTSQPEQEVG TSEGKPISSL DAFPTQEGTL SPVNLTDDQI 

       970        980        990       1000       1010       1020 
AAGLYACTNN ESTLKSIMKK KDGNKDSNGA KKNLQFVGIN GGYETTSSDD SSSDESSSSE 

      1030       1040       1050       1060       1070       1080 
SDDECDVIEY PLEEEEEEED EDTRGMAEGH HAVNIEGLKS ARVEDEMQVQ ECEPEKVEIR 

      1090       1100       1110       1120       1130       1140 
ERYELSEKML SACNLLKNTI NDPKALTSKD MRFCLNTLQH EWFRVSSQKS AIPAMVGDYI 

      1150       1160       1170       1180       1190       1200 
AAFEAISPDV LRYVINLADG NGNTALHYSV SHSNFEIVKL LLDADVCNVD HQNKAGYTPI 

      1210       1220       1230       1240       1250       1260 
MLAALAAVEA EKDMRIVEEL FGCGDVNAKA SQAGQTALML AVSHGRIDMV KGLLACGADV 

      1270       1280       1290       1300       1310       1320 
NIQDDEGSTA LMCASEHGHV EIVKLLLAQP GCNGHLEDND GSTALSIALE AGHKDIAVLL 

      1330       1340       1350 
YAHVNFAKAQ SPGTPRLGRK TSPGPTHRGS FD

« Hide

Isoform 2 (Kank-S) [UniParc].

Checksum: F7CB58D947CCCE4C
Show »

FASTA1,194129,782

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-464.
Tissue: Bone marrow.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-432.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS LYS-206 AND GLN-432.
Tissue: Testis.
[5]"A novel ankyrin repeat-containing gene (Kank) located at 9p24 is a growth suppressor of renal cell carcinoma."
Sarkar S., Roy B.C., Hatano N., Aoyagi T., Gohji K., Kiyama R.
J. Biol. Chem. 277:36585-36591(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PUTATIVE FUNCTION, SUBCELLULAR LOCATION.
[6]"Alternative splicing of the human Kank gene produces two types of Kank protein."
Wang Y., Onishi Y., Kakinuma N., Roy B.C., Aoyagi T., Kiyama R.
Biochem. Biophys. Res. Commun. 330:1247-1253(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE (ISOFORM 2), TISSUE SPECIFICITY.
[7]"Deletion of the ANKRD15 gene at 9p24.3 causes parent-of-origin-dependent inheritance of familial cerebral palsy."
Lerer I., Sagi M., Meiner V., Cohen T., Zlotogora J., Abeliovich D.
Hum. Mol. Genet. 14:3911-3920(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CPSQ2.
[8]"Nucleo-cytoplasmic shuttling of human Kank protein accompanies intracellular translocation of beta-catenin."
Wang Y., Kakinuma N., Zhu Y., Kiyama R.
J. Cell Sci. 119:4002-4010(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1, MUTAGENESIS OF LEU-43; ILE-52; 65-LYS--LYS-68; LEU-125; LEU-129; ILE-134; LEU-613; LEU-616; LEU-620; LEU-622; 979-LYS--LYS-981 AND 991-LYS-LYS-992.
[9]"Kank regulates RhoA-dependent formation of actin stress fibers and cell migration via 14-3-3 in PI3K-Akt signaling."
Kakinuma N., Roy B.C., Zhu Y., Wang Y., Kiyama R.
J. Cell Biol. 181:537-549(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-325, INTERACTION WITH YWHAB; YWHAG; YWHAE; YWHAH; YWHAQ; YWHAZ AND SFN, MUTAGENESIS OF SER-325.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A major mutation of KIF21A associated with congenital fibrosis of the extraocular muscles type 1 (CFEOM1) enhances translocation of Kank1 to the membrane."
Kakinuma N., Kiyama R.
Biochem. Biophys. Res. Commun. 386:639-644(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIF21A.
[12]"Kank attenuates actin remodeling by preventing interaction between IRSp53 and Rac1."
Roy B.C., Kakinuma N., Kiyama R.
J. Cell Biol. 184:253-267(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BAIAP2.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Effects of brefeldin A-inhibited guanine nucleotide-exchange (BIG) 1 and KANK1 proteins on cell polarity and directed migration during wound healing."
Li C.C., Kuo J.C., Waterman C.M., Kiyama R., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 108:19228-19233(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARFGEF1.
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D79994 mRNA. Translation: BAA11489.2. Different initiation.
AL136979 Genomic DNA. Translation: CAH70388.1.
AL136979 Genomic DNA. Translation: CAM13084.1.
CH471071 Genomic DNA. Translation: EAW58821.1.
CH471071 Genomic DNA. Translation: EAW58822.1.
BC037495 mRNA. Translation: AAH37495.1.
IPIIPI00339320.
RefSeqNP_001243805.1. NM_001256876.1.
NP_001243806.1. NM_001256877.1.
NP_055973.2. NM_015158.3.
NP_694856.1. NM_153186.4.
UniGeneHs.306764.

3D structure databases

ProteinModelPortalQ14678.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-56491N.
IntActQ14678. 13 interactions.
STRING9606.ENSP00000371734.

PTM databases

PhosphoSiteQ14678.

Polymorphism databases

DMDM73920184.

Proteomic databases

PaxDbQ14678.
PRIDEQ14678.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000382293; ENSP00000371730; ENSG00000107104.
ENST00000382297; ENSP00000371734; ENSG00000107104.
ENST00000382303; ENSP00000371740; ENSG00000107104.
GeneID23189.
KEGGhsa:23189.
UCSCuc003zgl.1. human.

Organism-specific databases

CTD23189.
GeneCardsGC09P000461.
HGNCHGNC:19309. KANK1.
HPAHPA005539.
MIM607704. gene.
612900. phenotype.
neXtProtNX_Q14678.
Orphanet91498. Familial congenital palsy of trochlear nerve.
210141. Inherited congenital spastic tetraplegia.
PharmGKBPA162392554.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000230897.
HOVERGENHBG050511.
InParanoidQ14678.
OMAVQTRDQM.
OrthoDBEOG49P9ZW.

Gene expression databases

ArrayExpressQ14678.
BgeeQ14678.
CleanExHS_KANK1.
GenevestigatorQ14678.
GermOnlineENSG00000107104. Homo sapiens.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR021939. KN_motif.
[Graphical view]
PfamPF00023. Ank. 3 hits.
PF12075. KN_motif. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMSSF48403. ANK. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKANK1. human.
GenomeRNAi23189.
NextBio44663.
SOURCESearch...

Entry information

Entry nameKANK1_HUMAN
AccessionPrimary (citable) accession number: Q14678
Secondary accession number(s): A2A2W8 expand/collapse secondary AC list , D3DRH3, Q5W0W0, Q8IY65, Q8WX74
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: August 30, 2005
Last modified: May 1, 2013
This is version 107 of the entry and version 3 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

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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