ID   ABR_HUMAN               Reviewed;         859 AA.
AC   Q12979; B3KW89; B7Z6H7; D3DTH3; D3DTH4; F5H3S2; F5H8B3; Q13693; Q13694;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   24-JAN-2024, entry version 203.
DE   RecName: Full=Active breakpoint cluster region-related protein {ECO:0000305};
GN   Name=ABR {ECO:0000312|HGNC:HGNC:81};
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 LONG).
RC   TISSUE=Hippocampus;
RX   PubMed=8262969; DOI=10.1016/s0021-9258(19)74248-3;
RA   Tan E.-C., Leung T., Manser E., Lim L.;
RT   "The human active breakpoint cluster region-related gene encodes a brain
RT   protein with homology to guanine nucleotide exchange proteins and GTPase-
RT   activating proteins.";
RL   J. Biol. Chem. 268:27291-27298(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP   ARG-517.
RC   TISSUE=Cerebellum, and Placenta;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Fibroblast;
RX   PubMed=8349582; DOI=10.1016/s0021-9258(19)85281-x;
RA   Heisterkamp N., Kaartinen V., van Soest S., Bokoch G.M., Groffen J.;
RT   "Human ABR encodes a protein with GAPrac activity and homology to the DBL
RT   nucleotide exchange factor domain.";
RL   J. Biol. Chem. 268:16903-16906(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 436-597.
RX   PubMed=2587217; DOI=10.1093/nar/17.21.8821;
RA   Heisterkamp N., Morris C., Groffen J.;
RT   "ABR, an active BCR-related gene.";
RL   Nucleic Acids Res. 17:8821-8831(1989).
RN   [7]
RP   FUNCTION, AND DOMAIN.
RX   PubMed=7479768; DOI=10.1073/pnas.92.22.10282;
RA   Chuang T.H., Xu X., Kaartinen V., Heisterkamp N., Groffen J., Bokoch G.M.;
RT   "Abr and Bcr are multifunctional regulators of the Rho GTP-binding protein
RT   family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:10282-10286(1995).
RN   [8]
RP   FUNCTION, AND MUTAGENESIS OF ARG-683 AND ASN-795.
RX   PubMed=17116687; DOI=10.1128/mcb.00756-06;
RA   Cho Y.J., Cunnick J.M., Yi S.J., Kaartinen V., Groffen J., Heisterkamp N.;
RT   "Abr and Bcr, two homologous Rac GTPase-activating proteins, control
RT   multiple cellular functions of murine macrophages.";
RL   Mol. Cell. Biol. 27:899-911(2007).
RN   [9]
RP   FUNCTION, INTERACTION WITH DLG4, AND MUTAGENESIS OF VAL-859.
RX   PubMed=20962234; DOI=10.1523/jneurosci.1711-10.2010;
RA   Oh D., Han S., Seo J., Lee J.R., Choi J., Groffen J., Kim K., Cho Y.S.,
RA   Choi H.S., Shin H., Woo J., Won H., Park S.K., Kim S.Y., Jo J.,
RA   Whitcomb D.J., Cho K., Kim H., Bae Y.C., Heisterkamp N., Choi S.Y., Kim E.;
RT   "Regulation of synaptic Rac1 activity, long-term potentiation maintenance,
RT   and learning and memory by BCR and ABR Rac GTPase-activating proteins.";
RL   J. Neurosci. 30:14134-14144(2010).
CC   -!- FUNCTION: Protein with a unique structure having two opposing
CC       regulatory activities toward small GTP-binding proteins. The C-terminus
CC       is a GTPase-activating protein domain which stimulates GTP hydrolysis
CC       by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP
CC       hydrolysis of RAC1 or CDC42, leading to down-regulation of the active
CC       GTP-bound form (PubMed:7479768, PubMed:17116687). The central Dbl
CC       homology (DH) domain functions as a guanine nucleotide exchange factor
CC       (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the
CC       conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound
CC       form (PubMed:7479768). Functions as an important negative regulator of
CC       neuronal RAC1 activity (By similarity). Regulates macrophage functions
CC       such as CSF-1 directed motility and phagocytosis through the modulation
CC       of RAC1 activity (By similarity). {ECO:0000250|UniProtKB:Q5SSL4,
CC       ECO:0000269|PubMed:17116687, ECO:0000269|PubMed:7479768}.
