STMN2_HUMAN
ID STMN2_HUMAN Reviewed; 179 AA.
AC Q93045; A8K9M2; G3V110; O14952; Q6PK68;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Stathmin-2;
DE AltName: Full=Superior cervical ganglion-10 protein;
DE Short=Protein SCG10;
GN Name=STMN2; Synonyms=SCG10, SCGN10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8622778; DOI=10.1016/0197-4580(95)02001-2;
RA Okazaki T., Wang H., Masliah E., Cao M., Johnson S.A., Sundsmo M.,
RA Saitoh T., Mori N.;
RT "SCG10, a neuron-specific growth-associated protein in Alzheimer's
RT disease.";
RL Neurobiol. Aging 16:883-894(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S.,
RA Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M.,
RA Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E., Hirai Y.;
RT "Molecular cloning of a human homologue of chicken silencer element (SCG10)
RT gene.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Neuroblastoma;
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).
RN [9]
RP PROTEIN SEQUENCE OF 12-43; 48-69; 78-86; 147-156 AND 172-179, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [11]
RP INTERACTION WITH ITM2C.
RX PubMed=18452648; DOI=10.5483/bmbrep.2008.41.4.287;
RA Gong Y., Wu J., Qiang H., Liu B., Chi Z., Chen T., Yin B., Peng X.,
RA Yuan J.;
RT "BRI3 associates with SCG10 and attenuates NGF-induced neurite outgrowth in
RT PC12 cells.";
RL BMB Rep. 41:287-293(2008).
RN [12]
RP INTERACTION WITH KIFBP.
RX PubMed=20621975; DOI=10.1093/hmg/ddq280;
RA Alves M.M., Burzynski G., Delalande J.M., Osinga J., van der Goot A.,
RA Dolga A.M., de Graaff E., Brooks A.S., Metzger M., Eisel U.L., Shepherd I.,
RA Eggen B.J., Hofstra R.M.;
RT "KBP interacts with SCG10, linking Goldberg-Shprintzen syndrome to
RT microtubule dynamics and neuronal differentiation.";
RL Hum. Mol. Genet. 19:3642-3651(2010).
RN [13]
RP INTERACTION WITH CIB1, AND SUBCELLULAR LOCATION.
RX PubMed=21215777; DOI=10.1016/j.bbamcr.2010.12.023;
RA Sobczak A., Debowska K., Blazejczyk M., Kreutz M.R., Kuznicki J., Wojda U.;
RT "Calmyrin1 binds to SCG10 protein (stathmin2) to modulate neurite
RT outgrowth.";
RL Biochim. Biophys. Acta 1813:1025-1037(2011).
RN [14]
RP PALMITOYLATION AT CYS-22 AND CYS-24 BY ZDHHC3; ZDHHC7 AND ZDHHC15, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21471001; DOI=10.1091/mbc.e10-10-0824;
RA Levy A.D., Devignot V., Fukata Y., Fukata M., Sobel A., Chauvin S.;
RT "Subcellular Golgi localization of stathmin family proteins is promoted by
RT a specific set of DHHC palmitoyl transferases.";
RL Mol. Biol. Cell 22:1930-1942(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Regulator of microtubule stability. When phosphorylated by
CC MAPK8, stabilizes microtubules and consequently controls neurite length
CC in cortical neurons. In the developing brain, negatively regulates the
CC rate of exit from multipolar stage and retards radial migration from
CC the ventricular zone (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAPK8 (By similarity). Interacts with ITM2C.
CC Interacts with KIFBP. Interacts (via the N-terminal region) with CIB1
CC (via C-terminal region); the interaction is direct, occurs in a
CC calcium-dependent manner and attenuates the neurite outgrowth
CC inhibition of STMN2. {ECO:0000250, ECO:0000269|PubMed:18452648,
CC ECO:0000269|PubMed:20621975, ECO:0000269|PubMed:21215777}.
