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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

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.4 Publications

GO - Molecular functioni

  1. beta-catenin binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of actin filament polymerization Source: UniProtKB
  2. negative regulation of cell migration Source: UniProtKB
  3. negative regulation of insulin receptor signaling pathway Source: UniProtKB
  4. negative regulation of lamellipodium morphogenesis Source: UniProtKB
  5. negative regulation of neuron projection development Source: UniProtKB
  6. negative regulation of Rho protein signal transduction 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 catenin import into nucleus Source: UniProtKB
  10. positive regulation of Wnt signaling pathway 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 2 Publications
Note: Colocalizes with KIF21A in membrane ruffles.
Isoform 1 : Cytoplasm. Nucleus
Note: Shuttles between the cytoplasm and nucleus.
Isoform 2 : Cytoplasm. Nucleus. Cell projectionruffle membrane
Note: Shuttles between the cytoplasm and nucleus.

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

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. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

MIMi612900. phenotype.
Orphaneti210141. Inherited congenital spastic tetraplegia.
PharmGKBiPA162392554.

PTM / Processingi

Molecule processing

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

BgeeiQ14678.
CleanExiHS_KANK1.
ExpressionAtlasiQ14678. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1161 – 119131ANK 1Add
BLAST
Repeati1195 – 122834ANK 2Add
BLAST
Repeati1233 – 126230ANK 3Add
BLAST
Repeati1266 – 129833ANK 4Add
BLAST
Repeati1300 – 132930ANK 5Add
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 KIF21AAdd
BLAST
Regioni613 – 62210Nuclear export signal 3 (NES 3)
Regioni979 – 99214Nuclear localization signal 2 (NLS 2)Add
BLAST
Regioni1156 – 1308153Interaction with KIF21AAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili258 – 31659Sequence AnalysisAdd
BLAST
Coiled coili361 – 39535Sequence AnalysisAdd
BLAST
Coiled coili446 – 50055Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 5 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00530000063448.
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

        10         20         30         40         50
MAHTTKVNGS ASGKAGDILS GDQDKEQKDP YFVETPYGYQ LDLDFLKYVD
60 70 80 90 100
DIQKGNTIKR LNIQKRRKPS VPCPEPRTTS GQQGIWTSTE SLSSSNSDDN
110 120 130 140 150
KQCPNFLIAR SQVTSTPISK PPPPLETSLP FLTIPENRQL PPPSPQLPKH
160 170 180 190 200
NLHVTKTLME TRRRLEQERA TMQMTPGEFR RPRLASFGGM GTTSSLPSFV
210 220 230 240 250
GSGNHNPAKH QLQNGYQGNG DYGSYAPAAP TTSSMGSSIR HSPLSSGIST
260 270 280 290 300
PVTNVSPMHL QHIREQMAIA LKRLKELEEQ VRTIPVLQVK ISVLQEEKRQ
310 320 330 340 350
LVSQLKNQRA ASQINVCGVR KRSYSAGNAS QLEQLSRARR SGGELYIDYE
360 370 380 390 400
EEEMETVEQS TQRIKEFRQL TADMQALEQK IQDSSCEASS ELRENGECRS
410 420 430 440 450
VAVGAEENMN DIVVYHRGSR SCKDAAVGTL VEMRNCGVSV TEAMLGVMTE
460 470 480 490 500
ADKEIELQQQ TIESLKEKIY RLEVQLRETT HDREMTKLKQ ELQAAGSRKK
510 520 530 540 550
VDKATMAQPL VFSKVVEAVV QTRDQMVGSH MDLVDTCVGT SVETNSVGIS
560 570 580 590 600
CQPECKNKVV GPELPMNWWI VKERVEMHDR CAGRSVEMCD KSVSVEVSVC
610 620 630 640 650
ETGSNTEESV NDLTLLKTNL NLKEVRSIGC GDCSVDVTVC SPKECASRGV
660 670 680 690 700
NTEAVSQVEA AVMAVPRTAD QDTSTDLEQV HQFTNTETAT LIESCTNTCL
710 720 730 740 750
STLDKQTSTQ TVETRTVAVG EGRVKDINSS TKTRSIGVGT LLSGHSGFDR
760 770 780 790 800
PSAVKTKESG VGQININDNY LVGLKMRTIA CGPPQLTVGL TASRRSVGVG
810 820 830 840 850
DDPVGESLEN PQPQAPLGMM TGLDHYIERI QKLLAEQQTL LAENYSELAE
860 870 880 890 900
AFGEPHSQMG SLNSQLISTL SSINSVMKSA STEELRNPDF QKTSLGKITG
910 920 930 940 950
NYLGYTCKCG GLQSGSPLSS QTSQPEQEVG TSEGKPISSL DAFPTQEGTL
960 970 980 990 1000
SPVNLTDDQI AAGLYACTNN ESTLKSIMKK KDGNKDSNGA KKNLQFVGIN
1010 1020 1030 1040 1050
GGYETTSSDD SSSDESSSSE SDDECDVIEY PLEEEEEEED EDTRGMAEGH
1060 1070 1080 1090 1100
HAVNIEGLKS ARVEDEMQVQ ECEPEKVEIR ERYELSEKML SACNLLKNTI
1110 1120 1130 1140 1150
NDPKALTSKD MRFCLNTLQH EWFRVSSQKS AIPAMVGDYI AAFEAISPDV
1160 1170 1180 1190 1200
LRYVINLADG NGNTALHYSV SHSNFEIVKL LLDADVCNVD HQNKAGYTPI
1210 1220 1230 1240 1250
MLAALAAVEA EKDMRIVEEL FGCGDVNAKA SQAGQTALML AVSHGRIDMV
1260 1270 1280 1290 1300
KGLLACGADV NIQDDEGSTA LMCASEHGHV EIVKLLLAQP GCNGHLEDND
1310 1320 1330 1340 1350
GSTALSIALE AGHKDIAVLL YAHVNFAKAQ SPGTPRLGRK TSPGPTHRGS

FD
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. CuratedVSP_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]
ENST00000619269; ENSP00000477725; 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...
MobiDBi 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 ]
ENST00000619269 ; ENSP00000477725 ; ENSG00000107104 . [Q14678-1 ]
GeneIDi 23189.
KEGGi hsa:23189.
UCSCi uc003zgl.2. human. [Q14678-1 ]

Organism-specific databases

CTDi 23189.
GeneCardsi GC09P000474.
HGNCi HGNC:19309. KANK1.
HPAi HPA005539.
MIMi 607704. gene.
612900. phenotype.
neXtProti NX_Q14678.
Orphaneti 210141. Inherited congenital spastic tetraplegia.
PharmGKBi PA162392554.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00530000063448.
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

Bgeei Q14678.
CleanExi HS_KANK1.
ExpressionAtlasi Q14678. baseline and differential.
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: October 29, 2014
This is version 122 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

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