CC88B_HUMAN
ID CC88B_HUMAN Reviewed; 1476 AA.
AC A6NC98; A5D8Y5; B5MDM2; Q05BL2; Q6RUV3; Q8N1Q6; Q8NF44; Q9H0H1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Coiled-coil domain-containing protein 88B;
DE AltName: Full=Brain leucine zipper domain-containing protein;
DE AltName: Full=Gipie {ECO:0000303|PubMed:21289099};
DE AltName: Full=Hook-related protein 3 {ECO:0000303|PubMed:25762780};
DE Short=HkRP3;
GN Name=CCDC88B; Synonyms=BRLZ;
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 [LARGE SCALE MRNA] (ISOFORM 6).
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-886.
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ALA-886.
RC TISSUE=Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1240 (ISOFORM 1), AND VARIANT ALA-886.
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 960-1476 (ISOFORM 4).
RA Rask L., Jensen N.A., Mitchelmore C.;
RT "BRLZ: a leucine zipper protein expressed in brain.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP FUNCTION, INTERACTION WITH HSPA5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY ER STRESS.
RX PubMed=21289099; DOI=10.1091/mbc.e10-08-0724;
RA Matsushita E., Asai N., Enomoto A., Kawamoto Y., Kato T., Mii S., Maeda K.,
RA Shibata R., Hattori S., Hagikura M., Takahashi K., Sokabe M., Murakumo Y.,
RA Murohara T., Takahashi M.;
RT "Protective role of Gipie, a Girdin family protein, in endoplasmic
RT reticulum stress responses in endothelial cells.";
RL Mol. Biol. Cell 22:736-747(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, 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).
RN [11]
RP FUNCTION, INTERACTION WITH DOCK8 AND MICROTUBULES, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=25762780; DOI=10.4049/jimmunol.1402897;
RA Ham H., Huynh W., Schoon R.A., Vale R.D., Billadeau D.D.;
RT "HkRP3 is a microtubule-binding protein regulating lytic granule clustering
RT and NK cell killing.";
RL J. Immunol. 194:3984-3996(2015).
CC -!- FUNCTION: Acts as a positive regulator of T-cell maturation and
CC inflammatory function. Required for several functions of T-cells, in
CC both the CD4(+) and the CD8(+) compartments and this includes
CC expression of cell surface markers of activation, proliferation, and
CC cytokine production in response to specific or non-specific stimulation
CC (By similarity). Enhances NK cell cytotoxicity by positively regulating
CC polarization of microtubule-organizing center (MTOC) to cytotoxic
CC synapse, lytic granule transport along microtubules, and dynein-
CC mediated clustering to MTOC (PubMed:25762780). Interacts with HSPA5 and
CC stabilizes the interaction between HSPA5 and ERN1, leading to
CC suppression of ERN1-induced JNK activation and endoplasmic reticulum
CC stress-induced apoptosis (PubMed:21289099).
CC {ECO:0000250|UniProtKB:Q4QRL3, ECO:0000269|PubMed:21289099,
CC ECO:0000269|PubMed:25762780}.
CC -!- SUBUNIT: Homodimer (PubMed:25762780). Interacts with DOCK8
CC (PubMed:25762780). Interacts (via C-terminus) with intact microtubules
CC (PubMed:25762780). Interacts with dynein-dynactin motor complex
CC (PubMed:25762780). Interacts (via C-terminus) with HSPA5
CC (PubMed:21289099). {ECO:0000250|UniProtKB:Q4QRL3,
CC ECO:0000269|PubMed:21289099, ECO:0000269|PubMed:25762780}.