CC -!- INTERACTION:
CC Q93045; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-714194, EBI-10175300;
CC Q93045; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-714194, EBI-11962928;
CC Q93045; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-714194, EBI-6658203;
CC Q93045; O95983-2: MBD3; NbExp=3; IntAct=EBI-714194, EBI-11978579;
CC Q93045; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-714194, EBI-741158;
CC Q93045; P20618: PSMB1; NbExp=3; IntAct=EBI-714194, EBI-372273;
CC Q93045; Q86VW0: SESTD1; NbExp=3; IntAct=EBI-714194, EBI-6117072;
CC Q93045; Q8IYF3: TEX11; NbExp=5; IntAct=EBI-714194, EBI-742397;
CC Q93045; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-714194, EBI-11523345;
CC Q93045; Q12800: TFCP2; NbExp=3; IntAct=EBI-714194, EBI-717422;
CC Q93045; P40222: TXLNA; NbExp=4; IntAct=EBI-714194, EBI-359793;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Cell projection, growth cone. Membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Cell projection, axon. Golgi apparatus. Endosome
CC {ECO:0000250}. Cell projection, lamellipodium. Note=Associated with
CC punctate structures in the perinuclear cytoplasm, axons, and growth
CC cones of developing neurons. SCG10 exists in both soluble and membrane-
CC bound forms. Colocalized with CIB1 in neurites of developing
CC hippocampal primary neurons (By similarity). Colocalized with CIB1 in
CC the cell body, neuritis and growth cones of neurons. Colocalized with
CC CIB1 to the leading edge of lamellipodia. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q93045-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93045-2; Sequence=VSP_045047;
CC -!- TISSUE SPECIFICITY: Neuron specific.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
CC -!- PTM: Phosphorylated mostly by MAPK8, but also by MAPK9 and MAPK10 in
CC the developing brain cortex. {ECO:0000250}.
CC -!- PTM: N-terminal palmitoylation promotes specific anchoring to the
CC cytosolic leaflet of Golgi membranes and subsequent vesicular
CC trafficking along dendrites and axons. Neuronal Stathmins are
CC substrates for palmitoyltransferases ZDHHC3, ZDHHC7 and ZDHHC15.
CC {ECO:0000269|PubMed:21471001}.
CC -!- SIMILARITY: Belongs to the stathmin family. {ECO:0000305}.
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DR EMBL; S82024; AAB36428.1; -; mRNA.
DR EMBL; D50375; BAA23326.1; -; mRNA.
DR EMBL; BT020034; AAV38837.1; -; mRNA.
DR EMBL; CR456833; CAG33114.1; -; mRNA.
DR EMBL; AK292737; BAF85426.1; -; mRNA.
DR EMBL; AC016240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW87064.1; -; Genomic_DNA.
DR EMBL; CH471068; EAW87065.1; -; Genomic_DNA.
DR EMBL; BC006302; AAH06302.1; -; mRNA.
DR EMBL; BQ069488; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS43748.1; -. [Q93045-1]
DR CCDS; CCDS56542.1; -. [Q93045-2]
DR RefSeq; NP_001186143.1; NM_001199214.1. [Q93045-2]
DR RefSeq; NP_008960.2; NM_007029.3. [Q93045-1]
DR AlphaFoldDB; Q93045; -.
DR SMR; Q93045; -.
DR BioGRID; 116258; 67.
DR IntAct; Q93045; 23.
DR MINT; Q93045; -.
DR STRING; 9606.ENSP00000429243; -.
DR iPTMnet; Q93045; -.
DR PhosphoSitePlus; Q93045; -.
DR BioMuta; STMN2; -.
DR DMDM; 51704330; -.
DR EPD; Q93045; -.
DR jPOST; Q93045; -.
DR MassIVE; Q93045; -.
DR MaxQB; Q93045; -.
DR PaxDb; Q93045; -.
DR PeptideAtlas; Q93045; -.
DR PRIDE; Q93045; -.
DR ProteomicsDB; 32221; -.
