ID SH3K1_RAT Reviewed; 709 AA.
AC Q925Q9; Q925R0; Q925R1; Q925R2; Q925R3; Q9JKQ0; Q9JKQ1; Q9JLU9;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=SH3 domain-containing kinase-binding protein 1;
DE AltName: Full=Regulator of ubiquitous kinase;
DE Short=Ruk;
DE AltName: Full=SH3-containing, expressed in tumorigenic astrocytes;
GN Name=Sh3kbp1; Synonyms=Ruk, Seta;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), AND INTERACTION
RP WITH PI3KR3.
RC TISSUE=Cerebellum, and Skin;
RX PubMed=10921882; DOI=10.1093/emboj/19.15.4015;
RA Gout I., Middleton G., Adu J., Ninkina N.N., Drobot L.B., Filonenko V.,
RA Matsuka G., Davies A.M., Waterfield M., Buchman V.L.;
RT "Negative regulation of PI 3-kinase by Ruk, a novel adaptor protein.";
RL EMBO J. 19:4015-4025(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
RX PubMed=11302255; DOI=10.1093/neuonc/2.1.6;
RA Boegler O., Furnari F.B., Kindler-Roehrborn A., Sykes V.W., Yung R.,
RA Huang H.-J.S., Cavenee W.K.;
RT "SETA: a novel SH3 domain-containing adapter molecule associated with
RT malignancy in astrocytes.";
RL Neuro-oncol. 2:6-15(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 65-709 (ISOFORMS 1 AND 2), AND INTERACTION
RP WITH CBL; GRB2 AND SHKBP1.
RX PubMed=11152963; DOI=10.1016/s0898-6568(00)00129-7;
RA Borinstein S.C., Hyatt M.A., Sykes V.W., Straub R.E., Lipkowitz S.,
RA Boulter J., Boegler O.;
RT "SETA is a multifunctional adapter protein with three SH3 domains that
RT binds Grb2, Cbl, and the novel SB1 proteins.";
RL Cell. Signal. 12:769-779(2000).
RN [4]
RP INTERACTION WITH PDCD6IP, AND SUBCELLULAR LOCATION.
RX PubMed=12771190; DOI=10.1242/jcs.00522;
RA Schmidt M.H., Chen B., Randazzo L.M., Boegler O.;
RT "SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse
RT cytoskeletal elements, including FAKs, and modulate cell adhesion.";
RL J. Cell Sci. 116:2845-2855(2003).
RN [5]
RP INTERACTION WITH ARHGAP27.
RC STRAIN=Sprague-Dawley;
RX PubMed=15147912; DOI=10.1016/j.febslet.2004.03.101;
RA Sakakibara T., Nemoto Y., Nukiwa T., Takeshima H.;
RT "Identification and characterization of a novel Rho GTPase activating
RT protein implicated in receptor-mediated endocytosis.";
RL FEBS Lett. 566:294-300(2004).
RN [6]
RP INTERACTION WITH MAGI2, AND SUBCELLULAR LOCATION.
RX PubMed=16751601; DOI=10.1093/jb/mvj105;
RA Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K.,
RA Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y.;
RT "CIN85 is localized at synapses and forms a complex with S-SCAM via
RT dendrin.";
RL J. Biochem. 139:931-939(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-555 AND SER-631,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 (ISOFORM 7), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Adapter protein involved in regulating diverse signal
CC transduction pathways. Involved in the regulation of endocytosis and
CC lysosomal degradation of ligand-induced receptor tyrosine kinases,
CC including EGFR and MET/hepatocyte growth factor receptor, through an
CC association with CBL and endophilins. The association with CBL, and
CC thus the receptor internalization, may be inhibited by an interaction
CC with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent
CC endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-
CC kinase activity by interaction with its regulatory subunit (By
CC similarity). May be involved in regulation of cell adhesion; promotes
CC the interaction between TTK2B and PDCD6IP. May be involved in the
CC regulation of cellular stress response via the MAPK pathways through
CC its interaction with MAP3K4. Is involved in modulation of tumor
CC necrosis factor mediated apoptosis. Plays a role in the regulation of
CC cell morphology and cytoskeletal organization. Required in the control
CC of cell shape and migration (By similarity). Has an essential role in
CC the stimulation of B cell activation (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q96B97}.
CC -!- SUBUNIT: Can self-associate and form homotetramers (By similarity).
CC Interacts with MAGI2, PDCD6IP, CBL, GRB2 and PI3KR3. Interacts with
CC CD2, F-actin capping protein, EGFR, MET, BLNK, MAP3K4, SPRY2, ARHGAP17,
CC CRK, BCAR1, SOS1, ASAP1, ARAP3, HIP1R, SYNJ2, INPP5D and STAP1.