CC   -!- SUBUNIT: Interacts with DLG4. {ECO:0000269|PubMed:20962234}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC       {ECO:0000250|UniProtKB:Q5SSL4}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q5SSL4}. Synapse
CC       {ECO:0000250|UniProtKB:A0A0G2JTR4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=Long;
CC         IsoId=Q12979-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q12979-2; Sequence=VSP_001815;
CC       Name=3;
CC         IsoId=Q12979-3; Sequence=VSP_046029, VSP_046030;
CC       Name=4;
CC         IsoId=Q12979-4; Sequence=VSP_046148;
CC   -!- TISSUE SPECIFICITY: Highly enriched in the brain. Much weaker
CC       expression in heart, lung and muscle.
CC   -!- DOMAIN: The central Dbl homology (DH) domain functions as a guanine
CC       nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA
CC       and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-
CC       bound to the GTP-bound form. The C-terminus is a Rho-GAP domain which
CC       stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. The protein has a
CC       unique structure having two opposing regulatory activities toward small
CC       GTP-binding proteins. {ECO:0000305|PubMed:7479768}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U01147; AAC50063.1; -; mRNA.
DR   EMBL; L19704; AAC37519.1; -; Genomic_DNA.
DR   EMBL; L19705; AAC37518.1; -; Genomic_DNA.
DR   EMBL; AK124547; BAG54051.1; -; mRNA.
DR   EMBL; AK300336; BAH13263.1; -; mRNA.
DR   EMBL; AC015884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC016292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC144836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90631.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90633.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90634.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90635.1; -; Genomic_DNA.
DR   CCDS; CCDS10999.1; -. [Q12979-1]
DR   CCDS; CCDS11000.1; -. [Q12979-2]
DR   CCDS; CCDS54060.1; -. [Q12979-4]
DR   CCDS; CCDS58497.1; -. [Q12979-3]
DR   PIR; A47485; A47485.
DR   PIR; A49307; A49307.
DR   RefSeq; NP_001083.2; NM_001092.4. [Q12979-2]
DR   RefSeq; NP_001153218.1; NM_001159746.2. [Q12979-4]
DR   RefSeq; NP_001243776.1; NM_001256847.2. [Q12979-3]
DR   RefSeq; NP_001269078.1; NM_001282149.1.
DR   RefSeq; NP_001309769.1; NM_001322840.1. [Q12979-4]
DR   RefSeq; NP_068781.2; NM_021962.4. [Q12979-1]
DR   AlphaFoldDB; Q12979; -.
DR   SMR; Q12979; -.
DR   BioGRID; 106547; 38.
DR   IntAct; Q12979; 9.
DR   MINT; Q12979; -.
DR   STRING; 9606.ENSP00000303909; -.
DR   iPTMnet; Q12979; -.
DR   PhosphoSitePlus; Q12979; -.
DR   BioMuta; ABR; -.
DR   DMDM; 357528764; -.
DR   EPD; Q12979; -.
DR   jPOST; Q12979; -.
DR   MassIVE; Q12979; -.
DR   MaxQB; Q12979; -.
DR   PaxDb; 9606-ENSP00000303909; -.
DR   PeptideAtlas; Q12979; -.
DR   ProteomicsDB; 26359; -.
DR   ProteomicsDB; 27736; -.
DR   ProteomicsDB; 59072; -. [Q12979-1]
DR   ProteomicsDB; 59073; -. [Q12979-2]
DR   Pumba; Q12979; -.
DR   Antibodypedia; 22668; 86 antibodies from 20 providers.
DR   DNASU; 29; -.
