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KF22B_XENLA
ID   KF22B_XENLA             Reviewed;         650 AA.
AC   Q7ZYL5; Q6GPG0; Q9I9A8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Kinesin-like protein KIF22-B;
DE   AltName: Full=Chromokinesin kid-B;
DE            Short=Xkid-B;
GN   Name=kif22-b; Synonyms=kid-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 [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=10966105; DOI=10.1016/s0092-8674(00)00048-9;
RA   Antonio C., Ferby I., Wilhelm H., Jones M., Karsenti E., Nebreda A.R.,
RA   Vernos I.;
RT   "Xkid, a chromokinesin required for chromosome alignment on the metaphase
RT   plate.";
RL   Cell 102:425-435(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Kinesin family member that is involved in spindle formation
CC       and the movements of chromosomes during mitosis and meiosis. Binds to
CC       microtubules and to DNA. {ECO:0000250|UniProtKB:Q9I869}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9I869}.
CC       Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- PTM: Ubiquitinated, leading to its subsequent proteasomal degradation.
CC       {ECO:0000250|UniProtKB:Q9I869}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH73177.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ249841; CAB71799.1; -; mRNA.
DR   EMBL; BC043733; AAH43733.1; -; mRNA.
DR   EMBL; BC073177; AAH73177.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001165449.1; NM_001171978.1.
DR   AlphaFoldDB; Q7ZYL5; -.
DR   SMR; Q7ZYL5; -.
DR   BioGRID; 1078895; 3.
DR   IntAct; Q7ZYL5; 1.
DR   DNASU; 100337511; -.
DR   GeneID; 100337511; -.
DR   KEGG; xla:100337511; -.
DR   CTD; 100337511; -.
DR   Xenbase; XB-GENE-6464372; kif22.L.
DR   OrthoDB; 787964at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 100337511; Expressed in egg cell and 17 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR026986; KIF22.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010994; RuvA_2-like.
DR   PANTHER; PTHR24115; PTHR24115; 1.
DR   PANTHER; PTHR24115:SF801; PTHR24115:SF801; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding;
KW   Microtubule; Motor protein; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..650
FT                   /note="Kinesin-like protein KIF22-B"
FT                   /id="PRO_0000347239"
FT   DOMAIN          31..359
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          365..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          452..498
FT                   /evidence="ECO:0000255"
FT   MOTIF           560..563
FT                   /note="Important for regulated proteolytic degradation"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        378..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   CONFLICT        18
FT                   /note="V -> A (in Ref. 1; CAB71799)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="Y -> H (in Ref. 1; CAB71799)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        214
FT                   /note="E -> A (in Ref. 1; CAB71799)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        522
FT                   /note="V -> A (in Ref. 1; CAB71799)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   650 AA;  73168 MW;  536088541FCE5353 CRC64;
     MVLTGPPQRE SVSMVKRVSM LDQHKKSSCA RVRVAVRLRP YMEEKEEDKV PTACVRGLDS
     HSLEIVNWRN QLETMQYQFD AFYGDSASQR EIYMGSVCHI LPHLLIGQNA SVFAYGPTGA
     GKTHTMLGNP DQPGVIPRAV RELLQMTRMA ASAPENENWT YTITMSYVEI YQEKVMDLLE
     PKNKDLPIRE DKDHNILIPG VTLKTINSFG DFDEHFIPAS QNRTVASTKL NDRSSRSHAV
     LLIKVQKSQQ VAPFRQLIGK LYLIDLAGSE DNRRTGNQGI RLKESGAINS SLFTLSKVVD
     ALNQGLPRIP YRDSKLTRLL QDSLGGSAHS VMITNIAPEQ TYYFDTLTAL NFAAKSKQII
     NKPFSRETTQ TVAQPAMKRP REEAEATTSS RQRKKSKTDS TESSPNSSME STGKRKLNLA
     SLDSAVVERL LKLDKILTEK GKKEAQLLST PKRERMALLK KWEESQMEIE RLKEKQKELE
     QKAMEAEARL EKSNNSDLSD SSVSENTFRA PLRGRNTSTA KVKKVLRVLP MQGNSQLQST
     IEEGIPVFEK KKKKQVTCDG HENQPTWEMN MRTDLLESGK ERILKLLNTG SVKELKSLQR
     IGDKKAKLII GWREVNGLFK NVEELECLEG ISAKQVSSFI KANILSSISS
 
 
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