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Q14678

- KANK1_HUMAN

UniProt

Q14678 - KANK1_HUMAN

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Protein
KN motif and ankyrin repeat domain-containing protein 1
Gene
KANK1, ANKRD15, KANK, KIAA0172
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  1. beta-catenin binding Source: UniProtKB
  2. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. negative regulation of Rho protein signal transduction Source: UniProtKB
  2. negative regulation of actin filament polymerization Source: UniProtKB
  3. negative regulation of cell migration Source: UniProtKB
  4. negative regulation of insulin receptor signaling pathway Source: UniProtKB
  5. negative regulation of lamellipodium morphogenesis Source: UniProtKB
  6. negative regulation of neuron projection development Source: UniProtKB
  7. negative regulation of ruffle assembly Source: UniProtKB
  8. negative regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  9. positive regulation of Wnt signaling pathway Source: UniProtKB
  10. positive regulation of catenin import into nucleus Source: UniProtKB
  11. positive regulation of wound healing Source: UniProtKB
  12. regulation of establishment of cell polarity Source: UniProtKB
  13. regulation of transcription, DNA-templated Source: UniProtKB-KW
  14. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:KANK1
Synonyms:ANKRD15, KANK, KIAA0172
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:19309. KANK1.

Subcellular locationi

Cell projectionruffle membrane
Note: Colocalizes with KIF21A in membrane ruffles.2 Publications
Isoform 1 : Cytoplasm. Nucleus
Note: Shuttles between the cytoplasm and nucleus.2 Publications
Isoform 2 : Cytoplasm. Nucleus. Cell projectionruffle membrane
Note: Shuttles between the cytoplasm and nucleus.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431L → A: Nuclear localization; when associated A-52; A-125; A-129; A-134; A-613; A-616; A-620 and A-622. 1 Publication
Mutagenesisi52 – 521I → A: Nuclear localization; when associated A-43; A-125; A-129; A-134; A-613; A-616; A-620 and A-622. 1 Publication
Mutagenesisi65 – 684KRRK → AAAA: Enhanced cytoplasmic localization; when associated with 979-A--A-981 and 991-A-A-992. 1 Publication
Mutagenesisi125 – 1251L → A: Nuclear localization; when associated A-43; A-52; A-129; A-134; A-613; A-616; A-620 and A-622. 1 Publication
Mutagenesisi129 – 1291L → A: Nuclear localization; when associated A-43; A-52; A-125; A-134; A-613; A-616; A-620 and A-622. 1 Publication
Mutagenesisi134 – 1341I → A: Nuclear localization; when associated A-43; A-52; A-125; A-129; A-613; A-616; A-620 and A-622. 1 Publication
Mutagenesisi325 – 3251S → A: Abolishes phosphorylation by PKB. Abolishes interaction with YWHAB; YWHAG; YWHAE; YWHAH; YWHAQ; YWHAZ and SFN. 1 Publication
Mutagenesisi613 – 6131L → A: Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-616; A-620 and A-622. 1 Publication
Mutagenesisi616 – 6161L → A: Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-613; A-620 and A-622. 1 Publication
Mutagenesisi620 – 6201L → A: Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-613; A-616 and A-622. 1 Publication
Mutagenesisi622 – 6221L → A: Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-613; A-616 and A-620. 1 Publication
Mutagenesisi979 – 9813KKK → AAA: Enhanced cytoplasmic localization; when associated with 65-A--A-68 and 991-A-A-992. 1 Publication
Mutagenesisi991 – 9922KK → AA: Enhanced cytoplasmic localization; when associated with 65-A--68 and 979-A--A-981.

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

MIMi612900. phenotype.
Orphaneti91498. Familial congenital palsy of trochlear nerve.
210141. Inherited congenital spastic tetraplegia.
PharmGKBiPA162392554.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13521352KN motif and ankyrin repeat domain-containing protein 1
PRO_0000066911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei325 – 3251Phosphoserine; by PKB3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14678.
PaxDbiQ14678.
PRIDEiQ14678.