DR   Ensembl; ENST00000291107.6; ENSP00000291107.2; ENSG00000159842.16. [Q12979-2]
DR   Ensembl; ENST00000302538.10; ENSP00000303909.5; ENSG00000159842.16. [Q12979-1]
DR   Ensembl; ENST00000543210.6; ENSP00000445198.2; ENSG00000159842.16. [Q12979-3]
DR   Ensembl; ENST00000544583.6; ENSP00000442048.2; ENSG00000159842.16. [Q12979-4]
DR   Ensembl; ENST00000611009.4; ENSP00000484030.1; ENSG00000276016.4. [Q12979-3]
DR   Ensembl; ENST00000611021.3; ENSP00000483168.1; ENSG00000278741.4. [Q12979-2]
DR   Ensembl; ENST00000612118.4; ENSP00000481740.1; ENSG00000278741.4. [Q12979-1]
DR   Ensembl; ENST00000615642.4; ENSP00000479455.1; ENSG00000278741.4. [Q12979-3]
DR   Ensembl; ENST00000620619.4; ENSP00000478880.1; ENSG00000278741.4. [Q12979-4]
DR   Ensembl; ENST00000625740.2; ENSP00000486511.1; ENSG00000276016.4. [Q12979-2]
DR   Ensembl; ENST00000627258.2; ENSP00000486214.1; ENSG00000278741.4. [Q12979-4]
DR   GeneID; 29; -.
DR   KEGG; hsa:29; -.
DR   MANE-Select; ENST00000302538.10; ENSP00000303909.5; NM_021962.5; NP_068781.2.
DR   UCSC; uc002fsd.6; human. [Q12979-1]
DR   AGR; HGNC:81; -.
DR   CTD; 29; -.
DR   DisGeNET; 29; -.
DR   GeneCards; ABR; -.
DR   HGNC; HGNC:81; ABR.
DR   HPA; ENSG00000159842; Tissue enhanced (brain).
DR   MIM; 600365; gene.
DR   neXtProt; NX_Q12979; -.
DR   OpenTargets; ENSG00000159842; -.
DR   PharmGKB; PA24417; -.
DR   VEuPathDB; HostDB:ENSG00000159842; -.
DR   eggNOG; KOG4269; Eukaryota.
DR   GeneTree; ENSGT00940000153491; -.
DR   HOGENOM; CLU_004000_1_0_1; -.
DR   InParanoid; Q12979; -.
DR   OMA; TMFYKIP; -.
DR   OrthoDB; 2916231at2759; -.
DR   PhylomeDB; Q12979; -.
DR   TreeFam; TF105082; -.
DR   PathwayCommons; Q12979; -.
DR   Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR   Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR   Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR   Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR   Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR   Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR   Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR   SignaLink; Q12979; -.
DR   SIGNOR; Q12979; -.
DR   BioGRID-ORCS; 29; 17 hits in 1143 CRISPR screens.
DR   ChiTaRS; ABR; human.
DR   GenomeRNAi; 29; -.
DR   Pharos; Q12979; Tbio.
DR   PRO; PR:Q12979; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q12979; Protein.
DR   Bgee; ENSG00000159842; Expressed in superior frontal gyrus and 102 other cell types or tissues.
DR   ExpressionAtlas; Q12979; baseline and differential.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISS:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR   GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:UniProtKB.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR   CDD; cd08686; C2_ABR; 1.
DR   CDD; cd13366; PH_ABR; 1.
DR   CDD; cd04387; RhoGAP_Bcr; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR037769; Abr/Bcr.
DR   InterPro; IPR037865; ABR_PH.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23182:SF5; ACTIVE BREAKPOINT CLUSTER REGION-RELATED PROTEIN; 1.
DR   PANTHER; PTHR23182; BREAKPOINT CLUSTER REGION PROTEIN BCR; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF19057; PH_19; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   Genevisible; Q12979; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; GTPase activation;
KW   Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW   Synapse.
