KIZ_BOVIN
ID KIZ_BOVIN Reviewed; 727 AA.
AC A0JNH1;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Centrosomal protein kizuna;
DE AltName: Full=Polo-like kinase 1 substrate 1;
GN Name=KIZ; Synonyms=PLK1S1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Centrosomal protein required for establishing a robust
CC mitotic centrosome architecture that can endure the forces that
CC converge on the centrosomes during spindle formation. Required for
CC stabilizing the expanded pericentriolar material around the centriole
CC (By similarity). {ECO:0000250|UniProtKB:Q2M2Z5}.
CC -!- SUBUNIT: Interacts with AKAP9, CEP72, ODF2, PCNT and TUBGCP2.
CC {ECO:0000250|UniProtKB:Q2M2Z5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q2M2Z5}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q2M2Z5}.
CC Note=Localizes to centrosomes throughout the cell cycle. After
CC centrosome duplication, it usually remains associated only with the
CC mother centrosome, containing the older mature centriole and particles
CC surrounding it. During prophase, additional particles accumulate around
CC both separating centrosomes. Does not accumulate at the microtubule
CC minus ends, but instead localizes to the centrosomes and
CC centrosome- surrounding area in a microtubule-independent and dependent
CC manner, respectively. {ECO:0000250|UniProtKB:Q2M2Z5}.
CC -!- PTM: Phosphorylation at Thr-387 by PLK1 is not needed for centrosomal
CC localization or pericentriolar material expansion but is indispensable
CC for spindle-pole stabilization. {ECO:0000250|UniProtKB:Q2M2Z5}.
CC -!- SIMILARITY: Belongs to the kizuna family. {ECO:0000305}.
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DR EMBL; BC126681; AAI26682.1; -; mRNA.
DR RefSeq; NP_001156930.1; NM_001163458.1.
DR AlphaFoldDB; A0JNH1; -.
DR SMR; A0JNH1; -.
DR STRING; 9913.ENSBTAP00000027949; -.
DR PaxDb; A0JNH1; -.
DR PRIDE; A0JNH1; -.
DR Ensembl; ENSBTAT00000027949; ENSBTAP00000027949; ENSBTAG00000020988.
DR GeneID; 513688; -.
DR KEGG; bta:513688; -.
DR CTD; 55857; -.
DR VEuPathDB; HostDB:ENSBTAG00000020988; -.
DR VGNC; VGNC:30620; KIZ.
DR eggNOG; ENOG502R72X; Eukaryota.
DR GeneTree; ENSGT00390000010121; -.
DR HOGENOM; CLU_026235_0_0_1; -.
DR InParanoid; A0JNH1; -.
DR OMA; ICESEKR; -.
DR OrthoDB; 573736at2759; -.
DR TreeFam; TF336086; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000020988; Expressed in spermatid and 108 other tissues.
DR ExpressionAtlas; A0JNH1; baseline and differential.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0007051; P:spindle organization; IBA:GO_Central.
DR InterPro; IPR026742; Centrosomal_kizuma.
DR PANTHER; PTHR16299; PTHR16299; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..727
FT /note="Centrosomal protein kizuna"
FT /id="PRO_0000381813"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 77..124
FT /evidence="ECO:0000255"
FT COMPBIAS 289..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M2Z5"
FT MOD_RES 387
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q2M2Z5"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M2Z5"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M2Z5"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M2Z5"
SQ SEQUENCE 727 AA; 80421 MW; 8ED4AB1740F790A5 CRC64;
MTERSGRGGG TRGASALPSP DYYEQVAHLQ QGLRNSEKKR LDLERKLYEY HQSDVCRAKL
KYIKLKKYLK EICESEKNAR IRNQEYLKQF ERIQANITAS LEKLQELKIE FETQIKKMQL
LSKDSLGKKG ELKDEDKEKV VMRAEINSGT AMSRGLYQPA TIFMGRQMSA VSGIGDFTTE
RKSPQPTKNF SIPDPHSHQQ TAQSSDVTGS RVVQTPGDTQ CLNKSDKIDG KTSLQIGEKT
PVTASALSEE EQTHCFEIGS NACQSKSNLS EGKKSAELHS PLWERLSPEN RTTDLKCDSS
RRSEGSEGEI LTREHIEVEE ERARPPVSPL SGSESCASEN ECPQEKPPAR KASSDHLPCE
DSQSQEPFRK KQEEQEEESL SSSSDLTVSV SEDDLILKSP ELQTNLGDTM EQEDGTETLN
VIHSEQERDA PSTGKPNCIL QAPSTPDSPN ESFTNLPAKE LCNHSDILRE GPDAYRTAVL
HQLSQLCPRG GSDKEQVRFE QTPASGLLRT RSGQHIAALK GHDTFVQEEE VAKLSGVFLV
SKLDQRTKAT ALLKKDLAEE HDNRLAVHSS KSSCSLPSTP SDESGIRNGK PTLWPKGVTT
REQEDESREE STEESMAARM PITETKAYQR LKQSALQGST HQAGDGFQEA TAPTSQPPGL
KTGSGTFKTK TTHKIASEAS FSSSEGSPLS RHENEGKLTT NLKSKAFWSE SDESNSEIEA
ALRPRTP
