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ZW10_RAT
ID   ZW10_RAT                Reviewed;         777 AA.
AC   Q4V8C2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Centromere/kinetochore protein zw10 homolog;
GN   Name=Zw10;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC       cells from prematurely exiting mitosis. Required for the assembly of
CC       the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its
CC       function related to the spindle assembly machinery is proposed to
CC       depend on its association in the mitotic RZZ complex. Involved in
CC       regulation of membrane traffic between the Golgi and the endoplasmic
CC       reticulum (ER); the function is proposed to depend on its association
CC       in the interphase NRZ complex which is believed to play a role in SNARE
CC       assembly at the ER (By similarity). {ECO:0000250|UniProtKB:O43264}.
CC   -!- SUBUNIT: Interacts with NBAS and KNTC1/ROD; the interactions are
CC       mutually exclusive and indicative for its association in two different
CC       vesicle tethering complexes (By similarity). Component of the RZZ
CC       complex composed of KNTC1/ROD, ZW10 and ZWILCH (By similarity).
CC       Component of the NRZ complex composed of NBAS, ZW10 and RINT1/TIP20L;
CC       NRZ associates with SNAREs STX18, USE1L, BNIP1/SEC20L and SEC22B (the
CC       assembly has been described as syntaxin 18 complex) (By similarity).
CC       Interacts directly with RINT1/TIP20L bound to BNIP1/SEC20L (By
CC       similarity). Interacts with C19orf25 and ZWINT (By similarity).
CC       Interacts with ZFYVE1 (By similarity). Interacts with RAB18 and this
CC       interaction is enhanced in the presence of ZFYVE1 (By similarity).
CC       {ECO:0000250|UniProtKB:O43264}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43264}.
CC       Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43264};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:O43264}. Chromosome,
CC       centromere, kinetochore {ECO:0000250|UniProtKB:O43264}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250|UniProtKB:O43264}. Lipid droplet
CC       {ECO:0000250|UniProtKB:O43264}. Note=Dynamic pattern of localization
CC       during the cell cycle. In most cells at interphase, present diffusely
CC       in the cytoplasm. In prometaphase, associated with the kinetochore. At
CC       metaphase, detected both at the kinetochores and, most prominently, at
CC       the spindle, particularly at the spindle poles. In very early anaphase,
CC       detected on segregating kinetochores. In late anaphase and telophase,
CC       accumulates at the spindle midzone. {ECO:0000250|UniProtKB:O43264}.
CC   -!- SIMILARITY: Belongs to the ZW10 family. {ECO:0000305}.
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DR   EMBL; BC097452; AAH97452.1; -; mRNA.
DR   RefSeq; NP_001019972.1; NM_001024801.1.
DR   AlphaFoldDB; Q4V8C2; -.
DR   SMR; Q4V8C2; -.
DR   STRING; 10116.ENSRNOP00000010595; -.
DR   iPTMnet; Q4V8C2; -.
DR   PhosphoSitePlus; Q4V8C2; -.
DR   jPOST; Q4V8C2; -.
DR   PaxDb; Q4V8C2; -.
DR   PRIDE; Q4V8C2; -.
DR   Ensembl; ENSRNOT00000080712; ENSRNOP00000071533; ENSRNOG00000054479.
DR   GeneID; 363059; -.
DR   KEGG; rno:363059; -.
DR   UCSC; RGD:1309197; rat.
DR   CTD; 9183; -.
DR   RGD; 1309197; Zw10.
DR   eggNOG; KOG2163; Eukaryota.
DR   GeneTree; ENSGT00390000016427; -.
DR   HOGENOM; CLU_012948_0_0_1; -.
DR   InParanoid; Q4V8C2; -.
DR   OMA; LMMILQA; -.
DR   OrthoDB; 422807at2759; -.
DR   PhylomeDB; Q4V8C2; -.
DR   TreeFam; TF105966; -.
DR   Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-RNO-68877; Mitotic Prometaphase.
DR   Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR   PRO; PR:Q4V8C2; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000054479; Expressed in testis and 20 other tissues.
DR   Genevisible; Q4V8C2; RN.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0070939; C:Dsl1/NZR complex; ISO:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000776; C:kinetochore; ISS:HGNC-UCL.
DR   GO; GO:0005828; C:kinetochore microtubule; ISS:HGNC-UCL.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR   GO; GO:1990423; C:RZZ complex; ISO:RGD.
DR   GO; GO:0000922; C:spindle pole; ISS:HGNC-UCL.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:HGNC-UCL.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:RGD.
DR   GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:HGNC-UCL.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:HGNC-UCL.
DR   GO; GO:0034501; P:protein localization to kinetochore; ISO:RGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISS:HGNC-UCL.
DR   GO; GO:0007096; P:regulation of exit from mitosis; ISS:HGNC-UCL.
DR   Gene3D; 1.10.357.150; -; 1.
DR   InterPro; IPR009361; RZZ-complex_Zw10.
DR   InterPro; IPR046362; Zw10/DSL1_C_sf.
DR   Pfam; PF06248; Zw10; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW   ER-Golgi transport; Kinetochore; Lipid droplet; Membrane; Mitosis;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   CHAIN           2..777
FT                   /note="Centromere/kinetochore protein zw10 homolog"
FT                   /id="PRO_0000184959"
FT   REGION          2..316
FT                   /note="Interaction with RINT1"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   REGION          2..81
FT                   /note="Interaction with ZWINT"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   COILED          14..130
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   MOD_RES         775
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
SQ   SEQUENCE   777 AA;  87967 MW;  C56BB79891D4C691 CRC64;
     MASFVTEVLA HSGSLEKEDL GTRISRLTRR VEEIKGEVCN MISKKYSEFL PTMQSAQALV
     TQVDTLSNDI DQLKSRIETE VCRDLHISTV EFTNLKQRLE RDSVVLNLLK QLQEFSSAIE
     EYNSALAEKK YIPAARLLEE AQECLKLLKS KKCFDLKMLK SLSMELTVQK QNILYHLGED
     WQKLVVWKFP PSKDTSSLES CLQTELHLCT EQPEKEMTPL PSISSVLLAF SILGELPTKL
     KSFGQMLLKY ILKPLVTCPS LHAVIERQPN SVSICFQSLA TDSEHPPPPE AFAKIQLVLE
     VLQKQLLDLP LDADLEIGKV PEIVLAEMLG EVIWEDLSDC LIRNCLVYSI PTNSSKLQQY
     EEIIQSTEEF EKSLKEMRFL KGDTTDLLKY ARNINSHFAN KKCQDVIVAA RHLMTSEIHN
     TVKIGPDCEE TLPDLPSPDA DHRLQVQVCK VQFTDAGNLE PETSLDPRSF SLPTCRISEA
     VKKLMELAYQ TLLEATTSSD QCAVQLFYSV RNIFHLFHDV VPTYHKENLQ KLPQLAAIHH
     NNCMYIAHHL LTLGHQFRSR LTPILCDGTT TFVDLVPGFR RLGTECFLAQ MRTQKGELLE
     RLSSARSFAN MDDEENYSAA SKAVRQVLHQ LKRLGIVWQD VLPVNIYCKA MGTLLNTVIA
     EMIGRITALE DISTEDGDRL YSLCKTVMDE GPQVFAPLSD ENKNKKYQEE VPVYVSKWMP
     FKELMIMLQA SLQEIGDRWA DGKGPLATAF PSSEVKALIR ALFQNTERRA AALAKIK
 
 
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