CC -!- INTERACTION:
CC A6NC98; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-347573, EBI-745073;
CC A6NC98; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-347573, EBI-8643161;
CC A6NC98; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-347573, EBI-11530605;
CC A6NC98; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-347573, EBI-10175300;
CC A6NC98; Q07002: CDK18; NbExp=3; IntAct=EBI-347573, EBI-746238;
CC A6NC98; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-347573, EBI-5453285;
CC A6NC98; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-347573, EBI-745369;
CC A6NC98; O60941-5: DTNB; NbExp=3; IntAct=EBI-347573, EBI-11984733;
CC A6NC98; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-347573, EBI-371876;
CC A6NC98; Q3B820: FAM161A; NbExp=3; IntAct=EBI-347573, EBI-719941;
CC A6NC98; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-347573, EBI-7225287;
CC A6NC98; P55040: GEM; NbExp=3; IntAct=EBI-347573, EBI-744104;
CC A6NC98; P08631-2: HCK; NbExp=3; IntAct=EBI-347573, EBI-9834454;
CC A6NC98; P09067: HOXB5; NbExp=3; IntAct=EBI-347573, EBI-3893317;
CC A6NC98; Q96AA8: JAKMIP2; NbExp=3; IntAct=EBI-347573, EBI-752007;
CC A6NC98; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-347573, EBI-2556193;
CC A6NC98; P20700: LMNB1; NbExp=3; IntAct=EBI-347573, EBI-968218;
CC A6NC98; Q03252: LMNB2; NbExp=3; IntAct=EBI-347573, EBI-2830427;
CC A6NC98; P25800: LMO1; NbExp=3; IntAct=EBI-347573, EBI-8639312;
CC A6NC98; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-347573, EBI-739832;
CC A6NC98; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-347573, EBI-744782;
CC A6NC98; Q13526: PIN1; NbExp=3; IntAct=EBI-347573, EBI-714158;
CC A6NC98; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-347573, EBI-2557469;
CC A6NC98; Q15311: RALBP1; NbExp=3; IntAct=EBI-347573, EBI-749285;
CC A6NC98; Q9Y580: RBM7; NbExp=3; IntAct=EBI-347573, EBI-746903;
CC A6NC98; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-347573, EBI-726876;
CC A6NC98; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-347573, EBI-747035;
CC A6NC98; Q96B97: SH3KBP1; NbExp=3; IntAct=EBI-347573, EBI-346595;
CC A6NC98; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-347573, EBI-8787464;
CC A6NC98; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-347573, EBI-765817;
CC A6NC98; Q99816: TSG101; NbExp=3; IntAct=EBI-347573, EBI-346882;
CC A6NC98; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-347573, EBI-744794;
CC A6NC98; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-347573, EBI-10241197;
CC A6NC98; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-347573, EBI-10687282;
CC A6NC98; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-347573, EBI-6116822;
CC A6NC98; O75604: USP2; NbExp=3; IntAct=EBI-347573, EBI-743272;
CC A6NC98; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-347573, EBI-14104088;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q4QRL3};
CC Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton,
CC microtubule organizing center {ECO:0000269|PubMed:25762780}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:21289099}. Golgi apparatus
CC {ECO:0000269|PubMed:21289099}. Cytoplasm {ECO:0000269|PubMed:21289099}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=A6NC98-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6NC98-2; Sequence=VSP_030962, VSP_030964;
CC Name=3;
CC IsoId=A6NC98-3; Sequence=VSP_030957, VSP_030958, VSP_030960,
CC VSP_030961;
CC Name=4;
CC IsoId=A6NC98-4; Sequence=VSP_030963;
CC Name=5;
CC IsoId=A6NC98-5; Sequence=VSP_030956, VSP_030959, VSP_030965;
CC Name=6;
CC IsoId=A6NC98-6; Sequence=VSP_035405, VSP_035406;
CC -!- TISSUE SPECIFICITY: Expressed in endothelium (at protein level)
CC (PubMed:21289099). Expressed in NK cells (at protein level)
CC (PubMed:25762780). {ECO:0000269|PubMed:21289099,
CC ECO:0000269|PubMed:25762780}.
CC -!- INDUCTION: By endoplasmic reticulum stress.
CC {ECO:0000269|PubMed:21289099}.
CC -!- SIMILARITY: Belongs to the CCDC88 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03417.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL136799; CAB66733.2; -; mRNA.
DR EMBL; AK090436; BAC03417.1; ALT_INIT; mRNA.
DR EMBL; AK095289; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AP003774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040232; AAH40232.1; -; mRNA.
DR EMBL; BC141866; AAI41867.1; -; mRNA.
DR EMBL; AY491401; AAR83719.1; -; mRNA.
DR CCDS; CCDS8072.2; -. [A6NC98-1]
DR RefSeq; NP_115627.6; NM_032251.5. [A6NC98-1]
DR AlphaFoldDB; A6NC98; -.
DR SMR; A6NC98; -.
DR BioGRID; 129505; 43.
DR IntAct; A6NC98; 43.
DR MINT; A6NC98; -.
DR STRING; 9606.ENSP00000349238; -.
DR iPTMnet; A6NC98; -.
DR PhosphoSitePlus; A6NC98; -.
DR BioMuta; CCDC88B; -.
DR EPD; A6NC98; -.
DR jPOST; A6NC98; -.
DR MassIVE; A6NC98; -.
DR MaxQB; A6NC98; -.
DR PaxDb; A6NC98; -.
DR PeptideAtlas; A6NC98; -.
DR PRIDE; A6NC98; -.