CC Interacts with CBL and CBLB, but does not interact with CBLC. Two
CC molecules of SH3KBP1 seem to bind through their respective SH3 1 domain
CC to one molecule of CBLB. The interaction with CBL or CBLB and EGFR is
CC increased upon EGF stimulation. The interaction with CBL is attenuated
CC by PDCD6IP. Interacts through its proline-rich region with the SH3
CC domain of endophilins SH3GL1, SH3GL2 and SH3GL3. The SH3KBP1-endophilin
CC complex seems to associate with a complex containing the phosphorylated
CC receptor (EGFR or MET) and phosphorylated CBL. Probably associates with
CC ASAP1 and phosphorylated EGFR. Probably part of a complex consisting of
CC at least SH3KBP1, ASAP1 and ARAP3. Interacts with focal adhesion
CC kinases PTK2/FAK1 and PTK2B/PYK2, probably as a dimer. Interacts with
CC DAB2 and probably associates with chathrin through its interaction with
CC DAB2. Part of a complex consisting of SH3KBP1, DAB2, and clathrin heavy
CC chain. DAB2 and clathrin dissociate from SH3KBP1 following growth
CC factor treatment, enabling interaction with CBL. Interacts with DDN and
CC probably associates with MAGI2 through its interaction with DDN.
CC Interacts with the SH3 domains of SRC tyrosine-protein kinases SRC,
CC LCK, LYN, FGR, FYN and HCK. Interacts with TRADD, BIRC2, TRAF1, TRAF2
CC and TNFR1, and the association with a TNFR1-associated complex upon
CC stimulation with TNF-alpha seems to be mediated by SRC. Probably part
CC of a complex consisting of at least SH3KBP1, ASAP1 and ARAP3 (By
CC similarity). Interacts with ARHGAP27. Interacts (via SH3 domains) with
CC SHKBP1 (via PXXXPR motifs) (PubMed:11152963). Interaction with CBL is
CC abolished in the presence of SHKBP1 (By similarity). Interacts (via SH3
CC domains) with ZFP36 (via extreme C-terminal region). Interacts with
CC MAP3K4; this interaction enhances the association with ZFP36 (By
CC similarity). {ECO:0000250|UniProtKB:Q8R550,
CC ECO:0000250|UniProtKB:Q96B97, ECO:0000269|PubMed:10921882,
CC ECO:0000269|PubMed:11152963, ECO:0000269|PubMed:12771190,
CC ECO:0000269|PubMed:15147912, ECO:0000269|PubMed:16751601}.
CC -!- INTERACTION:
CC Q925Q9; Q15811-2: ITSN1; Xeno; NbExp=4; IntAct=EBI-8020091, EBI-8052395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96B97}.
CC Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Peripheral
CC membrane protein. Synapse, synaptosome. Cell junction, focal adhesion.
CC Note=Localized in endocytic vesicles containing clustered receptors.
CC Colocalizes with ASAP1 in vesicular structures. Colocalized with actin
CC microfilaments and focal adhesions. Colocalized with MAGI2 in
CC synaptosomes. Colocalizes with ZFP36 in the cytoplasm (By similarity).
CC Translocation to EGFR containing vesicles upon EGF stimulation is
CC inhibited in the presence of SH3KBP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8R550, ECO:0000250|UniProtKB:Q96B97}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q925Q9-1; Sequence=Displayed;
CC Name=2; Synonyms=Ruk-l;
CC IsoId=Q925Q9-2; Sequence=VSP_007512;
CC Name=3; Synonyms=Ruk-m3;
CC IsoId=Q925Q9-3; Sequence=VSP_007516;
CC Name=4; Synonyms=Ruk-h;
CC IsoId=Q925Q9-4; Sequence=VSP_007515;
CC Name=5; Synonyms=Ruk-s;
CC IsoId=Q925Q9-5; Sequence=VSP_007517;
CC Name=6; Synonyms=Ruk-m1;
CC IsoId=Q925Q9-6; Sequence=VSP_007514;
CC Name=7;
CC IsoId=Q925Q9-7; Sequence=VSP_007513, VSP_007512;
CC -!- TISSUE SPECIFICITY: Highly expressed in spinal cord.
CC -!- PTM: Monoubiquitinated by CBL and CBLB after EGF stimulation; probably
CC on its C-terminus. {ECO:0000250}.
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DR EMBL; AF255884; AAK51625.1; -; mRNA.
