HAUS8_HUMAN
ID HAUS8_HUMAN Reviewed; 410 AA.
AC Q9BT25; B4DJA7; C9JBZ4; Q49AC4; Q86WF0; Q96FX3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=HAUS augmin-like complex subunit 8;
DE AltName: Full=HEC1/NDC80-interacting centrosome-associated protein 1;
DE AltName: Full=Sarcoma antigen NY-SAR-48;
GN Name=HAUS8; Synonyms=HICE1;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP VARIANT ARG-83.
RX PubMed=18362163; DOI=10.1128/mcb.01923-07;
RA Wu G., Lin Y.-T., Wei R., Chen Y., Shan Z., Lee W.-H.;
RT "Hice1, a novel microtubule-associated protein required for maintenance of
RT spindle integrity and chromosomal stability in human cells.";
RL Mol. Cell. Biol. 28:3652-3662(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Subthalamic nucleus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-283 (ISOFORM 1).
RX PubMed=12601173; DOI=10.1073/pnas.0437972100;
RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B.,
RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.;
RT "Immunomic analysis of human sarcoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-410 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 152-410 (ISOFORMS 1/2), AND VARIANT ARG-83.
RC TISSUE=Eye, and Placenta;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION IN THE HAUS AUGMIN-LIKE COMPLEX, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19427217; DOI=10.1016/j.cub.2009.04.033;
RA Lawo S., Bashkurov M., Mullin M., Ferreria M.G., Kittler R., Habermann B.,
RA Tagliaferro A., Poser I., Hutchins J.R.A., Hegemann B., Pinchev D.,
RA Buchholz F., Peters J.-M., Hyman A.A., Gingras A.-C., Pelletier L.;
RT "HAUS, the 8-subunit human augmin complex, regulates centrosome and spindle
RT integrity.";
RL Curr. Biol. 19:816-826(2009).
RN [10]
RP IDENTIFICATION IN THE HAUS AUGMIN-LIKE COMPLEX, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19369198; DOI=10.1073/pnas.0901587106;
RA Uehara R., Nozawa R.-S., Tomioka A., Petry S., Vale R.D., Obuse C.,
RA Goshima G.;
RT "The augmin complex plays a critical role in spindle microtubule generation
RT for mitotic progression and cytokinesis in human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6998-7003(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP INTERACTION WITH EML3 AND TUBG1, AND SUBCELLULAR LOCATION.
RX PubMed=30723163; DOI=10.1074/jbc.ra118.007164;
RA Luo J., Yang B., Xin G., Sun M., Zhang B., Guo X., Jiang Q., Zhang C.;
RT "The microtubule-associated protein EML3 regulates mitotic spindle assembly
RT by recruiting the Augmin complex to spindle microtubules.";
RL J. Biol. Chem. 294:5643-5656(2019).
CC -!- FUNCTION: Contributes to mitotic spindle assembly, maintenance of
CC centrosome integrity and completion of cytokinesis as part of the HAUS
CC augmin-like complex. {ECO:0000269|PubMed:18362163,
CC ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.
CC -!- SUBUNIT: Component of the HAUS augmin-like complex. The complex
CC interacts with the gamma-tubulin ring complex and this interaction is
CC required for spindle assembly. Associates with microtubules. The
CC interaction with microtubules is strong during mitosis, while it is
CC weak or absent during interphase. It is unclear whether this
CC interaction is direct or indirect. Interacts with EML3 (phosphorylated
CC at 'Thr-881') and TUBG1 (PubMed:30723163).
CC {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217,
CC ECO:0000269|PubMed:30723163}.
