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Protein

Centrosomal protein kizuna

Gene

KIZ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Centrosomal protein required for establishing a robust mitotic centrosome architecture that can endure the forces that converge on the centrosomes during spindle formation. Required for stabilizing the expanded pericentriolar material around the centriole.1 Publication

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • spindle organization Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

SIGNORiQ2M2Z5.

Names & Taxonomyi

Protein namesi
Recommended name:
Centrosomal protein kizuna
Alternative name(s):
Polo-like kinase 1 substrate 1
Gene namesi
Name:KIZ
Synonyms:C20orf19, NCRNA00153, PLK1S1
ORF Names:HT013
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15865. KIZ.

Subcellular locationi

GO - Cellular componenti

  • cell projection Source: UniProtKB-KW
  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 69 (RP69)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
See also OMIM:615780

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi249 – 2491T → A: Does not affect phosphorylation status. 1 Publication
Mutagenesisi379 – 3791T → A: Abolishes phosphorylation by PLK1. 1 Publication
Mutagenesisi379 – 3791T → E: Phosphomimetic mutant able to partially restore focused bipolar spindles to PLK1-depleted cells that otherwise possess aberrant spindles with diffuse or multiple gamma-tubulin signals. 1 Publication

Keywords - Diseasei

Retinitis pigmentosa

Organism-specific databases

MalaCardsiKIZ.
MIMi615780. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA165392491.

Polymorphism and mutation databases

BioMutaiPLK1S1.
DMDMi257051030.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 673673Centrosomal protein kizunaPRO_0000301851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei317 – 3171PhosphoserineCombined sources
Modified residuei321 – 3211PhosphoserineCombined sources
Modified residuei379 – 3791Phosphothreonine; by PLK11 Publication
Modified residuei647 – 6471PhosphoserineCombined sources
Modified residuei650 – 6501PhosphoserineCombined sources
Modified residuei652 – 6521PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation at Thr-379 by PLK1 is not needed for centrosomal localization or pericentriolar material expansion but is indispensable for spindle-pole stabilization.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ2M2Z5.
MaxQBiQ2M2Z5.
PeptideAtlasiQ2M2Z5.
PRIDEiQ2M2Z5.

PTM databases

iPTMnetiQ2M2Z5.
PhosphoSiteiQ2M2Z5.

Expressioni

Gene expression databases

CleanExiHS_NCRNA00153.
ExpressionAtlasiQ2M2Z5. baseline and differential.
GenevisibleiQ2M2Z5. HS.

Interactioni

Subunit structurei

Interacts with AKAP9, CEP72, ODF2, PCNT and TUBGCP2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP72Q9P2093EBI-2554344,EBI-739498
MEOX2A4D1273EBI-2554344,EBI-10172134
TACC3Q9Y6A53EBI-2554344,EBI-2554984

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120959. 11 interactions.
IntActiQ2M2Z5. 7 interactions.
MINTiMINT-7298019.

Structurei

3D structure databases

ProteinModelPortaliQ2M2Z5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the kizuna family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000010121.
InParanoidiQ2M2Z5.
KOiK16539.
OMAiQPATIFM.
PhylomeDBiQ2M2Z5.

Family and domain databases

InterProiIPR026742. Centrosomal_kizuma.
[Graphical view]
PANTHERiPTHR16299. PTHR16299. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q2M2Z5-1) [UniParc]FASTAAdd to basket

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
MSRTLASAVP LSSPDYYERL GQLQHGLRDS EKKRLDLEKK LYEYNQSDTC
60 70 80 90 100
RVKLKYVKLK NYLKEICESE KKAHTRNQEY LKRFERVQAH VVHFTTNTEK
110 120 130 140 150
LQKLKLEYET QIKKMLCSKD SLGLKEELTD EDREKVAVHE GINSGTAMSR
160 170 180 190 200
GLYQPATIFM GRQMSAILSM RDFSTEHKSP QPTKNFSIPD PHSHRQTAQS
210 220 230 240 250
SNVTDSCVVQ TSNDTQCLNK SDNIDGKASL QIGEKMPVTA SVLSEEEQTH
260 270 280 290 300
CLEIGSNTRH GKSNLSEGKK SAELNSPLRE RLSPENRTTD LKCDSSSGSE
310 320 330 340 350
GEILTREHIE VEEKRASPPV SPIPVSEYCE SENKWSQEKH SPWEGVSDHL
360 370 380 390 400
AHREPKSQKP FRKMQEEEEE SWSTSSDLTI SISEDDLILE SPEPQPNPGG
410 420 430 440 450
KMEGEDGIEA LKLIHAEQER VALSTEKNCI LQTLSSPDSE KESSTNAPTR
460 470 480 490 500
EPGQTPDSDV PRAQVGQHVA TLKEHDNSVK EEATALLRKA LTEECGRRSA
510 520 530 540 550
IHSSESSCSL PSILNDNSGI KEAKPAVWLN SVPTREQEVS SGCGDKSKKE
560 570 580 590 600
NVAADIPITE TEAYQLLKKA TLQDNTNQTE NRFQKTDASV SHLSGLNIGS
610 620 630 640 650
GAFETKTANK IASEASFSSS EGSPLSRHEN KKKPVINLKS NALWDESDDS
660 670
NSEIEAALRP RNHNTDDSDD FYD
Length:673
Mass (Da):75,111
Last modified:September 1, 2009 - v2
Checksum:i3B6BDE3A479B5933
GO
Isoform 2 (identifier: Q2M2Z5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-103: Missing.
     104-105: LK → MQ