PTM databases

PhosphoSiteiQ14678.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ14678.
BgeeiQ14678.
CleanExiHS_KANK1.
GenevestigatoriQ14678.

Organism-specific databases

HPAiHPA005539.

Interactioni

Subunit structurei

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 CTNNB1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BAIAP2Q9UQB86EBI-2556221,EBI-525456
BAIAP2Q9UQB8-44EBI-6173812,EBI-6174091
CTNNB1P352222EBI-2556221,EBI-491549
KIF21AQ7Z4S63EBI-6173812,EBI-2691397
YWHAEP622583EBI-6173812,EBI-356498
YWHAGP619813EBI-6173812,EBI-359832
YWHAHQ049173EBI-6173812,EBI-306940
YWHAQP273483EBI-6173812,EBI-359854

Protein-protein interaction databases

BioGridi116798. 3 interactions.
DIPiDIP-56491N.
IntActiQ14678. 14 interactions.
MINTiMINT-7997401.
STRINGi9606.ENSP00000371734.

Structurei

3D structure databases

ProteinModelPortaliQ14678.
SMRiQ14678. Positions 1084-1325.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1161 – 119131ANK 1
Add
BLAST
Repeati1195 – 122834ANK 2
Add
BLAST
Repeati1233 – 126230ANK 3
Add
BLAST
Repeati1266 – 129833ANK 4
Add
BLAST
Repeati1300 – 132930ANK 5
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 5210Nuclear export signal 1 (NES 1)
Regioni65 – 684Nuclear localization signal 1 (NLS 1)
Regioni125 – 13410Nuclear export signal 2 (NES 2)
Regioni291 – 467177Interaction with KIF21A
Add
BLAST
Regioni613 – 62210Nuclear export signal 3 (NES 3)
Regioni979 – 99214Nuclear localization signal 2 (NLS 2)
Add
BLAST
Regioni1156 – 1308153Interaction with KIF21A
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili258 – 31659 Reviewed prediction
Add
BLAST
Coiled coili361 – 39535 Reviewed prediction
Add
BLAST
Coiled coili446 – 50055 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Contains 5 ANK repeats.

Keywords - Domaini

ANK repeat, Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000230897.
HOVERGENiHBG050511.
InParanoidiQ14678.
OMAiMTGLDHY.
OrthoDBiEOG7NW687.
PhylomeDBiQ14678.
TreeFamiTF324499.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR021939. KN_motif.
[Graphical view]
PfamiPF00023. Ank. 3 hits.
PF12075. KN_motif. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative promoter usage. Align