CC -!- INTERACTION:
CC Q9BT25; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-2558143, EBI-747505;
CC Q9BT25; P55212: CASP6; NbExp=3; IntAct=EBI-2558143, EBI-718729;
CC Q9BT25; Q8TD31-3: CCHCR1; NbExp=5; IntAct=EBI-2558143, EBI-10175300;
CC Q9BT25; Q05D60: DEUP1; NbExp=3; IntAct=EBI-2558143, EBI-748597;
CC Q9BT25; P22607: FGFR3; NbExp=3; IntAct=EBI-2558143, EBI-348399;
CC Q9BT25; Q14957: GRIN2C; NbExp=3; IntAct=EBI-2558143, EBI-8285963;
CC Q9BT25; Q7Z4H7: HAUS6; NbExp=9; IntAct=EBI-2558143, EBI-2558196;
CC Q9BT25; P01112: HRAS; NbExp=3; IntAct=EBI-2558143, EBI-350145;
CC Q9BT25; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2558143, EBI-21591415;
CC Q9BT25; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-2558143, EBI-744782;
CC Q9BT25; Q9H7Z3: NRDE2; NbExp=3; IntAct=EBI-2558143, EBI-1042642;
CC Q9BT25; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2558143, EBI-741158;
CC Q9BT25; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-2558143, EBI-741048;
CC Q9BT25; P62826: RAN; NbExp=3; IntAct=EBI-2558143, EBI-286642;
CC Q9BT25; Q99757: TXN2; NbExp=3; IntAct=EBI-2558143, EBI-2932492;
CC Q9BT25; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-2558143, EBI-739895;
CC Q9BT25; Q96DA0: ZG16B; NbExp=3; IntAct=EBI-2558143, EBI-953824;
CC Q9BT25; Q9Y649; NbExp=3; IntAct=EBI-2558143, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000269|PubMed:19369198,
CC ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217,
CC ECO:0000269|PubMed:30723163}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000305|PubMed:19369198}. Note=During interphase, primarily
CC cytoplasmic and associates with centrosomes and with the mitotic
CC spindles, preferentially at the spindle pole vicinity. During anaphase
CC and telophase, additionally associates with the spindle midzone and
CC midbody, respectively. Localizes to mitotic spindle microtubules.
CC {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217,
CC ECO:0000269|PubMed:30723163}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BT25-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BT25-2; Sequence=VSP_031543;
CC Name=3;
CC IsoId=Q9BT25-3; Sequence=VSP_047167;
CC -!- SIMILARITY: Belongs to the HAUS8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10176.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO65172.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO65172.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK295994; BAG58769.1; -; mRNA.
DR EMBL; AC020908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84570.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84571.1; -; Genomic_DNA.
DR EMBL; AY211919; AAO65172.1; ALT_SEQ; mRNA.
DR EMBL; BC004398; AAH04398.1; -; mRNA.
DR EMBL; BC010176; AAH10176.1; ALT_INIT; mRNA.
DR CCDS; CCDS32948.1; -. [Q9BT25-1]
DR CCDS; CCDS46009.1; -. [Q9BT25-3]
DR RefSeq; NP_001011699.1; NM_001011699.1. [Q9BT25-3]
DR RefSeq; NP_219485.1; NM_033417.1. [Q9BT25-1]
DR AlphaFoldDB; Q9BT25; -.
DR SMR; Q9BT25; -.
DR BioGRID; 125017; 136.
DR ComplexPortal; CPX-1847; HAUS complex.
DR CORUM; Q9BT25; -.
DR DIP; DIP-48834N; -.
DR IntAct; Q9BT25; 82.
DR MINT; Q9BT25; -.
DR STRING; 9606.ENSP00000253669; -.
DR iPTMnet; Q9BT25; -.
DR PhosphoSitePlus; Q9BT25; -.
DR BioMuta; HAUS8; -.
DR DMDM; 229462967; -.
DR EPD; Q9BT25; -.
DR jPOST; Q9BT25; -.
DR MassIVE; Q9BT25; -.
DR MaxQB; Q9BT25; -.
DR PaxDb; Q9BT25; -.
DR PeptideAtlas; Q9BT25; -.
DR PRIDE; Q9BT25; -.
DR ProteomicsDB; 78945; -. [Q9BT25-1]
DR ProteomicsDB; 78946; -. [Q9BT25-2]
DR ProteomicsDB; 9526; -.
DR Antibodypedia; 27511; 207 antibodies from 25 providers.