DR ProteomicsDB; 811; -. [A6NC98-1]
DR ProteomicsDB; 812; -. [A6NC98-2]
DR ProteomicsDB; 813; -. [A6NC98-3]
DR ProteomicsDB; 814; -. [A6NC98-4]
DR ProteomicsDB; 815; -. [A6NC98-5]
DR ProteomicsDB; 816; -. [A6NC98-6]
DR Antibodypedia; 15381; 49 antibodies from 11 providers.
DR DNASU; 283234; -.
DR Ensembl; ENST00000301897.5; ENSP00000301897.4; ENSG00000168071.22. [A6NC98-6]
DR Ensembl; ENST00000356786.10; ENSP00000349238.5; ENSG00000168071.22. [A6NC98-1]
DR GeneID; 283234; -.
DR KEGG; hsa:283234; -.
DR MANE-Select; ENST00000356786.10; ENSP00000349238.5; NM_032251.6; NP_115627.6.
DR UCSC; uc001nzy.4; human. [A6NC98-1]
DR CTD; 283234; -.
DR DisGeNET; 283234; -.
DR GeneCards; CCDC88B; -.
DR HGNC; HGNC:26757; CCDC88B.
DR HPA; ENSG00000168071; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 611205; gene.
DR neXtProt; NX_A6NC98; -.
DR OpenTargets; ENSG00000168071; -.
DR PharmGKB; PA162381820; -.
DR VEuPathDB; HostDB:ENSG00000168071; -.
DR eggNOG; KOG4643; Eukaryota.
DR GeneTree; ENSGT00940000162048; -.
DR HOGENOM; CLU_002567_1_0_1; -.
DR InParanoid; A6NC98; -.
DR OMA; SERDDHM; -.
DR OrthoDB; 59187at2759; -.
DR PhylomeDB; A6NC98; -.
DR TreeFam; TF320231; -.
DR PathwayCommons; A6NC98; -.
DR SignaLink; A6NC98; -.
DR BioGRID-ORCS; 283234; 22 hits in 1080 CRISPR screens.
DR ChiTaRS; CCDC88B; human.
DR GenomeRNAi; 283234; -.
DR Pharos; A6NC98; Tbio.
DR PRO; PR:A6NC98; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; A6NC98; protein.
DR Bgee; ENSG00000168071; Expressed in granulocyte and 97 other tissues.
DR ExpressionAtlas; A6NC98; baseline and differential.
DR Genevisible; A6NC98; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR043936; HOOK_N.
DR Pfam; PF19047; HOOK_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..1476
FT /note="Coiled-coil domain-containing protein 88B"
FT /id="PRO_0000317454"
FT REGION 427..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 253..481
FT /evidence="ECO:0000255"
FT COILED 720..1303
FT /evidence="ECO:0000255"
FT COMPBIAS 570..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4QRL3"
FT MOD_RES 1379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4QRL3"
FT VAR_SEQ 1..1337
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_035405"
FT VAR_SEQ 1..864
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030956"
FT VAR_SEQ 1..351
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030957"
FT VAR_SEQ 352..403
FT /note="QLEEERVLSGVLEASKALLEEQLEAARERCARLHETQRENLLLRTRLGEAHA
FT -> MGGAGALGGAGGVQGAAGRAAGGCPRALRPAARDPAREPAAANPAGRGPCGK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030958"
FT VAR_SEQ 865..872
FT /note="REKEALQA -> MKNRGLRE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030959"
FT VAR_SEQ 955..972
FT /note="LRQGPAGLGPKKRAEPQL -> VMPARLGAGGHATLPSIP (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030960"
FT VAR_SEQ 973..1476
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030961"
FT VAR_SEQ 987..1034
FT /note="NAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQA ->
FT VSVGPQWALGRCPVQCECGSTVDPGLGGIPCSVSVDSQWARGWGCPMQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_030962"
