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Database: UniProt/SWISS-PROT
Entry: HS90B_BOVIN
LinkDB: HS90B_BOVIN
Original site: HS90B_BOVIN 
ID   HS90B_BOVIN             Reviewed;         724 AA.
AC   Q76LV1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Heat shock protein HSP 90-beta;
GN   Name=HSP90AB1; Synonyms=HSPCB;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RA   Watanabe A., Uchida I., Fujimoto Y., Nakata K., Oikawa S.;
RT   "cDNA sequences of two isoforms of bovine heat-shock protein 90.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC       maintenance and proper regulation of specific target proteins involved
CC       for instance in cell cycle control and signal transduction. Undergoes a
CC       functional cycle linked to its ATPase activity. This cycle probably
CC       induces conformational changes in the client proteins, thereby causing
CC       their activation. Interacts dynamically with various co-chaperones that
CC       modulate its substrate recognition, ATPase cycle and chaperone
CC       function. Engages with a range of client protein classes via its
CC       interaction with various co-chaperone proteins or complexes, that act
CC       as adapters, simultaneously able to interact with the specific client
CC       and the central chaperone itself. Recruitment of ATP and co-chaperone
CC       followed by client protein forms a functional chaperone. After the
CC       completion of the chaperoning process, properly folded client protein
CC       and co-chaperone leave HSP90 in an ADP-bound partially open
CC       conformation and finally, ADP is released from HSP90 which acquires an
CC       open conformation for the next cycle. Apart from its chaperone
CC       activity, it also plays a role in the regulation of the transcription
CC       machinery. HSP90 and its co-chaperones modulate transcription at least
CC       at three different levels. They first alter the steady-state levels of
CC       certain transcription factors in response to various physiological
CC       cues. Second, they modulate the activity of certain epigenetic
CC       modifiers, such as histone deacetylases or DNA methyl transferases, and
CC       thereby respond to the change in the environment. Third, they
CC       participate in the eviction of histones from the promoter region of
CC       certain genes and thereby turn on gene expression. Antagonizes STUB1-
CC       mediated inhibition of TGF-beta signaling via inhibition of STUB1-
CC       mediated SMAD3 ubiquitination and degradation. Promotes cell
CC       differentiation by chaperoning BIRC2 and thereby protecting from auto-
CC       ubiquitination and degradation by the proteasomal machinery. Main
CC       chaperone involved in the phosphorylation/activation of the STAT1 by
CC       chaperoning both JAK2 and PRKCE under heat shock and in turn, activates
CC       its own transcription. Involved in the translocation into ERGIC
CC       (endoplasmic reticulum-Golgi intermediate compartment) of leaderless
CC       cargos (lacking the secretion signal sequence) such as the interleukin
CC       1/IL-1; the translocation process is mediated by the cargo receptor
CC       TMED10. {ECO:0000250|UniProtKB:P08238}.
CC   -!- ACTIVITY REGULATION: In the resting state, through the dimerization of
CC       its C-terminal domain, HSP90 forms a homodimer which is defined as the
CC       open conformation. Upon ATP-binding, the N-terminal domain undergoes
CC       significant conformational changes and comes in contact to form an
CC       active closed conformation. After HSP90 finishes its chaperoning tasks
CC       of assisting the proper folding, stabilization and activation of client
CC       proteins under the active state, ATP molecule is hydrolyzed to ADP
CC       which then dissociates from HSP90 and directs the protein back to the
CC       resting state. {ECO:0000250|UniProtKB:P08238}.
CC   -!- SUBUNIT: Monomer. Homodimer (By similarity). Forms a complex with CDK6
CC       and CDC37. Interacts with UNC45A; binding to UNC45A involves 2 UNC45A
CC       monomers per HSP90AB1 dimer (By similarity). Interacts with CHORDC1 (By
CC       similarity). Interacts with DNAJC7. Interacts with FKBP4. May interact
CC       with NWD1. Interacts with SGTA. Interacts with HSF1 in an ATP-dependent
CC       manner. Interacts with MET; the interaction suppresses MET kinase
CC       activity. Interacts with ERBB2 in an ATP-dependent manner; the
CC       interaction suppresses ERBB2 kinase activity. Interacts with HIF1A,
CC       KEAP1 and RHOBTB2. Interacts with STUB1 and SMAD3. Interacts with XPO1
CC       and AHSA1. Interacts with BIRC2. Interacts with KCNQ4; promotes cell
CC       surface expression of KCNQ4. Interacts with BIRC2; prevents auto-
CC       ubiquitination and degradation of its client protein BIRC2. Interacts
CC       with NOS3. Interacts with AHR; interaction is inhibited by HSP90AB1
CC       phosphorylation on Ser-226 and Ser-255. Interacts with STIP1 and CDC37;
CC       upon SMYD2-dependent methylation. Interacts with JAK2 and PRKCE;
CC       promotes functional activation in a heat shock-dependent manner.
