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CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2)

 CLAP2_MOUSE             Reviewed;        1286 AA.
Q8BRT1; Q8CHE3; Q99JI3; Q9DB80;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=CLIP-associating protein 2;
AltName: Full=Cytoplasmic linker-associated protein 2;
Name=Clasp2; Synonyms=Kiaa0627;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION,
ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INTERACTION WITH CLIP2 AND
RSN, AND MUTAGENESIS OF CYS-6 AND CYS-10.
PubMed=11290329; DOI=10.1016/S0092-8674(01)00288-4;
Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
Galjart N.;
"Clasps are CLIP-115 and -170 associating proteins involved in the
regional regulation of microtubule dynamics in motile fibroblasts.";
Cell 104:923-935(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
STRAIN=C57BL/6J; TISSUE=Brain cortex, and Cerebellum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-1286 (ISOFORM 1).
PubMed=12465718; DOI=10.1093/dnares/9.5.179;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
I. The complete nucleotide sequences of 100 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 9:179-188(2002).
[5]
SEQUENCE REVISION.
Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[7]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=16123238; DOI=10.1530/rep.1.00651;
Moore C.A., Zernicka-Goetz M.;
"PAR-1 and the microtubule-associated proteins CLASP2 and dynactin-p50
have specific localisation on mouse meiotic and first mitotic
spindles.";
Reproduction 130:311-320(2005).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16914514; DOI=10.1091/mbc.E06-07-0579;
Pereira A.L., Pereira A.J., Maia A.R.R., Drabek K., Sayas C.L.,
Hergert P.J., Lince-Faria M., Matos I., Duque C., Stepanova T.,
Rieder C.L., Earnshaw W.C., Galjart N., Maiato H.;
"Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by
regulating spindle and kinetochore function.";
Mol. Biol. Cell 17:4526-4542(2006).
[9]
INTERACTION WITH MACF1.
PubMed=18854161; DOI=10.1016/j.cell.2008.07.045;
Wu X., Kodama A., Fuchs E.;
"ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and
has ATPase activity.";
Cell 135:137-148(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-374; SER-376;
SER-620 AND SER-947, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 642-873, AND DOMAIN.
PubMed=26003921; DOI=10.1016/j.jmb.2015.05.012;
Maki T., Grimaldi A.D., Fuchigami S., Kaverina I., Hayashi I.;
"CLASP2 has two distinct TOG domains that contribute differently to
microtubule dynamics.";
J. Mol. Biol. 427:2379-2395(2015).
-!- FUNCTION: Microtubule plus-end tracking protein that promotes the
stabilization of dynamic microtubules. Involved in the nucleation
of noncentrosomal microtubules originating from the trans-Golgi
network (TGN). Required for the polarization of the cytoplasmic
microtubule arrays in migrating cells towards the leading edge of
the cell. May act at the cell cortex to enhance the frequency of
rescue of depolymerizing microtubules by attaching their plus-ends
to cortical platforms composed of ERC1 and PHLDB2. This cortical
microtubule stabilizing activity is regulated at least in part by
phosphatidylinositol 3-kinase signaling. Also performs a similar
stabilizing function at the kinetochore which is essential for the
bipolar alignment of chromosomes on the mitotic spindle. Acts as a
mediator of ERBB2-dependent stabilization of microtubules at the
cell cortex. {ECO:0000250|UniProtKB:O75122,
ECO:0000269|PubMed:16914514}.
-!- SUBUNIT: Interacts with microtubules (PubMed:11290329). Interacts
with MAPRE1; probably required for targeting to growing
microtubule plus ends. Interacts with ERC1, MAPRE3 and PHLDB2. The
interaction with ERC1 may be mediated by PHLDB2. Interacts with
GCC2; recruits CLASP2 to Golgi membranes (By similarity).