DR EMBL; AF255885; AAK51626.1; -; mRNA.
DR EMBL; AF255886; AAK51627.1; -; mRNA.
DR EMBL; AF255887; AAK51628.1; -; mRNA.
DR EMBL; AF255888; AAK51629.1; -; mRNA.
DR EMBL; AF131867; AAF36522.1; -; mRNA.
DR EMBL; AF230519; AAF43035.1; -; mRNA.
DR EMBL; AF230520; AAF43036.1; -; mRNA.
DR RefSeq; NP_445812.1; NM_053360.2. [Q925Q9-2]
DR RefSeq; XP_006256992.1; XM_006256930.3. [Q925Q9-3]
DR RefSeq; XP_006256993.1; XM_006256931.1. [Q925Q9-1]
DR RefSeq; XP_008771422.1; XM_008773200.2. [Q925Q9-4]
DR RefSeq; XP_008771423.1; XM_008773201.2.
DR RefSeq; XP_008771424.1; XM_008773202.2. [Q925Q9-4]
DR RefSeq; XP_017457655.1; XM_017602166.1.
DR AlphaFoldDB; Q925Q9; -.
DR SMR; Q925Q9; -.
DR IntAct; Q925Q9; 5.
DR MINT; Q925Q9; -.
DR STRING; 10116.ENSRNOP00000006741; -.
DR iPTMnet; Q925Q9; -.
DR PhosphoSitePlus; Q925Q9; -.
DR jPOST; Q925Q9; -.
DR PaxDb; 10116-ENSRNOP00000006741; -.
DR Ensembl; ENSRNOT00000006741.8; ENSRNOP00000006741.7; ENSRNOG00000004322.9. [Q925Q9-1]
DR Ensembl; ENSRNOT00000096669.1; ENSRNOP00000083463.1; ENSRNOG00000004322.9. [Q925Q9-3]
DR Ensembl; ENSRNOT00055047129; ENSRNOP00055038745; ENSRNOG00055026871. [Q925Q9-1]
DR Ensembl; ENSRNOT00060032668; ENSRNOP00060026670; ENSRNOG00060018228. [Q925Q9-1]
DR Ensembl; ENSRNOT00065021818; ENSRNOP00065016896; ENSRNOG00065013202. [Q925Q9-1]
DR GeneID; 84357; -.
DR KEGG; rno:84357; -.
DR AGR; RGD:620904; -.
DR CTD; 30011; -.
DR RGD; 620904; Sh3kbp1.
DR eggNOG; KOG4348; Eukaryota.
DR GeneTree; ENSGT00940000155886; -.
DR HOGENOM; CLU_024255_1_0_1; -.
DR InParanoid; Q925Q9; -.
DR OMA; QHITKNR; -.
DR OrthoDB; 2972088at2759; -.
DR PhylomeDB; Q925Q9; -.
DR TreeFam; TF350191; -.
DR Reactome; R-RNO-182971; EGFR downregulation.
DR Reactome; R-RNO-6807004; Negative regulation of MET activity.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-8866376; Reelin signalling pathway.
DR Reactome; R-RNO-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR PRO; PR:Q925Q9; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000004322; Expressed in heart and 20 other cell types or tissues.
DR ExpressionAtlas; Q925Q9; baseline and differential.
DR Genevisible; Q925Q9; RN.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0050871; P:positive regulation of B cell activation; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; TAS:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR CDD; cd12052; SH3_CIN85_1; 1.
DR CDD; cd12055; SH3_CIN85_2; 1.
DR CDD; cd12057; SH3_CIN85_3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR InterPro; IPR035770; CIN85_SH3_1.
DR InterPro; IPR035771; CIN85_SH3_2.
DR InterPro; IPR035772; CIN85_SH3_3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14167:SF6; SH3 DOMAIN-CONTAINING KINASE-BINDING PROTEIN 1; 1.
DR Pfam; PF14604; SH3_9; 3.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50002; SH3; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cell junction; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; SH3-binding; Synapse; Synaptosome;
KW Ubl conjugation.
