SH3R2_HUMAN
ID SH3R2_HUMAN Reviewed; 729 AA.
AC Q8TEC5; A8K961; Q08AM9; Q6GMR9; Q8N5S8; Q96LP8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase SH3RF2;
DE EC=2.3.2.27 {ECO:0000269|PubMed:24130170};
DE AltName: Full=Heart protein phosphatase 1-binding protein;
DE Short=HEPP1;
DE AltName: Full=POSH-eliminating RING protein {ECO:0000303|PubMed:22128169};
DE AltName: Full=Protein phosphatase 1 regulatory subunit 39;
DE AltName: Full=RING finger protein 158;
DE AltName: Full=RING-type E3 ubiquitin transferase SH3RF2 {ECO:0000305};
DE AltName: Full=SH3 domain-containing RING finger protein 2;
GN Name=SH3RF2;
GN Synonyms=POSH3 {ECO:0000303|PubMed:20696164},
GN POSHER {ECO:0000303|PubMed:22128169}, PPP1R39, RNF158;
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 3), FUNCTION, INTERACTION WITH PPP1CA,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF VAL-643 AND PHE-645.
RX PubMed=19945436; DOI=10.1016/j.bbrc.2009.11.123;
RA Chen C.Y., Lai N.S., Yang J.J., Huang H.L., Hung W.C., Li C., Lin T.H.,
RA Huang H.B.;
RT "FLJ23654 encodes a heart protein phosphatase 1-binding protein (Hepp1).";
RL Biochem. Biophys. Res. Commun. 391:698-702(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP CYS-267; ARG-592; ILE-687 AND ALA-710.
RC TISSUE=Colon, and Testis;
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP CYS-267; ARG-592 AND ALA-710.
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 [5]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [6]
RP FUNCTION, AND INTERACTION WITH PPP1CA.
RX PubMed=19389623; DOI=10.1016/j.chembiol.2009.02.012;
RA Hendrickx A., Beullens M., Ceulemans H., Den Abt T., Van Eynde A.,
RA Nicolaescu E., Lesage B., Bollen M.;
RT "Docking motif-guided mapping of the interactome of protein phosphatase-
RT 1.";
RL Chem. Biol. 16:365-371(2009).
RN [7]
RP NOMENCLATURE.
RX PubMed=20696164; DOI=10.1016/j.febslet.2010.07.060;
RA Kaerkkaeinen S., van der Linden M., Renkema G.H.;
RT "POSH2 is a RING finger E3 ligase with Rac1 binding activity through a
RT partial CRIB domain.";
RL FEBS Lett. 584:3867-3872(2010).
RN [8]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE.
RX PubMed=22128169; DOI=10.1074/jbc.m111.269431;
RA Wilhelm M., Kukekov N.V., Schmit T.L., Biagas K.V., Sproul A.A., Gire S.,
RA Maes M.E., Xu Z., Greene L.A.;
RT "Sh3rf2/POSHER protein promotes cell survival by RING-mediated proteasomal
RT degradation of the c-Jun N-terminal kinase scaffold POSH (Plenty of SH3s)
RT protein.";
RL J. Biol. Chem. 287:2247-2256(2012).
RN [9]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PAK4 AND TNFRSF1A, AND
RP AUTOUBIQUITINATION.
RX PubMed=24130170; DOI=10.1093/carcin/bgt338;
RA Kim T.W., Kang Y.K., Park Z.Y., Kim Y.H., Hong S.W., Oh S.J., Sohn H.A.,
RA Yang S.J., Jang Y.J., Lee D.C., Kim S.Y., Yoo H.S., Kim E., Yeom Y.I.,
RA Park K.C.;
RT "SH3RF2 functions as an oncogene by mediating PAK4 protein stability.";
RL Carcinogenesis 35:624-634(2014).
CC -!- FUNCTION: Has E3 ubiquitin-protein ligase activity (PubMed:24130170).