DR ProteomicsDB; 75686; -. [Q93045-1]
DR ABCD; Q93045; 1 sequenced antibody.
DR Antibodypedia; 6337; 462 antibodies from 40 providers.
DR DNASU; 11075; -.
DR Ensembl; ENST00000220876.12; ENSP00000220876.7; ENSG00000104435.14. [Q93045-1]
DR Ensembl; ENST00000518111.5; ENSP00000429243.1; ENSG00000104435.14. [Q93045-2]
DR GeneID; 11075; -.
DR KEGG; hsa:11075; -.
DR MANE-Select; ENST00000220876.12; ENSP00000220876.7; NM_007029.4; NP_008960.2.
DR UCSC; uc003ybj.3; human. [Q93045-1]
DR CTD; 11075; -.
DR DisGeNET; 11075; -.
DR GeneCards; STMN2; -.
DR HGNC; HGNC:10577; STMN2.
DR HPA; ENSG00000104435; Tissue enriched (brain).
DR MIM; 600621; gene.
DR neXtProt; NX_Q93045; -.
DR OpenTargets; ENSG00000104435; -.
DR PharmGKB; PA35540; -.
DR VEuPathDB; HostDB:ENSG00000104435; -.
DR eggNOG; ENOG502RENQ; Eukaryota.
DR GeneTree; ENSGT01030000234597; -.
DR InParanoid; Q93045; -.
DR OMA; HMAAMME; -.
DR OrthoDB; 1381987at2759; -.
DR PhylomeDB; Q93045; -.
DR TreeFam; TF326935; -.
DR PathwayCommons; Q93045; -.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q93045; -.
DR SIGNOR; Q93045; -.
DR BioGRID-ORCS; 11075; 5 hits in 1061 CRISPR screens.
DR ChiTaRS; STMN2; human.
DR GeneWiki; STMN2; -.
DR GenomeRNAi; 11075; -.
DR Pharos; Q93045; Tbio.
DR PRO; PR:Q93045; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q93045; protein.
DR Bgee; ENSG00000104435; Expressed in cortical plate and 160 other tissues.
DR ExpressionAtlas; Q93045; baseline and differential.
DR Genevisible; Q93045; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:UniProtKB.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR InterPro; IPR026729; Stathmin-2.
DR InterPro; IPR030514; Stathmin_CS.
DR InterPro; IPR000956; Stathmin_fam.
DR InterPro; IPR036002; Stathmin_sf.
DR PANTHER; PTHR10104; PTHR10104; 1.
DR PANTHER; PTHR10104:SF18; PTHR10104:SF18; 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 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Endosome; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..179
FT /note="Stathmin-2"
FT /id="PRO_0000182396"
FT DOMAIN 38..179
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT REGION 1..26
FT /note="Membrane attachment"
FT /evidence="ECO:0000255"
FT REGION 39..96
FT /note="Regulatory/phosphorylation domain"
FT /evidence="ECO:0000255"
FT COILED 75..179
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55821, ECO:0000255"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21818"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16949, ECO:0000255"
FT LIPID 22
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21471001"
FT LIPID 24
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21471001"
FT VAR_SEQ 161..179
FT /note="ERHAAEVRRNKELQVELSG -> LVKFISSELKESIESQFLELQREGEKQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045047"
FT CONFLICT 92
FT /note="E -> G (in Ref. 1; AAB36428)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="E -> G (in Ref. 2; BAA23326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 179 AA; 20828 MW; F9A258A1B57E620D CRC64;
MAKTAMAYKE KMKELSMLSL ICSCFYPEPR NINIYTYDDM EVKQINKRAS GQAFELILKP
PSPISEAPRT LASPKKKDLS LEEIQKKLEA AEERRKSQEA QVLKQLAEKR EHEREVLQKA
LEENNNFSKM AEEKLILKME QIKENREANL AAIIERLQEK ERHAAEVRRN KELQVELSG