FT CHAIN 1..709
FT /note="SH3 domain-containing kinase-binding protein 1"
FT /id="PRO_0000097730"
FT DOMAIN 1..58
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 98..157
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 311..372
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..708
FT /evidence="ECO:0000255"
FT COMPBIAS 222..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R550"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R550"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B97"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B97"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96B97"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B97"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B97"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..652
FT /note="MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNF
FT VREIKKDVKKDLLSNKAPEKPMHDVSSGNSLLSSETILRTNKRGERRRRRCQVAFSYLP
FT QNDDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKELSGESDELGISQDEQL
FT SKSRPEGFLPASLLPFPAHGAKGKTTFEGTILYRAAPGKTEGHRRYYSLRETTGSESDG
FT GDSSSTKSEGANGTVATAAIQPKKVKGVGFGDIFKDKPIKLRPRSIEVENDFLPVEKTI
FT GKKLPPATSTPDPSKTEMDSRTKTKDYCKVIFPYEAQNDDELTIKEGDIVTLINKDCID
FT VGWWEGELNGRRGVFPDNFVKLLPSDFDKEGNRPKKPPPPSAPVIKQGAGTTERKHEIK
FT KIPPERPETLPNRTEEKERPEREPKLDLQKPSVPAIPPKKPRPPKTNSLNRPGVLPPRR
FT PERPVGPLTHTRGDSSKIDLAGSTLSGILDKDLSDRSNDIDLEGFDSVISSTEKLSHPT
FT TSRPKATGRRPPSQSLTSSSLSSPDIFDSPSPEEDKEEHISLAHRGIDVSKKTSRTVTI
FT SQVSDNKASLPPKPGTMAAASSGPASLSSVASSPMSSSLGTAGQRASSPSLFSAEGKAK
FT TESAVSSQAA -> MGEEVSSGGKNISTEQASCGASQPRGSQTLWSFPLEWRNYNWEEV
FT TSSYINPRP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10921882"
FT /id="VSP_007517"
FT VAR_SEQ 1..599
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10921882"
FT /id="VSP_007515"
FT VAR_SEQ 1..305
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:10921882"
FT /id="VSP_007514"
FT VAR_SEQ 1..286
FT /note="MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNF
FT VREIKKDVKKDLLSNKAPEKPMHDVSSGNSLLSSETILRTNKRGERRRRRCQVAFSYLP
FT QNDDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKELSGESDELGISQDEQL
FT SKSRPEGFLPASLLPFPAHGAKGKTTFEGTILYRAAPGKTEGHRRYYSLRETTGSESDG
FT GDSSSTKSEGANGTVATAAIQPKKVKGVGFGDIFKDKPIKLRPRSIEVENDFLPVEK
FT -> MGEE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10921882"
FT /id="VSP_007516"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:11302255"
FT /id="VSP_007513"
FT VAR_SEQ 174..217
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10921882,
FT ECO:0000303|PubMed:11152963, ECO:0000303|PubMed:11302255"
FT /id="VSP_007512"
FT CONFLICT 99
FT /note="R -> Q (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="K -> Q (in Ref. 3; AAF43035/AAF43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="L -> V (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="T -> S (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="S -> F (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT MOD_RES Q925Q9-2:183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q925Q9-7:110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 709 AA; 78086 MW; B995308497072064 CRC64;
MVEAIVEFDY QAQHDDELTI SVGEVITNIR KEDGGWWEGQ INGRRGLFPD NFVREIKKDV
KKDLLSNKAP EKPMHDVSSG NSLLSSETIL RTNKRGERRR RRCQVAFSYL PQNDDELELK
VGDIIEVVGE VEEGWWEGVL NGKTGMFPSN FIKELSGESD ELGISQDEQL SKSRPEGFLP
ASLLPFPAHG AKGKTTFEGT ILYRAAPGKT EGHRRYYSLR ETTGSESDGG DSSSTKSEGA
NGTVATAAIQ PKKVKGVGFG DIFKDKPIKL RPRSIEVEND FLPVEKTIGK KLPPATSTPD
PSKTEMDSRT KTKDYCKVIF PYEAQNDDEL TIKEGDIVTL INKDCIDVGW WEGELNGRRG
VFPDNFVKLL PSDFDKEGNR PKKPPPPSAP VIKQGAGTTE RKHEIKKIPP ERPETLPNRT
EEKERPEREP KLDLQKPSVP AIPPKKPRPP KTNSLNRPGV LPPRRPERPV GPLTHTRGDS
SKIDLAGSTL SGILDKDLSD RSNDIDLEGF DSVISSTEKL SHPTTSRPKA TGRRPPSQSL
TSSSLSSPDI FDSPSPEEDK EEHISLAHRG IDVSKKTSRT VTISQVSDNK ASLPPKPGTM
AAASSGPASL SSVASSPMSS SLGTAGQRAS SPSLFSAEGK AKTESAVSSQ AAIEELKMQV
RELRTIIETM KDQQKREIKQ LLSELDEEKK IRLRLQMEVN DIKKALQSK
//