Interacts with CLIP2 and RSN (PubMed:11290329). Interacts with
MACF1 (PubMed:18854161). {ECO:0000250|UniProtKB:O75122,
ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:18854161}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11290329}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Chromosome, centromere,
kinetochore. Cytoplasm, cytoskeleton, spindle. Cytoplasm,
cytoskeleton, spindle pole. Golgi apparatus
{ECO:0000269|PubMed:11290329}. Golgi apparatus, trans-Golgi
network {ECO:0000250|UniProtKB:O75122}. Cell membrane
{ECO:0000250|UniProtKB:O75122}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:O75122}. Note=Localizes to microtubule plus
ends (PubMed:11290329). Localizes to centrosomes, kinetochores and
the mitotic spindle from prometaphase. Subsequently localizes to
the spindle midzone from anaphase and to the midbody from
telophase. In migrating cells localizes to the plus ends of
microtubules within the cell body and to the entire microtubule
lattice within the lamella. Localizes to the cell cortex and this
requires ERC1 and PHLDB2 (By similarity). Also localizes to
meiotic spindle poles. The MEMO1-RHOA-DIAPH1 signaling pathway
controls localization of the phosphorylated form to the cell
membrane (By similarity). {ECO:0000250|UniProtKB:O75122,
ECO:0000269|PubMed:11290329}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8BRT1-1; Sequence=Displayed;
Name=2;
IsoId=Q8BRT1-5; Sequence=VSP_015808, VSP_015811;
Name=3;
IsoId=Q8BRT1-6; Sequence=VSP_015809, VSP_015810, VSP_015812;
-!- TISSUE SPECIFICITY: Highly expressed in brain and at low levels in
heart, kidney and lung. {ECO:0000269|PubMed:11290329}.
-!- DEVELOPMENTAL STAGE: Expressed in oocytes and early embryos.
{ECO:0000269|PubMed:16123238}.
-!- DOMAIN: The two SXIP sequence motifs mediate interaction with
MAPRE1; this is necessary for targeting to growing microtubule
plus ends. {ECO:0000250|UniProtKB:O75122}.
-!- DOMAIN: Two TOG regions display structural characteristics similar
to HEAT repeat domains and mediate interaction with microtubules.
{ECO:0000250|UniProtKB:O75122, ECO:0000269|PubMed:26003921}.
-!- PTM: Phosphorylated by GSK3B. Phosphorylation by GSK3B may
negatively regulate binding to microtubule lattices in lamella.
Isoform 2 is phosphorylated on Ser-241.
-!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC41436.2; Type=Frameshift; Positions=737; Evidence={ECO:0000305};
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EMBL; AJ276961; CAC35161.1; -; mRNA.
EMBL; AK043551; BAC31579.1; -; mRNA.
EMBL; AK005146; BAB23842.1; -; mRNA.
EMBL; BC030468; AAH30468.1; -; mRNA.
EMBL; AB093252; BAC41436.2; ALT_FRAME; Transcribed_RNA.
CCDS; CCDS52948.1; -. [Q8BRT1-1]
RefSeq; NP_001273528.1; NM_001286599.1.
RefSeq; NP_001273529.1; NM_001286600.1.
RefSeq; NP_001273530.1; NM_001286601.1.
RefSeq; NP_001273531.1; NM_001286602.1.
RefSeq; NP_001273532.1; NM_001286603.1. [Q8BRT1-6]
UniGene; Mm.222272; -.
PDB; 3WOZ; X-ray; 2.20 A; A/B/C/D=642-873.
PDBsum; 3WOZ; -.
ProteinModelPortal; Q8BRT1; -.
SMR; Q8BRT1; -.
BioGrid; 218155; 7.
IntAct; Q8BRT1; 5.
MINT; MINT-4112101; -.
STRING; 10090.ENSMUSP00000130201; -.
iPTMnet; Q8BRT1; -.
PhosphoSitePlus; Q8BRT1; -.
EPD; Q8BRT1; -.
PaxDb; Q8BRT1; -.
PeptideAtlas; Q8BRT1; -.
PRIDE; Q8BRT1; -.
GeneID; 76499; -.
KEGG; mmu:76499; -.
UCSC; uc009rwt.2; mouse. [Q8BRT1-6]
CTD; 23122; -.
MGI; MGI:1923749; Clasp2.
eggNOG; KOG2956; Eukaryota.
eggNOG; ENOG410ZMY0; LUCA.
HOGENOM; HOG000185856; -.
HOVERGEN; HBG079692; -.
InParanoid; Q8BRT1; -.
KO; K16578; -.
PhylomeDB; Q8BRT1; -.
PRO; PR:Q8BRT1; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CLASP2; -.
GO; GO:0044295; C:axonal growth cone; ISO:MGI.
GO; GO:0045180; C:basal cortex; ISO:MGI.
GO; GO:0005938; C:cell cortex; ISO:MGI.
GO; GO:0031252; C:cell leading edge; IDA:MGI.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:1903754; C:cortical microtubule plus-end; ISO:MGI.
GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005874; C:microtubule; ISS:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
GO; GO:0051015; F:actin filament binding; ISO:MGI.
GO; GO:0002162; F:dystroglycan binding; ISO:MGI.
GO; GO:0008017; F:microtubule binding; IDA:MGI.
GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IMP:MGI.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; ISO:MGI.
GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; ISO:MGI.
GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; ISO:MGI.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISO:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
GO; GO:0030516; P:regulation of axon extension; ISO:MGI.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0010470; P:regulation of gastrulation; ISO:MGI.
GO; GO:0031113; P:regulation of microtubule polymerization; ISO:MGI.
GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:MGI.
GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
GO; GO:0006903; P:vesicle targeting; ISO:MGI.
Gene3D; 1.25.10.10; -; 2.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR024395; CLASP_N_dom.
InterPro; IPR034085; TOG.
Pfam; PF12348; CLASP_N; 1.
SMART; SM01349; TOG; 3.
SUPFAM; SSF48371; SSF48371; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Cell membrane; Cell projection; Centromere; Chromosome;
Complete proteome; Cytoplasm; Cytoskeleton; Golgi apparatus;
Kinetochore; Meiosis; Membrane; Microtubule; Mitosis; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 1286 CLIP-associating protein 2.
/FTId=PRO_0000089850.
REPEAT 179 214 HEAT 1. {ECO:0000255}.
REPEAT 215 251 HEAT 2. {ECO:0000255}.
REPEAT 256 293 HEAT 3. {ECO:0000255}.
REPEAT 702 739 HEAT 4. {ECO:0000255}.
REPEAT 764 801 HEAT 5. {ECO:0000255}.
REPEAT 1046 1083 HEAT 6. {ECO:0000255}.
REPEAT 1090 1127 HEAT 7. {ECO:0000255}.
REPEAT 1208 1245 HEAT 8. {ECO:0000255}.
REGION 1 40 Golgi localization.
REGION 66 317 TOG 1. {ECO:0000250|UniProtKB:O75122}.
REGION 450 565 Interaction with microtubules, MAPRE1 and
MAPRE3. {ECO:0000250}.
REGION 642 873 TOG 2. {ECO:0000250|UniProtKB:O75122}.
REGION 864 1286 Interaction with RSN and localization to
the Golgi and kinetochores.
{ECO:0000250}.
REGION 1009 1286 Required for cortical localization.
{ECO:0000250}.
MOTIF 500 503 SXIP motif 1; mediates interaction with
MAPRE1 and targeting to microtubule plus
ends. {ECO:0000250|UniProtKB:O75122}.
MOTIF 523 526 SXIP motif 2; mediates interaction with
MAPRE1 and targeting to microtubule plus
ends. {ECO:0000250|UniProtKB:O75122}.
COMPBIAS 459 572 Ser-rich.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000250|UniProtKB:Q99JD4}.
MOD_RES 322 322 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 374 374 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 376 376 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000250|UniProtKB:Q99JD4}.
MOD_RES 461 461 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 495 495 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 531 531 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 581 581 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 614 614 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 779 779 Phosphothreonine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 884 884 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 944 944 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 947 947 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1005 1005 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
MOD_RES 1021 1021 Phosphoserine.
{ECO:0000250|UniProtKB:O75122}.
VAR_SEQ 1 12 MRRLICKRICDY -> MEPRGAEYFCAQVLQKDVSGRLQAG
EELLLCLGTPGAIPDLEDDPSRLAKTVDALTRWVGSSNYRV
SLLGLEILSAFVDRLSTRFKSYVTMVTTALIDRMGDVKDKV
REEAQNLTLKLMDEVAPPMYIWEQLASGFKHKNFRSREGVC
LCLIETLNIFGTQPLVISKLVPHLCVLFGDSNSQVRNAALS
AVVEIYRHVGEKLRIDLCKRDIPPARLEMVLAKFDEVQNSG
GMILSVCKD (in isoform 2).
{ECO:0000303|PubMed:11290329}.
/FTId=VSP_015808.
VAR_SEQ 1 12 MRRLICKRICDY -> MAMGDD (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_015809.
VAR_SEQ 119 173 LKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVV
REACITVAHLSTVL -> CMSCSLVASEVERALAWPLWSHL
ATYQHHCHCTLSHEDLPEKRLTSPVSSAFVQH (in
isoform 3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_015810.
VAR_SEQ 142 1054 Missing (in isoform 2).
{ECO:0000303|PubMed:11290329}.
/FTId=VSP_015811.
VAR_SEQ 174 1286 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_015812.
MUTAGEN 6 6 C->S: Impairs Golgi localization; when
associated with S-10.
{ECO:0000269|PubMed:11290329}.
MUTAGEN 10 10 C->S: Impairs Golgi localization; when
associated with S-6.
{ECO:0000269|PubMed:11290329}.
CONFLICT 657 657 S -> T (in Ref. 4; BAC41436).
{ECO:0000305}.
CONFLICT 683 683 I -> V (in Ref. 4; BAC41436).