CC       Interacts with HSP90AA1; interaction is constitutive. HSP90AB1-CDC37
CC       chaperone complex interacts with inactive MAPK7 (via N-terminal half)
CC       in resting cells; the interaction is MAP2K5-independent and prevents
CC       from ubiquitination and proteasomal degradation. Interacts with CDC25A;
CC       prevents heat shock-mediated CDC25A degradation and contributes to cell
CC       cycle progression. Interacts with TP53 (via DNA binding domain);
CC       suppresses TP53 aggregation and prevents from irreversible thermal
CC       inactivation. Interacts with TGFB1 processed form (LAP); inhibits
CC       latent TGFB1 activation (By similarity). Interacts with TRIM8; prevents
CC       nucleus translocation of phosphorylated STAT3 and HSP90AB1 (By
CC       similarity). Interacts with NR3C1 (via domain NR LBD) and NR1D1 (via
CC       domain NR LBD) (By similarity). Interacts with PDCL3 (By similarity).
CC       Interacts with TTC4 (via TPR repeats) (By similarity). Interacts with
CC       IL1B; the interaction facilitates cargo translocation into the ERGIC
CC       (By similarity). {ECO:0000250|UniProtKB:P08238,
CC       ECO:0000250|UniProtKB:P11499, ECO:0000250|UniProtKB:P34058}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08238}.
CC       Melanosome {ECO:0000250|UniProtKB:P08238}. Nucleus
CC       {ECO:0000250|UniProtKB:P08238}. Secreted
CC       {ECO:0000250|UniProtKB:P08238}. Cell membrane
CC       {ECO:0000250|UniProtKB:P08238}. Dynein axonemal particle
CC       {ECO:0000250|UniProtKB:Q6AZV1}. Note=Translocates with BIRC2 from the
CC       nucleus to the cytoplasm during differentiation. Secreted when
CC       associated with TGFB1 processed form (LAP).
CC       {ECO:0000250|UniProtKB:P08238}.
CC   -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC       repeat-containing proteins. {ECO:0000250|UniProtKB:P07900}.
CC   -!- PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).
CC       {ECO:0000250|UniProtKB:P08238}.
CC   -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P08238}.
CC   -!- PTM: S-nitrosylated; negatively regulates the ATPase activity.
CC       {ECO:0000250|UniProtKB:P08238}.
CC   -!- PTM: Phosphorylation at Tyr-301 by SRC is induced by
CC       lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255 inhibits AHR
CC       interaction. {ECO:0000250|UniProtKB:P08238}.
CC   -!- PTM: Methylated by SMYD2; facilitates dimerization and chaperone
CC       complex formation; promotes cancer cell proliferation.
CC       {ECO:0000250|UniProtKB:P08238}.
CC   -!- PTM: Cleaved following oxidative stress resulting in HSP90AB1 protein
CC       radicals formation; disrupts the chaperoning function and the
CC       degradation of its client proteins. {ECO:0000250|UniProtKB:P08238}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; AB072369; BAC82488.1; -; mRNA.
DR   EMBL; BT025368; ABF57324.1; -; mRNA.
DR   RefSeq; NP_001073105.1; NM_001079637.1.
DR   AlphaFoldDB; Q76LV1; -.
DR   SMR; Q76LV1; -.
DR   BioGRID; 613028; 4.
DR   IntAct; Q76LV1; 1.
DR   STRING; 9913.ENSBTAP00000072629; -.
DR   GlyCosmos; Q76LV1; 2 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000001034; -.
DR   PeptideAtlas; Q76LV1; -.
DR   Ensembl; ENSBTAT00000081693.1; ENSBTAP00000072629.1; ENSBTAG00000000778.5.
DR   GeneID; 767874; -.
DR   KEGG; bta:767874; -.
DR   CTD; 3326; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000778; -.
DR   VGNC; VGNC:55918; HSP90AB1.