FT VAR_SEQ 1019..1136
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_030963"
FT VAR_SEQ 1035..1476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_030964"
FT VAR_SEQ 1320..1476
FT /note="VKRLMRPRREGGPPGGLRLGADGAGSTESLGGPPETELPEGREADGTGSPSP
FT APMRRAQSSLCLRDETLAGGQRRKLSSRFPVGRSSESFSPGDTPRQRFRQRHPGPLGAP
FT VSHSKGPGVGWENSAETLQEHETDANREGPEVQEPEKRPLTPSLSQ -> GPLPRHPCA
FT GPRAPSACGMRPWQAGSGGNSAQGSRWGEALSHSALGTPLGNDSDSAIQAPWGRPSPTA
FT KDLVWDGRTPLRPCRNTKQMPTERALRYRNRRNVPSPHPSASDTVGTAGLGVQPSRHWS
FT VSGGPRQPKSSGSQGPQGESLDKEAWALRSSTVSAGARRWSWDECVDRGDGWPPRAAPG
FT WSSGSSRWLPLRQRSLGDPPAEGGWQELAREPPALSRWEAESQCWGTVAWADLEP (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030965"
FT VAR_SEQ 1338..1367
FT /note="LGADGAGSTESLGGPPETELPEGREADGTG -> MPCAARSRSSWRRSWTNT
FT ACWSLCPCPGPR (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_035406"
FT VARIANT 193
FT /note="D -> E (in dbSNP:rs647152)"
FT /id="VAR_038523"
FT VARIANT 639
FT /note="W -> R (in dbSNP:rs685870)"
FT /id="VAR_038524"
FT VARIANT 886
FT /note="D -> A (in dbSNP:rs1318165)"
FT /evidence="ECO:0000269|PubMed:12693554,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_038525"
FT CONFLICT 291
FT /note="L -> W (in Ref. 1; BAC03417)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="T -> I (in Ref. 5; AAI41867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1476 AA; 164809 MW; 4DB82F199F224EFC CRC64;
MEGGKGPRLR DFLSGSLATW ALGLAGLVGE AEDSEGEEEE EEEEPPLWLE KRFLRLSDGA
LLLRVLGIIA PSSRGGPRML RGLDGPAAWR VWNLNHLWGR LRDFYQEELQ LLILSPPPDL
QTLGFDPLSE EAVEQLEGVL RLLLGASVQC EHRELFIRHI QGLSLEVQSE LAAAIQEVTQ
PGAGVVLALS GPDPGELAPA ELEMLSRSLM GTLSKLARER DLGAQRLAEL LLEREPLCLR
PEAPSRAPAE GPSHHLALQL ANAKAQLRRL RQELEEKAEL LLDSQAEVQG LEAEIRRLRQ
EAQALSGQAK RAELYREEAE ALRERAGRLP RLQEELRRCR ERLQAAEAYK SQLEEERVLS
GVLEASKALL EEQLEAARER CARLHETQRE NLLLRTRLGE AHAELDSLRH QVDQLAEENV
ELELELQRSL EPPPGSPGEA PLAGAAPSLQ DEVREAEAGR LRTLERENRE LRGLLQVLQG
QPGGQHPLLE APREDPVLPV LEEAPQTPVA FDHSPQGLVQ KARDGGPQAL DLAPPALDSV
LEASAECPQA PDSDPQEAES PLQAAAMDPQ ASDWSPQESG SPVETQESPE KAGRRSSLQS
PASVAPPQGP GTKIQAPQLL GGETEGREAP QGELVPEAWG LRQEGPEHKP GPSEPSSVQL
EEQEGPNQGL DLATGQAEAR EHDQRLEGTV RDPAWQKPQQ KSEGALEVQV WEGPIPGESL
ASGVAEQEAL REEVAQLRRK AEALGDELEA QARKLEAQNT EAARLSKELA QARRAEAEAH
REAEAQAWEQ ARLREAVEAA GQELESASQE REALVEALAA AGRERRQWER EGSRLRAQSE
AAEERMQVLE SEGRQHLEEA ERERREKEAL QAELEKAVVR GKELGDRLEH LQRELEQAAL
ERQEFLREKE SQHQRYQGLE QRLEAELQAA ATSKEEALME LKTRALQLEE ELFQLRQGPA
GLGPKKRAEP QLVETQNVRL IEVERSNAML VAEKAALQGQ LQHLEGQLGS LQGRAQELLL
QSQRAQEHSS RLQAEKSVLE IQGQELHRKL EVLEEEVRAA RQSQEETRGQ QQALLRDHKA
LAQLQRRQEA ELEGLLVRHR DLKANMRALE LAHRELQGRH EQLQAQRASV EAQEVALLAE
RERLMQDGHR QRGLEEELRR LQSEHDRAQM LLAELSRERG ELQGERGELR GRLARLELER
AQLEMQSQQL RESNQQLDLS ACRLTTQCEL LTQLRSAQEE ENRQLLAEVQ ALSRENRELL
ERSLESRDHL HREQREYLDQ LNALRREKQK LVEKIMDQYR VLEPVPLPRT KKGSWLADKV
KRLMRPRREG GPPGGLRLGA DGAGSTESLG GPPETELPEG READGTGSPS PAPMRRAQSS
LCLRDETLAG GQRRKLSSRF PVGRSSESFS PGDTPRQRFR QRHPGPLGAP VSHSKGPGVG
WENSAETLQE HETDANREGP EVQEPEKRPL TPSLSQ