CC Acts as an anti-apoptotic regulator of the JNK pathway by
CC ubiquitinating and promoting the degradation of SH3RF1, a scaffold
CC protein that is required for pro-apoptotic JNK activation
CC (PubMed:22128169). Facilitates TNF-alpha-mediated recruitment of
CC adapter proteins TRADD and RIPK1 to TNFRSF1A and regulates PAK4 protein
CC stability via inhibition of its ubiquitin-mediated proteasomal
CC degradation (PubMed:24130170). Inhibits PPP1CA phosphatase activity
CC (PubMed:19945436, PubMed:19389623). {ECO:0000269|PubMed:19389623,
CC ECO:0000269|PubMed:19945436, ECO:0000269|PubMed:22128169,
CC ECO:0000269|PubMed:24130170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:24130170};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with FASLG and PPP1CA (PubMed:19389623,
CC PubMed:19807924, PubMed:19945436). Interacts with PAK4 and TNFRSF1A
CC (PubMed:24130170). Interacts with DLK1, MAP3K10/MLK2, MAPK8IP1/JIP1,
CC MAPK8IP2/JIP2 and MAPK8IP3/JIP3. Interacts with RAC1 (both active
CC GTP- or inactive GDP-bound forms) (By similarity).
CC {ECO:0000250|UniProtKB:Q498M5, ECO:0000269|PubMed:19389623,
CC ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:19945436,
CC ECO:0000269|PubMed:24130170}.
CC -!- INTERACTION:
CC Q8TEC5; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-2130111, EBI-357530;
CC Q8TEC5; Q9Y2J4: AMOTL2; NbExp=4; IntAct=EBI-2130111, EBI-746752;
CC Q8TEC5; O95429: BAG4; NbExp=3; IntAct=EBI-2130111, EBI-2949658;
CC Q8TEC5; Q8N9N5: BANP; NbExp=3; IntAct=EBI-2130111, EBI-744695;
CC Q8TEC5; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-2130111, EBI-10171570;
CC Q8TEC5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2130111, EBI-3867333;
CC Q8TEC5; O43281-2: EFS; NbExp=3; IntAct=EBI-2130111, EBI-11525448;
CC Q8TEC5; Q08379: GOLGA2; NbExp=4; IntAct=EBI-2130111, EBI-618309;
CC Q8TEC5; Q5JR59-3: MTUS2; NbExp=4; IntAct=EBI-2130111, EBI-11522433;
CC Q8TEC5; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-2130111, EBI-11750983;
CC Q8TEC5; P62136: PPP1CA; NbExp=3; IntAct=EBI-2130111, EBI-357253;
CC Q8TEC5; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-2130111, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24130170}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TEC5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TEC5-2; Sequence=VSP_022058, VSP_022059;
CC Name=3;
CC IsoId=Q8TEC5-3; Sequence=VSP_040662;
CC -!- TISSUE SPECIFICITY: Heart (at protein level). Up-regulated in colon
CC cancer tissues as compared to normal colon tissues (at protein level).
CC Testis. In the heart, present in the apex, left atrium, right atrium,
CC left ventricle and right ventricle, but not in the aorta.
CC {ECO:0000269|PubMed:19945436, ECO:0000269|PubMed:24130170}.
CC -!- DOMAIN: The RING finger domain is required for ubiquitin ligase
CC activity and autoubiquitination. {ECO:0000269|PubMed:24130170}.
CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:24130170}.
CC -!- SIMILARITY: Belongs to the SH3RF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31650.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB85025.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK058046; BAB71639.1; -; mRNA.
DR EMBL; AK074234; BAB85025.1; ALT_TERM; mRNA.
DR EMBL; AK292576; BAF85265.1; -; mRNA.
DR EMBL; AC005216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031650; AAH31650.2; ALT_INIT; mRNA.
DR EMBL; BC073914; AAH73914.1; -; mRNA.
DR EMBL; BC125106; AAI25107.1; -; mRNA.