Isoform 1 (identifier: Q14678-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAHTTKVNGS ASGKAGDILS GDQDKEQKDP YFVETPYGYQ LDLDFLKYVD     50
DIQKGNTIKR LNIQKRRKPS VPCPEPRTTS GQQGIWTSTE SLSSSNSDDN 100
KQCPNFLIAR SQVTSTPISK PPPPLETSLP FLTIPENRQL PPPSPQLPKH 150
NLHVTKTLME TRRRLEQERA TMQMTPGEFR RPRLASFGGM GTTSSLPSFV 200
GSGNHNPAKH QLQNGYQGNG DYGSYAPAAP TTSSMGSSIR HSPLSSGIST 250
PVTNVSPMHL QHIREQMAIA LKRLKELEEQ VRTIPVLQVK ISVLQEEKRQ 300
LVSQLKNQRA ASQINVCGVR KRSYSAGNAS QLEQLSRARR SGGELYIDYE 350
EEEMETVEQS TQRIKEFRQL TADMQALEQK IQDSSCEASS ELRENGECRS 400
VAVGAEENMN DIVVYHRGSR SCKDAAVGTL VEMRNCGVSV TEAMLGVMTE 450
ADKEIELQQQ TIESLKEKIY RLEVQLRETT HDREMTKLKQ ELQAAGSRKK 500
VDKATMAQPL VFSKVVEAVV QTRDQMVGSH MDLVDTCVGT SVETNSVGIS 550
CQPECKNKVV GPELPMNWWI VKERVEMHDR CAGRSVEMCD KSVSVEVSVC 600
ETGSNTEESV NDLTLLKTNL NLKEVRSIGC GDCSVDVTVC SPKECASRGV 650
NTEAVSQVEA AVMAVPRTAD QDTSTDLEQV HQFTNTETAT LIESCTNTCL 700
STLDKQTSTQ TVETRTVAVG EGRVKDINSS TKTRSIGVGT LLSGHSGFDR 750
PSAVKTKESG VGQININDNY LVGLKMRTIA CGPPQLTVGL TASRRSVGVG 800
DDPVGESLEN PQPQAPLGMM TGLDHYIERI QKLLAEQQTL LAENYSELAE 850
AFGEPHSQMG SLNSQLISTL SSINSVMKSA STEELRNPDF QKTSLGKITG 900
NYLGYTCKCG GLQSGSPLSS QTSQPEQEVG TSEGKPISSL DAFPTQEGTL 950
SPVNLTDDQI AAGLYACTNN ESTLKSIMKK KDGNKDSNGA KKNLQFVGIN 1000
GGYETTSSDD SSSDESSSSE SDDECDVIEY PLEEEEEEED EDTRGMAEGH 1050
HAVNIEGLKS ARVEDEMQVQ ECEPEKVEIR ERYELSEKML SACNLLKNTI 1100
NDPKALTSKD MRFCLNTLQH EWFRVSSQKS AIPAMVGDYI AAFEAISPDV 1150
LRYVINLADG NGNTALHYSV SHSNFEIVKL LLDADVCNVD HQNKAGYTPI 1200
MLAALAAVEA EKDMRIVEEL FGCGDVNAKA SQAGQTALML AVSHGRIDMV 1250
KGLLACGADV NIQDDEGSTA LMCASEHGHV EIVKLLLAQP GCNGHLEDND 1300
GSTALSIALE AGHKDIAVLL YAHVNFAKAQ SPGTPRLGRK TSPGPTHRGS 1350
FD 1352
Length:1,352
Mass (Da):147,289
Last modified:August 30, 2005 - v3
Checksum:i0C3993143391363B
GO
Isoform 2 (identifier: Q14678-2) [UniParc]FASTAAdd to Basket

Also known as: Kank-S

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

Show »
Length:1,194
Mass (Da):129,782
Checksum:iF7CB58D947CCCE4C
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti206 – 2061N → K.1 Publication
Corresponds to variant rs17857145 [ dbSNP | Ensembl ].
VAR_026212
Natural varianti210 – 2101H → Q.
Corresponds to variant rs28374506 [ dbSNP | Ensembl ].
VAR_048298
Natural varianti321 – 3211K → R.
Corresponds to variant rs17857159 [ dbSNP | Ensembl ].
VAR_048299
Natural varianti432 – 4321E → Q.2 Publications
Corresponds to variant rs4465020 [ dbSNP | Ensembl ].
VAR_026213
Natural varianti464 – 4641S → A.1 Publication
Corresponds to variant rs912174 [ dbSNP | Ensembl ].
VAR_016697
Natural varianti664 – 6641A → V.
Corresponds to variant rs3824421 [ dbSNP | Ensembl ].
VAR_048300
Natural varianti667 – 6671R → H.
Corresponds to variant rs3824420 [ dbSNP | Ensembl ].
VAR_048301
Natural varianti901 – 9011N → S.
Corresponds to variant rs12352313 [ dbSNP | Ensembl ].
VAR_048302
Natural varianti1055 – 10551I → T.
Corresponds to variant rs34832656 [ dbSNP | Ensembl ].
VAR_048303

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 158158Missing in isoform 2.
VSP_043958Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34976.1. [Q14678-1]
CCDS6441.1. [Q14678-2]
RefSeqiNP_001243805.1. NM_001256876.1. [Q14678-1]
NP_001243806.1. NM_001256877.1. [Q14678-1]
NP_055973.2. NM_015158.3. [Q14678-1]
XP_006716807.1. XM_006716744.1. [Q14678-1]
UniGeneiHs.306764.

