INCEB_XENLA
ID INCEB_XENLA Reviewed; 892 AA.
AC Q32N93;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Inner centromere protein B;
GN Name=incenp-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the chromosomal passenger complex (CPC), a
CC complex that acts as a key regulator of mitosis. The CPC complex has
CC essential functions at the centromere in ensuring correct chromosome
CC alignment and segregation and is required for chromatin-induced
CC microtubule stabilization and spindle assembly. Acts as a scaffold
CC regulating CPC localization and activity. The C-terminus associates
CC with aurkb/aurora-B, the N-terminus associated with cdca8/borealin
CC and/or cdca9/dasra-A tethers the CPC to the inner centromere, and the
CC microtubule binding activity within the central SAH domain directs
CC aurkb/aurora-B toward substrates near microtubules. Activates aurkb.
CC {ECO:0000250|UniProtKB:O13024, ECO:0000250|UniProtKB:P53352}.
CC -!- SUBUNIT: Component of the CPC at least composed of survivin/birc5,
CC incenp, cdca8/borealin and/or cdca9/dasra-A, and aurkb/aurora-B.
CC Interacts (via C-terminus) with aurkb (via N-terminus and kinase
CC domain). Interacts (via N-terminus) with birc5.1, birc5.2, cdca8 and
CC cdca9. Interacts with mtus1 (By similarity).
CC {ECO:0000250|UniProtKB:O13024, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NQS7}.
CC Chromosome {ECO:0000250|UniProtKB:O13024}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:O13024}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:O13024}. Midbody {ECO:0000250|UniProtKB:Q9NQS7}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9NQS7}.
CC Note=Localizes on chromosome arms and inner centromeres from prophase
CC through metaphase and then transferring to the spindle midzone and
CC midbody from anaphase through cytokinesis. Colocalizes to the
CC equatorial cell cortex at anaphase. Colocalizes with AURKB at mitotic
CC chromosomes. {ECO:0000250|UniProtKB:O13024}.
CC -!- DOMAIN: The INbox mediates interaction with aurkb/aurora-B.
CC {ECO:0000250|UniProtKB:O13024}.
CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high
CC content of charged residues which are predicted to stabilize the alpha-
CC helical structure by ionic bonds. It can refold after extension
CC suggesting an in vivo force-dependent function. The isolated SAH domain
CC is monomeric. {ECO:0000250|UniProtKB:P53352}.
CC -!- SIMILARITY: Belongs to the INCENP family. {ECO:0000305}.
CC -!- CAUTION: Originally predicted to contain a coiled coil domain but shown
CC to contain a stable SAH domain instead. {ECO:0000250|UniProtKB:P53352}.
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DR EMBL; BC108767; AAI08768.1; -; mRNA.
DR RefSeq; NP_001131043.1; NM_001137571.1.
DR AlphaFoldDB; Q32N93; -.
DR SMR; Q32N93; -.
DR PRIDE; Q32N93; -.
DR DNASU; 398822; -.
DR GeneID; 398822; -.
DR KEGG; xla:398822; -.
DR CTD; 398822; -.
DR Xenbase; XB-GENE-990404; incenp.S.
DR OrthoDB; 671886at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 398822; Expressed in egg cell and 18 other tissues.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0032133; C:chromosome passenger complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:InterPro.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IEA:InterPro.
DR GO; GO:0051225; P:spindle assembly; ISS:UniProtKB.
DR InterPro; IPR039130; INCENP.
DR InterPro; IPR022006; INCENP_N.
DR InterPro; IPR005635; Inner_centromere_prot_ARK-bd.
DR PANTHER; PTHR13142; PTHR13142; 1.
DR Pfam; PF03941; INCENP_ARK-bind; 1.
DR Pfam; PF12178; INCENP_N; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..892
FT /note="Inner centromere protein B"
FT /id="PRO_0000278830"
FT REGION 50..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..725
FT /note="SAH"
FT /evidence="ECO:0000250|UniProtKB:P53352"
FT REGION 569..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..876
FT /note="IN box"
FT /evidence="ECO:0000305"
FT COMPBIAS 68..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 870
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 892 AA; 102938 MW; 3813377C40DD6C04 CRC64;
MNDAECLSHL LQVCSRKTEE FVRTLDTKHM VWLLEIEEEA RKMFSSDFNA EPELMPKTPS
QKRRRKKRTS ILPDENRDPS GRRISRRRSS ANWSSSVRRL SVRNQIKAND DSIQEGPAQP
KRMTRARAQA SIMCPPAVEQ ALPESPSQLC QKSVQVKISE HERRSAEQKL RESEIEDSEM
KTDVQPIPEI TKDHISEIMN AAGPPPIPDI PAVPVTPENK SRAAGKLKIS GSSTPIQTAA
VVDLTCESPR PANELVNEQP LNLSNESATP TGSKSDRRSV RRSLVVRKSS SRRASLVSQF
SLVSKRESMT REAVRKSIRQ SISKKKAAME TSSTSSQRSC HSSIEMVDDE ITIKIRPETA
PSETVSEEAP AAESPRSSLR SRAFKKIAIS NLSESEEPPR RVTRQMVAVD AEPTPETADD
AQNNRRKSYK RAVDELSDDE RPSEGECSPP RKKTPSPPCP PSKIVKPPPH MKSFLHTVQK
NQFLMMTPGS IGKNITLKSF IKRNTPLKPD PKSEEKERQR LDALRKKEEA ELQRKQKIEE
GKKRKQEELK LRREDRLRKV LQARERVEQL EEEKKKKFEQ KFAQIDEKSE KVREDRMAEE
KAKKKTMVKK QEEVECRRKQ EEEARKLKAK QMEEEERRHQ ELLQKKREEE EMERQKKMAE
AKRLAEQERE RQVFAEKERL RAERERERIE REKALQLQRE LERAAQEKEQ QRREAEERKK
REQQQRLEQE RLERLRTEQE VKRLQEEQQR KAKEQAAAAA APVMNVTVDM QNSPACESYE
MTPKSYKVPS VKANADNYGM DLNSDDSTDD ESQPRKPIPA WASGNLLAQA VSQQYYKPID
ADHMYGTIDS PKLEELFNKS KPRYFKRTSS AVWHSPPLSN RHHLAVGYGL KY