DR CCDS; CCDS4280.1; -. [Q8TEC5-1]
DR RefSeq; NP_689763.3; NM_152550.3. [Q8TEC5-1]
DR RefSeq; XP_006714820.1; XM_006714757.1. [Q8TEC5-1]
DR RefSeq; XP_011535871.1; XM_011537569.2. [Q8TEC5-1]
DR RefSeq; XP_016864625.1; XM_017009136.1. [Q8TEC5-1]
DR AlphaFoldDB; Q8TEC5; -.
DR SMR; Q8TEC5; -.
DR BioGRID; 127517; 56.
DR IntAct; Q8TEC5; 21.
DR STRING; 9606.ENSP00000424497; -.
DR GlyGen; Q8TEC5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TEC5; -.
DR PhosphoSitePlus; Q8TEC5; -.
DR BioMuta; SH3RF2; -.
DR DMDM; 296452957; -.
DR EPD; Q8TEC5; -.
DR jPOST; Q8TEC5; -.
DR MassIVE; Q8TEC5; -.
DR MaxQB; Q8TEC5; -.
DR PaxDb; Q8TEC5; -.
DR PeptideAtlas; Q8TEC5; -.
DR PRIDE; Q8TEC5; -.
DR ProteomicsDB; 74443; -. [Q8TEC5-1]
DR ProteomicsDB; 74444; -. [Q8TEC5-2]
DR ProteomicsDB; 74445; -. [Q8TEC5-3]
DR TopDownProteomics; Q8TEC5-1; -. [Q8TEC5-1]
DR Antibodypedia; 27503; 141 antibodies from 26 providers.
DR DNASU; 153769; -.
DR Ensembl; ENST00000359120.9; ENSP00000352028.4; ENSG00000156463.18. [Q8TEC5-1]
DR Ensembl; ENST00000511217.1; ENSP00000424497.1; ENSG00000156463.18. [Q8TEC5-1]
DR GeneID; 153769; -.
DR KEGG; hsa:153769; -.
DR MANE-Select; ENST00000359120.9; ENSP00000352028.4; NM_152550.4; NP_689763.4.
DR UCSC; uc003lnt.4; human. [Q8TEC5-1]
DR CTD; 153769; -.
DR DisGeNET; 153769; -.
DR GeneCards; SH3RF2; -.
DR HGNC; HGNC:26299; SH3RF2.
DR HPA; ENSG00000156463; Tissue enhanced (heart muscle, skeletal muscle, skin).
DR MIM; 613377; gene.
DR neXtProt; NX_Q8TEC5; -.
DR OpenTargets; ENSG00000156463; -.
DR PharmGKB; PA134944983; -.
DR VEuPathDB; HostDB:ENSG00000156463; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160067; -.
DR HOGENOM; CLU_015769_2_0_1; -.
DR InParanoid; Q8TEC5; -.
DR OMA; SVITQHM; -.
DR OrthoDB; 291531at2759; -.
DR PhylomeDB; Q8TEC5; -.
DR TreeFam; TF105571; -.
DR PathwayCommons; Q8TEC5; -.
DR SignaLink; Q8TEC5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 153769; 40 hits in 1113 CRISPR screens.
DR ChiTaRS; SH3RF2; human.
DR GenomeRNAi; 153769; -.
DR Pharos; Q8TEC5; Tbio.
DR PRO; PR:Q8TEC5; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8TEC5; protein.
DR Bgee; ENSG00000156463; Expressed in left ventricle myocardium and 138 other tissues.
DR Genevisible; Q8TEC5; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd11929; SH3_SH3RF2_1; 1.
DR CDD; cd11932; SH3_SH3RF2_2; 1.
DR CDD; cd11784; SH3_SH3RF2_3; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028511; SH3RF2.
DR InterPro; IPR035792; SH3RF2_SH3_1.
DR InterPro; IPR035794; SH3RF2_SH3_2.