Genome annotation databases

EnsembliENST00000382293; ENSP00000371730; ENSG00000107104. [Q14678-2]
ENST00000382297; ENSP00000371734; ENSG00000107104. [Q14678-1]
ENST00000382303; ENSP00000371740; ENSG00000107104. [Q14678-1]
GeneIDi23189.
KEGGihsa:23189.
UCSCiuc003zgl.2. human. [Q14678-1]

Polymorphism databases

DMDMi73920184.

Keywords - Coding sequence diversityi

Alternative promoter usage, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34976.1. [Q14678-1 ]
CCDS6441.1. [Q14678-2 ]
RefSeqi NP_001243805.1. NM_001256876.1. [Q14678-1 ]
NP_001243806.1. NM_001256877.1. [Q14678-1 ]
NP_055973.2. NM_015158.3. [Q14678-1 ]
XP_006716807.1. XM_006716744.1. [Q14678-1 ]
UniGenei Hs.306764.

3D structure databases

ProteinModelPortali Q14678.
SMRi Q14678. Positions 1084-1325.
ModBasei Search...

Protein-protein interaction databases

BioGridi 116798. 3 interactions.
DIPi DIP-56491N.
IntActi Q14678. 14 interactions.
MINTi MINT-7997401.
STRINGi 9606.ENSP00000371734.

PTM databases

PhosphoSitei Q14678.

Polymorphism databases

DMDMi 73920184.

Proteomic databases

MaxQBi Q14678.
PaxDbi Q14678.
PRIDEi Q14678.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000382293 ; ENSP00000371730 ; ENSG00000107104 . [Q14678-2 ]
ENST00000382297 ; ENSP00000371734 ; ENSG00000107104 . [Q14678-1 ]
ENST00000382303 ; ENSP00000371740 ; ENSG00000107104 . [Q14678-1 ]
GeneIDi 23189.
KEGGi hsa:23189.
UCSCi uc003zgl.2. human. [Q14678-1 ]

Organism-specific databases

CTDi 23189.
GeneCardsi GC09P000461.
HGNCi HGNC:19309. KANK1.
HPAi HPA005539.
MIMi 607704. gene.
612900. phenotype.
neXtProti NX_Q14678.
Orphaneti 91498. Familial congenital palsy of trochlear nerve.
210141. Inherited congenital spastic tetraplegia.
PharmGKBi PA162392554.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOGENOMi HOG000230897.
HOVERGENi HBG050511.
InParanoidi Q14678.
OMAi MTGLDHY.
OrthoDBi EOG7NW687.
PhylomeDBi Q14678.
TreeFami TF324499.

Miscellaneous databases

ChiTaRSi KANK1. human.
GeneWikii ANKRD15.
GenomeRNAii 23189.
NextBioi 44663.
PROi Q14678.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14678.
Bgeei Q14678.
CleanExi HS_KANK1.
Genevestigatori Q14678.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR021939. KN_motif.
[Graphical view ]
Pfami PF00023. Ank. 3 hits.
PF12075. KN_motif. 1 hit.
[Graphical view ]
SMARTi SM00248. ANK. 6 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKANK1_HUMAN
AccessioniPrimary (citable) accession number: Q14678
Secondary accession number(s): A2A2W8
, D3DRH3, Q5W0W0, Q8IY65, Q8WX74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: August 30, 2005
Last modified: September 3, 2014
This is version 120 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

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