FT   CHAIN           1..859
FT                   /note="Active breakpoint cluster region-related protein"
FT                   /id="PRO_0000080902"
FT   DOMAIN          91..284
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          301..459
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          484..613
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          647..845
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          26..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         57
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSL4"
FT   VAR_SEQ         1..82
FT                   /note="MEPLSHRGLPRLSWIDTLYSNFSYGTDEYDGEGNEEQKGPPEGSETMPYIDE
FT                   SPTMSPQLSARSQGGGDGVSPTPPEGLAPG -> MEEEEEAIGLLDKVLEDEDVFLLEE
FT                   CELGTPTSPGSGSPFLVAVK (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001815"
FT   VAR_SEQ         1..48
FT                   /note="MEPLSHRGLPRLSWIDTLYSNFSYGTDEYDGEGNEEQKGPPEGSETMP ->
FT                   MTDVLPQPDCSPKAGREPLALEESGSKRPPNTGARLWGRVRNKLLRNK (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046029"
FT   VAR_SEQ         1..46
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046148"
FT   VAR_SEQ         49..597
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046030"
FT   VARIANT         517
FT                   /note="K -> R (in dbSNP:rs34169260)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_057186"
FT   MUTAGEN         683
FT                   /note="R->A: Reduces GAP activity. Loss of GAP activity;
FT                   when associated with A-795."
FT                   /evidence="ECO:0000269|PubMed:17116687"
FT   MUTAGEN         795
FT                   /note="N->A: Loss of GAP activity; when associated with
FT                   A-683."
FT                   /evidence="ECO:0000269|PubMed:17116687"
FT   MUTAGEN         859
FT                   /note="V->A: Abolishes interaction with DLG4. No effect on
FT                   synaptic localization."
FT                   /evidence="ECO:0000269|PubMed:20962234"
FT   CONFLICT        67
FT                   /note="G -> R (in Ref. 1; AAC50063)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        483
FT                   /note="R -> K (in Ref. 2; BAG54051)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        625
FT                   /note="K -> R (in Ref. 2; BAH13263)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        657..660
FT                   /note="RSKV -> VQGA (in Ref. 3; AAC37519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        761
FT                   /note="L -> V (in Ref. 3; AAC37519)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   859 AA;  97598 MW;  3A5BE3AD2455A194 CRC64;
     MEPLSHRGLP RLSWIDTLYS NFSYGTDEYD GEGNEEQKGP PEGSETMPYI DESPTMSPQL
     SARSQGGGDG VSPTPPEGLA PGVEAGKGLE MRKLVLSGFL ASEEIYINQL EALLLPMKPL
     KATATTSQPV LTIQQIETIF YKIQDIYEIH KEFYDNLCPK VQQWDSQVTM GHLFQKLASQ
     LGVYKAFVDN YKVALETAEK CSQSNNQFQK ISEELKVKGP KDSKDSHTSV TMEALLYKPI
     DRVTRSTLVL HDLLKHTPVD HPDYPLLQDA LRISQNFLSS INEDIDPRRT AVTTPKGETR
     QLVKDGFLVE VSESSRKLRH VFLFTDVLLC AKLKKTSAGK HQQYDCKWYI PLADLVFPSP
     EESEASPQVH PFPDHELEDM KMKISALKSE IQKEKANKGQ SRAIERLKKK MFENEFLLLL
     NSPTIPFRIH NRNGKSYLFL LSSDYERSEW REAIQKLQKK DLQAFVLSSV ELQVLTGSCF
     KLRTVHNIPV TSNKDDDESP GLYGFLHVIV HSAKGFKQSA NLYCTLEVDS FGYFVSKAKT
     RVFRDTAEPK WDEEFEIELE GSQSLRILCY EKCYDKTKVN KDNNEIVDKI MGKGQIQLDP
     QTVETKNWHT DVIEMNGIKV EFSMKFTSRD MSLKRTPSKK QTGVFGVKIS VVTKRERSKV
     PYIVRQCVEE VEKRGIEEVG IYRISGVATD IQALKAVFDA NNKDILLMLS DMDINAIAGT
     LKLYFRELPE PLLTDRLYPA FMEGIALSDP AAKENCMMHL LRSLPDPNLI TFLFLLEHLK
     RVAEKEPINK MSLHNLATVF GPTLLRPSEV ESKAHLTSAA DIWSHDVMAQ VQVLLYYLQH
     PPISFAELKR NTLYFSTDV
//