{ECO:0000305}.
CONFLICT 699 699 P -> L (in Ref. 4; BAC41436).
{ECO:0000305}.
CONFLICT 702 702 K -> KR (in Ref. 4; BAC41436).
{ECO:0000305}.
HELIX 648 655 {ECO:0000244|PDB:3WOZ}.
HELIX 660 675 {ECO:0000244|PDB:3WOZ}.
HELIX 682 695 {ECO:0000244|PDB:3WOZ}.
HELIX 701 718 {ECO:0000244|PDB:3WOZ}.
HELIX 719 721 {ECO:0000244|PDB:3WOZ}.
TURN 723 725 {ECO:0000244|PDB:3WOZ}.
HELIX 726 737 {ECO:0000244|PDB:3WOZ}.
HELIX 743 759 {ECO:0000244|PDB:3WOZ}.
HELIX 762 774 {ECO:0000244|PDB:3WOZ}.
STRAND 776 778 {ECO:0000244|PDB:3WOZ}.
HELIX 782 796 {ECO:0000244|PDB:3WOZ}.
HELIX 801 803 {ECO:0000244|PDB:3WOZ}.
HELIX 808 820 {ECO:0000244|PDB:3WOZ}.
HELIX 827 843 {ECO:0000244|PDB:3WOZ}.
HELIX 845 853 {ECO:0000244|PDB:3WOZ}.
HELIX 857 867 {ECO:0000244|PDB:3WOZ}.
SEQUENCE 1286 AA; 140739 MW; 5B208D8F4E90CB93 CRC64;
MRRLICKRIC DYKSFDDEES VDGNRPSSAA SAFKVPAPKT PGNPVSSARK PGSAGGPKVG
GPSKEGGAGA VDEDDFIKAF TDVPSVQIYS SRELEETLNK IREILSDDKH DWDQRANALK
KIRSLLVAGA AQYDCFFQHL RLLDGALKLS AKDLRSQVVR EACITVAHLS TVLGNKFDHG
AEAIVPTLFN LVPNSAKVMA TSGCAAIRFI IRHTHVPRLI PLITSNCTSK SVPVRRRSFE
FLDLLLQEWQ THSLERHAAV LVETIKKGIH DADAEARVEA RKTYMGLRNH FPGEAETLYN
SLEPSYQKSL QTYLKSSGSV ASLPQSDRSS SSSQESLNRP FSSKWSTANP STVAGRVSVG
GSKANPLPGS LQRSRSDIDV NAAAGAKAHH AAGQAVRSGR LGAGALNPGS YASLEDTSDK
MDGTASDDGR VRAKLSTPLV AVGNAKTDSR GRSRTKMVSQ SQPGSRSGSP GRVLTTTALS
TVSSGAQRVL VNSASAQKRS KIPRSQGCSR EASPSRLSVA RSSRIPRPSV SQGCSREASR
ESSRDTSPVR SFQPLGPGYG ISQSSRLSSS VSAMRVLNTG SDVEEAVADA LLLGDIRTKK
KPARRRYESY GMHSDDDANS DASSACSERS YSSRNGSIPT YMRQTEDVAE VLNRCASSNW
SERKEGLLGL QNLLKNQRTL SRIELKRLCE IFTRMFADPH GKVFSMFLET LVDFIQVHKD
DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ KALDITRESF PNDLQFNILM RFTVDQTQTP
SLKVKVAILK YIETLAKQMD PRDFTNSSET RLAVSRVITW TTEPKSSDVR KAAQSVLISL
FELNTPEFTM LLGALPKTFQ DGATKLLHNH LRNTGNGTQS SMGSPLTRPT PRSPANWSSP
LTSPTNTSQN TLSPSAFDYD TENMNSEDIY SSLRGVTEAI QNFSFRSQED MSEPVRRDPK
KEDGDTICSG PGMSDPRAGG DAADGSQPAL DNKASLLHSM PLHSSPRSRD YNPYNYSDSI
SPFNKSALKE AMFDDDADQF PDDLSLDHSD LVAELLKELS NHNERIEERK IALYELMKLT
QEESFSVWDE HFKTILLLLL ETLGDKEPTI RALALKVLKE ILRHQPARFK NYAELTVMKT
LEAHKDPHKE VVRSAEEAAS VLATSISPEQ CIKVLCPIIQ TADYPINLAA IKMQTKVIER
VSKETLNMLL PEIMPGLIQG YDNSESSVRK ACVFCLVAVH AVIGDELKPH LSQLTGSKMK
LLNLYIKRAQ TGSAGADPTA DVSGQS


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