Show »
Length:570
Mass (Da):62,798
Checksum:i24F593D7ECCA4BF3
GO
Isoform 3 (identifier: Q2M2Z5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     628-673: Missing.

Note: No experimental confirmation available.
Show »
Length:627
Mass (Da):69,784
Checksum:i10CB283429F7D3B7
GO
Isoform 4 (identifier: Q2M2Z5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     642-673: ALWDESDDSNSEIEAALRPRNHNTDDSDDFYD → GERDNRTLDFLFLF

Show »
Length:655
Mass (Da):73,140
Checksum:i469FCB81E188B615
GO
Isoform 5 (identifier: Q2M2Z5-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     134-135: EK → MQ

Note: No experimental confirmation available.
Show »
Length:540
Mass (Da):59,243
Checksum:i519B65A4F1D63402
GO

Sequence cautioni

The sequence AAF67652.1 differs from that shown. Reason: Frameshift at position 283. Curated
The sequence AAH39296.1 differs from that shown. Reason: Frameshift at position 279. Curated
The sequence AAP97689.1 differs from that shown. Reason: Frameshift at position 198. Curated
The sequence BAG59066.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti369 – 3691E → G in AAF67652 (PubMed:15489334).Curated
Sequence conflicti573 – 5731Q → R in BAG56710 (PubMed:14702039).Curated
Sequence conflicti594 – 5941S → L in BAG59066 (PubMed:14702039).Curated
Sequence conflicti642 – 67231ALWDE…SDDFY → GERDNRTLDFLFLF in BAG59066 (PubMed:14702039).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti139 – 1391H → Q.2 Publications
Corresponds to variant rs4815025 [ dbSNP | Ensembl ].
VAR_034909
Natural varianti236 – 2361M → T.3 Publications
Corresponds to variant rs2236178 [ dbSNP | Ensembl ].
VAR_034910

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 133133Missing in isoform 5. 1 PublicationVSP_037837Add
BLAST
Alternative sequencei1 – 103103Missing in isoform 2. 1 PublicationVSP_027879Add
BLAST
Alternative sequencei104 – 1052LK → MQ in isoform 2. 1 PublicationVSP_027880
Alternative sequencei134 – 1352EK → MQ in isoform 5. 1 PublicationVSP_037838
Alternative sequencei628 – 67346Missing in isoform 3. 1 PublicationVSP_027881Add
BLAST
Alternative sequencei642 – 67332ALWDE…DDFYD → GERDNRTLDFLFLF in isoform 4. 2 PublicationsVSP_027882Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK293166 mRNA. Translation: BAG56710.1.
AK296399 mRNA. Translation: BAG59066.1. Different initiation.
AF451990 mRNA. Translation: AAP97689.1. Frameshift.
AL110120 Genomic DNA. No translation available.
AL117332 Genomic DNA. No translation available.
AL121759 Genomic DNA. No translation available.
CH471133 Genomic DNA. Translation: EAX10188.1.
BC039296 mRNA. Translation: AAH39296.1. Frameshift.
BC045826 mRNA. Translation: AAH45826.1.
BC065550 mRNA. Translation: AAH65550.1.
BC090879 mRNA. Translation: AAH90879.2.
BC105093 mRNA. Translation: AAI05094.1.
BC113370 mRNA. Translation: AAI13371.1.
AF220187 mRNA. Translation: AAF67652.1. Frameshift.
CCDSiCCDS74706.1. [Q2M2Z5-1]
CCDS74707.1. [Q2M2Z5-2]
CCDS74708.1. [Q2M2Z5-5]
RefSeqiNP_001156494.1. NM_001163022.1. [Q2M2Z5-2]
NP_001156495.1. NM_001163023.1. [Q2M2Z5-5]
NP_001263318.1. NM_001276389.1.
NP_060944.3. NM_018474.4. [Q2M2Z5-1]
UniGeneiHs.187635.