DR   eggNOG; KOG0019; Eukaryota.
DR   GeneTree; ENSGT01020000230401; -.
DR   InParanoid; Q76LV1; -.
DR   OMA; TRMKAEQ; -.
DR   OrthoDB; 547579at2759; -.
DR   Reactome; R-BTA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR   Reactome; R-BTA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-BTA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-BTA-3371511; HSF1 activation.
DR   Reactome; R-BTA-3371568; Attenuation phase.
DR   Reactome; R-BTA-3371571; HSF1-dependent transactivation.
DR   Reactome; R-BTA-399954; Sema3A PAK dependent Axon repulsion.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Reactome; R-BTA-844456; The NLRP3 inflammasome.
DR   Reactome; R-BTA-8937144; Aryl hydrocarbon receptor signalling.
DR   Reactome; R-BTA-8939211; ESR-mediated signaling.
DR   Reactome; R-BTA-9013418; RHOBTB2 GTPase cycle.
DR   Reactome; R-BTA-9018519; Estrogen-dependent gene expression.
DR   PRO; PR:Q76LV1; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000000778; Expressed in granulosa cell and 102 other cell types or tissues.
DR   ExpressionAtlas; Q76LV1; baseline and differential.
DR   GO; GO:0034751; C:aryl hydrocarbon receptor complex; ISS:UniProtKB.
DR   GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
DR   GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0044294; C:dendritic growth cone; IEA:Ensembl.
DR   GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:1990565; C:HSP90-CDC37 chaperone complex; IEA:Ensembl.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0043008; F:ATP-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0097718; F:disordered domain specific binding; IBA:GO_Central.
DR   GO; GO:0070182; F:DNA polymerase binding; IEA:Ensembl.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:1990226; F:histone methyltransferase binding; IEA:Ensembl.
DR   GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR   GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0019887; F:protein kinase regulator activity; IEA:Ensembl.
DR   GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:1901389; P:negative regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR   GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
DR   GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0097435; P:supramolecular fiber organization; IEA:Ensembl.
DR   GO; GO:1905323; P:telomerase holoenzyme complex assembly; IEA:Ensembl.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IEA:Ensembl.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:Ensembl.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11528:SF79; HEAT SHOCK PROTEIN HSP 90-BETA-RELATED; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cell membrane; Chaperone; Cytoplasm;
KW   Glycoprotein; Membrane; Methylation; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; S-nitrosylation; Secreted;
KW   Stress response; Ubl conjugation.
FT   CHAIN           1..724
FT                   /note="Heat shock protein HSP 90-beta"
FT                   /id="PRO_0000247933"
FT   REGION          1..527
FT                   /note="Interaction with TP53"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   REGION          1..214
FT                   /note="Interaction with BIRC2"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   REGION          9..231
FT                   /note="Interaction with NR3C1"
FT                   /evidence="ECO:0000250|UniProtKB:P11499"
FT   REGION          215..552
FT                   /note="Interaction with AHSA1"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   REGION          222..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..608
FT                   /note="Interaction with NR3C1"
FT                   /evidence="ECO:0000250|UniProtKB:P11499"
FT   REGION          620..723
FT                   /note="Interaction with NR1D1"
FT                   /evidence="ECO:0000250|UniProtKB:P11499"
FT   REGION          694..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           720..724
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        241..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            126..127
FT                   /note="Cleaved under oxidative stress"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         219
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11499"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11499"
FT   MOD_RES         297
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         301
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         305
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P11499"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         399
FT                   /note="N6-malonyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         435
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         479
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         481
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         484
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P11499"
FT   MOD_RES         531
FT                   /note="N6-methylated lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         531
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11499"
FT   MOD_RES         574
FT                   /note="N6-methylated lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         577
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11499"
FT   MOD_RES         590
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         624
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11499"
FT   MOD_RES         669
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   MOD_RES         718
FT                   /note="Phosphoserine; by PLK2 and PLK3"
FT                   /evidence="ECO:0000250|UniProtKB:P08238"
FT   CARBOHYD        434
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        452
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   724 AA;  83253 MW;  F5C0C65A143CCBD8 CRC64;
     MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT
     DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLVN NLGTIAKSGT KAFMEALQAG
     ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK
     VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE
     DKDDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
     YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV
     FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA
     EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ
     KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG
     LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
     NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE
     TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP SAAVPDEIPP LEGDEDASRM
     EEVD
//
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