DR DNASU; 93323; -.
DR Ensembl; ENST00000253669.10; ENSP00000253669.4; ENSG00000131351.15. [Q9BT25-1]
DR Ensembl; ENST00000448593.6; ENSP00000395298.1; ENSG00000131351.15. [Q9BT25-3]
DR Ensembl; ENST00000593360.1; ENSP00000470829.1; ENSG00000131351.15. [Q9BT25-2]
DR GeneID; 93323; -.
DR KEGG; hsa:93323; -.
DR MANE-Select; ENST00000253669.10; ENSP00000253669.4; NM_033417.2; NP_219485.1.
DR UCSC; uc002nfe.4; human. [Q9BT25-1]
DR CTD; 93323; -.
DR DisGeNET; 93323; -.
DR GeneCards; HAUS8; -.
DR HGNC; HGNC:30532; HAUS8.
DR HPA; ENSG00000131351; Low tissue specificity.
DR MIM; 613434; gene.
DR neXtProt; NX_Q9BT25; -.
DR OpenTargets; ENSG00000131351; -.
DR PharmGKB; PA165393466; -.
DR VEuPathDB; HostDB:ENSG00000131351; -.
DR eggNOG; ENOG502S04A; Eukaryota.
DR GeneTree; ENSGT00390000010974; -.
DR HOGENOM; CLU_060977_0_0_1; -.
DR InParanoid; Q9BT25; -.
DR OMA; TAKMEHN; -.
DR OrthoDB; 809178at2759; -.
DR PhylomeDB; Q9BT25; -.
DR TreeFam; TF332998; -.
DR PathwayCommons; Q9BT25; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q9BT25; -.
DR SIGNOR; Q9BT25; -.
DR BioGRID-ORCS; 93323; 661 hits in 1094 CRISPR screens.
DR ChiTaRS; HAUS8; human.
DR GenomeRNAi; 93323; -.
DR Pharos; Q9BT25; Tbio.
DR PRO; PR:Q9BT25; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BT25; protein.
DR Bgee; ENSG00000131351; Expressed in granulocyte and 102 other tissues.
DR ExpressionAtlas; Q9BT25; baseline and differential.
DR Genevisible; Q9BT25; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070652; C:HAUS complex; IDA:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
DR GO; GO:0005880; C:nuclear microtubule; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..410
FT /note="HAUS augmin-like complex subunit 8"
FT /id="PRO_0000319937"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 156..208
FT /evidence="ECO:0000255"
FT COMPBIAS 21..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_031543"
FT VAR_SEQ 77
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047167"
FT VARIANT 83
FT /note="G -> R (in dbSNP:rs1130222)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18362163"
FT /id="VAR_039056"
FT CONFLICT 38
FT /note="R -> P (in Ref. 6; AAH04398)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="Q -> QLQ (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="E -> D (in Ref. 5; AAO65172)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="T -> I (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="T -> L (in Ref. 5; AAO65172)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="L -> F (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 354..355
FT /note="Missing (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 44857 MW; 05D7B175523E5DA5 CRC64;
MADSSGRGAG KPATGPTNSS SAKKKDKRVQ GGRVIESRYL QYEKKTTQKA PAGDGSQTRG
KMSEGGRKSS LLQKSKADSS GVGKGDLQST LLEGHGTAPP DLDLSAINDK SIVKKTPQLA
KTISKKPEST SFSAPRKKSP DLSEAMEMME SQTLLLTLLS VKMENNLAEF ERRAEKNLLI
MCKEKEKLQK KAHELKRRLL LSQRKRELAD VLDAQIEMLS PFEAVATRFK EQYRTFATAL
DTTRHELPVR SIHLEGDGQQ LLDALQHELV TTQRLLGELD VGDSEENVQV LDLLSELKDV
TAKKDLELRR SFAQVLELSA EASKEAALAN QEVWEETQGM APPSRWYFNQ DSACRESGGA
PKNTPLSEDD NPGASSAPAQ ATFISPSEDF SSSSQAEVPP SLSRSGRDLS