Genome annotation databases

EnsembliENST00000616848; ENSP00000480612; ENSG00000088970. [Q2M2Z5-5]
ENST00000619189; ENSP00000479542; ENSG00000088970. [Q2M2Z5-1]
ENST00000620891; ENSP00000478019; ENSG00000088970. [Q2M2Z5-2]
GeneIDi55857.
KEGGihsa:55857.
UCSCiuc032pdl.2. human. [Q2M2Z5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK293166 mRNA. Translation: BAG56710.1.
AK296399 mRNA. Translation: BAG59066.1. Different initiation.
AF451990 mRNA. Translation: AAP97689.1. Frameshift.
AL110120 Genomic DNA. No translation available.
AL117332 Genomic DNA. No translation available.
AL121759 Genomic DNA. No translation available.
CH471133 Genomic DNA. Translation: EAX10188.1.
BC039296 mRNA. Translation: AAH39296.1. Frameshift.
BC045826 mRNA. Translation: AAH45826.1.
BC065550 mRNA. Translation: AAH65550.1.
BC090879 mRNA. Translation: AAH90879.2.
BC105093 mRNA. Translation: AAI05094.1.
BC113370 mRNA. Translation: AAI13371.1.
AF220187 mRNA. Translation: AAF67652.1. Frameshift.
CCDSiCCDS74706.1. [Q2M2Z5-1]
CCDS74707.1. [Q2M2Z5-2]
CCDS74708.1. [Q2M2Z5-5]
RefSeqiNP_001156494.1. NM_001163022.1. [Q2M2Z5-2]
NP_001156495.1. NM_001163023.1. [Q2M2Z5-5]
NP_001263318.1. NM_001276389.1.
NP_060944.3. NM_018474.4. [Q2M2Z5-1]
UniGeneiHs.187635.

3D structure databases

ProteinModelPortaliQ2M2Z5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120959. 11 interactions.
IntActiQ2M2Z5. 7 interactions.
MINTiMINT-7298019.

PTM databases

iPTMnetiQ2M2Z5.
PhosphoSiteiQ2M2Z5.

Polymorphism and mutation databases

BioMutaiPLK1S1.
DMDMi257051030.

Proteomic databases

EPDiQ2M2Z5.
MaxQBiQ2M2Z5.
PeptideAtlasiQ2M2Z5.
PRIDEiQ2M2Z5.

Protocols and materials databases

DNASUi55857.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000616848; ENSP00000480612; ENSG00000088970. [Q2M2Z5-5]
ENST00000619189; ENSP00000479542; ENSG00000088970. [Q2M2Z5-1]
ENST00000620891; ENSP00000478019; ENSG00000088970. [Q2M2Z5-2]
GeneIDi55857.
KEGGihsa:55857.
UCSCiuc032pdl.2. human. [Q2M2Z5-1]

Organism-specific databases

CTDi55857.
GeneCardsiKIZ.
H-InvDBHIX0015682.
HGNCiHGNC:15865. KIZ.
MalaCardsiKIZ.
MIMi615757. gene.
615780. phenotype.
neXtProtiNX_Q2M2Z5.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA165392491.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000010121.
InParanoidiQ2M2Z5.
KOiK16539.
OMAiQPATIFM.
PhylomeDBiQ2M2Z5.

Enzyme and pathway databases

SIGNORiQ2M2Z5.

Miscellaneous databases

GenomeRNAii55857.
PROiQ2M2Z5.
SOURCEiSearch...

Gene expression databases

CleanExiHS_NCRNA00153.
ExpressionAtlasiQ2M2Z5. baseline and differential.
GenevisibleiQ2M2Z5. HS.

Family and domain databases

InterProiIPR026742. Centrosomal_kizuma.
[Graphical view]
PANTHERiPTHR16299. PTHR16299. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-672 (ISOFORM 4), VARIANT THR-236.
    Tissue: Neuroblastoma and Thalamus.
  2. Guo J.H., Yu L.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Hypothalamus.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLN-139 AND THR-236.
  5. "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] (ISOFORMS 1; 2 AND 3), VARIANTS GLN-139 AND THR-236.
    Tissue: Hippocampus, Pituitary and Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 280-673 (ISOFORMS 1/2).
    Tissue: Hypothalamus.
  7. "The Plk1 target Kizuna stabilizes mitotic centrosomes to ensure spindle bipolarity."
    Oshimori N., Ohsugi M., Yamamoto T.
    Nat. Cell Biol. 8:1095-1101(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-379, MUTAGENESIS OF THR-249 AND THR-379, INTERACTION WITH AKAP9; ODF2; PCNT AND TUBGCP2.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; SER-321; SER-647; SER-650 AND SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Cep72 regulates the localization of key centrosomal proteins and proper bipolar spindle formation."
    Oshimori N., Li X., Ohsugi M., Yamamoto T.
    EMBO J. 28:2066-2076(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEP72.
  10. Cited for: SUBCELLULAR LOCATION, INVOLVEMENT IN RP69.

Entry informationi

Entry nameiKIZ_HUMAN
AccessioniPrimary (citable) accession number: Q2M2Z5
Secondary accession number(s): B4DDE9
, B4DK54, Q4G0M8, Q4G0S5, Q5BKY3, Q6P0M6, Q71ME0, Q9NZ35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 1, 2009
Last modified: July 6, 2016
This is version 83 of the entry and version 2 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

Miscellaneous

Kizuna means 'bonds' in Japanese.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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

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.