STMN1_GEKJA
ID STMN1_GEKJA Reviewed; 149 AA.
AC A9YWH3; Q5EI00;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Stathmin;
GN Name=STMN1; Synonyms=STMN;
OS Gekko japonicus (Schlegel's Japanese gecko).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Gekkota; Gekkonidae; Gekkoninae; Gekko.
OX NCBI_TaxID=146911;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Gu X., Ding F., Liu Y., Liu M., Gong L., Shao C.;
RT "Analysis of expressed sequence tags and cloning of full length cDNA from
RT brain and spinal cord cDNA library in Gecko.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jiang X., Wang Y., Ding F., Liu Y., Huan Y., Ren L.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the regulation of the microtubule (MT) filament
CC system by destabilizing microtubules. Prevents assembly and promotes
CC disassembly of microtubules (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to two alpha/beta-tubulin heterodimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the stathmin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW78997.1; Type=Miscellaneous discrepancy; Note=Probable sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AY880382; AAW78997.1; ALT_SEQ; mRNA.
DR EMBL; EU304453; ABY27080.1; -; mRNA.
DR AlphaFoldDB; A9YWH3; -.
DR SMR; A9YWH3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:InterPro.
DR InterPro; IPR030514; Stathmin_CS.
DR InterPro; IPR000956; Stathmin_fam.
DR InterPro; IPR036002; Stathmin_sf.
DR PANTHER; PTHR10104; PTHR10104; 1.
DR Pfam; PF00836; Stathmin; 1.
DR PIRSF; PIRSF002285; Stathmin; 1.
DR PRINTS; PR00345; STATHMIN.
DR SUPFAM; SSF101494; SSF101494; 1.
DR PROSITE; PS00563; STATHMIN_1; 1.
DR PROSITE; PS01041; STATHMIN_2; 1.
DR PROSITE; PS51663; STATHMIN_3; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein.
FT CHAIN 1..149
FT /note="Stathmin"
FT /id="PRO_0000372586"
FT DOMAIN 4..145
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT REGION 121..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..141
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 149 AA; 17303 MW; 316426F60DABCD01 CRC64;
MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER
RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL
ERLREKDKHI EEVRKNKESK DPADETEAD