DR InterPro; IPR035822; SH3RF2_SH3_3.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14167:SF60; PTHR14167:SF60; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repeat; SH3 domain;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..729
FT /note="E3 ubiquitin-protein ligase SH3RF2"
FT /id="PRO_0000269512"
FT DOMAIN 125..184
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 187..252
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 380..441
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 12..53
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 78..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..459
FT /note="Interaction with PAK4"
FT /evidence="ECO:0000269|PubMed:24130170"
FT REGION 497..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..646
FT /note="Interaction with PPP1CA"
FT COMPBIAS 266..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q498M5"
FT VAR_SEQ 1..543
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19945436"
FT /id="VSP_040662"
FT VAR_SEQ 1..508
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022058"
FT VAR_SEQ 509..519
FT /note="LRKGRSSMRKN -> MRKSKWWQRD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022059"
FT VARIANT 16
FT /note="F -> S (in dbSNP:rs34739859)"
FT /id="VAR_052118"
FT VARIANT 174
FT /note="F -> V (in dbSNP:rs34942619)"
FT /id="VAR_052119"
FT VARIANT 267
FT /note="R -> C (in dbSNP:rs758037)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_029788"
FT VARIANT 477
FT /note="R -> Q (in dbSNP:rs35165046)"
FT /id="VAR_052120"
FT VARIANT 592
FT /note="W -> R (in dbSNP:rs2962525)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_029789"
FT VARIANT 687
FT /note="V -> I (in dbSNP:rs11435)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_029790"
FT VARIANT 710
FT /note="G -> A (in dbSNP:rs1056149)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_029791"
FT MUTAGEN 643
FT /note="V->G: Significant loss of interaction with PPP1CA.
FT Significant loss of interaction with PPP1CA; when
FT associated with G-645."
FT /evidence="ECO:0000269|PubMed:19945436"
FT MUTAGEN 645
FT /note="F->G: Significant loss of interaction with PPP1CA.
FT Significant loss of interaction with PPP1CA; when
FT associated with G-643."
FT /evidence="ECO:0000269|PubMed:19945436"
FT CONFLICT 148
FT /note="K -> R (in Ref. 2; BAB85025)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="N -> S (in Ref. 2; BAB85025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 79320 MW; F85CCC0188DA8477 CRC64;
MDDLTLLDLL ECPVCFEKLD VTAKVLPCQH TFCKPCLQRV FKAHKELRCP ECRTPVFSNI
EALPANLLLV RLLDGVRSGQ SSGRGGSFRR PGTMTLQDGR KSRTNPRRLQ ASPFRLVPNV
RIHMDGVPRA KALCNYRGQN PGDLRFNKGD IILLRRQLDE NWYQGEINGI SGNFPASSVE
VIKQLPQPPP LCRALYNFDL RGKDKSENQD CLTFLKDDII TVISRVDENW AEGKLGDKVG
IFPILFVEPN LTARHLLEKN KGRQSSRTKN LSLVSSSSRG NTSTLRRGPG SRRKVPGQFS
ITTALNTLNR MVHSPSGRHM VEISTPVLIS SSNPSVITQP MEKADVPSSC VGQVSTYHPA
PVSPGHSTAV VSLPGSQQHL SANMFVALHS YSAHGPDELD LQKGEGVRVL GKCQDGWLRG
VSLVTGRVGI FPNNYVIPIF RKTSSFPDSR SPGLYTTWTL STSSVSSQGS ISEGDPRQSR
PFKSVFVPTA IVNPVRSTAG PGTLGQGSLR KGRSSMRKNG SLQRPLQSGI PTLVVGSLRR
SPTMVLRPQQ FQFYQPQGIP SSPSAVVVEM GSKPALTGEP ALTCISRGSE AWIHSAASSL
IMEDKEIPIK SEPLPKPPAS APPSILVKPE NSRNGIEKQV KTVRFQNYSP PPTKHYTSHP
TSGKPEQPAT LKASQPEAAS LGPEMTVLFA HRSGCHSGQQ TDLRRKSALG KATTLVSTAS
GTQTVFPSK
