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SH3K1_RAT
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   03-AUG-2022, entry version 152.
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. [Q925Q9-4]
DR   RefSeq; XP_008771424.1; XM_008773202.2. [Q925Q9-4]
DR   RefSeq; XP_017457655.1; XM_017602166.1. [Q925Q9-6]
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; Q925Q9; -.
DR   PRIDE; Q925Q9; -.
DR   Ensembl; ENSRNOT00000006741; ENSRNOP00000006741; ENSRNOG00000004322. [Q925Q9-1]
DR   Ensembl; ENSRNOT00000096669; ENSRNOP00000083463; ENSRNOG00000004322. [Q925Q9-3]
DR   GeneID; 84357; -.
DR   KEGG; rno:84357; -.
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   OrthoDB; 1577081at2759; -.
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 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   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   InterPro; IPR028506; Sorbin_SH3.
DR   PANTHER; PTHR14167:SF6; PTHR14167:SF6; 2.
DR   Pfam; PF14604; SH3_9; 3.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF50044; SSF50044; 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
 
 
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