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Database: UniProt
Entry: KCNA5_HUMAN
LinkDB: KCNA5_HUMAN
Original site: KCNA5_HUMAN 
ID   KCNA5_HUMAN             Reviewed;         613 AA.
AC   P22460; Q4KKT8; Q4VAJ1; Q4VAJ2; Q9UDA4;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   22-NOV-2017, entry version 176.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 5;
DE   AltName: Full=HPCN1;
DE   AltName: Full=Voltage-gated potassium channel HK2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv1.5;
GN   Name=KCNA5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RX   PubMed=2001794;
RA   Tamkun M.M., Knoth K.M., Walbridge J.A., Kroemer H., Roden D.M.,
RA   Glover D.M.;
RT   "Molecular cloning and characterization of two voltage-gated K+
RT   channel cDNAs from human ventricle.";
RL   FASEB J. 5:331-337(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Insulinoma;
RX   PubMed=1986382; DOI=10.1073/pnas.88.1.53;
RA   Philipson L.H., Hice R.E., Schaefer K., Lamendola J., Bell G.I.,
RA   Nelson D.J., Steiner D.F.;
RT   "Sequence and functional expression in Xenopus oocytes of a human
RT   insulinoma and islet potassium channel.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:53-57(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RX   PubMed=1349297; DOI=10.1016/0888-7543(92)90302-9;
RA   Curran M.E., Landes G.M., Keating M.T.;
RT   "Molecular cloning, characterization, and genomic localization of a
RT   human potassium channel gene.";
RL   Genomics 12:729-737(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8505626; DOI=10.1085/jgp.101.4.513;
RA   Snyders D.J., Tamkun M.M., Bennett P.B.;
RT   "A rapidly activating and slowly inactivating potassium channel cloned
RT   from human heart. Functional analysis after stable mammalian cell
RT   culture expression.";
RL   J. Gen. Physiol. 101:513-543(1993).
RN   [6]
RP   FUNCTION, AND ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX   PubMed=11524461; DOI=10.1085/jgp.118.3.315;
RA   Kurata H.T., Soon G.S., Fedida D.;
RT   "Altered state dependence of c-type inactivation in the long and short
RT   forms of human Kv1.5.";
RL   J. Gen. Physiol. 118:315-332(2001).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KCNAB1.
RX   PubMed=12130714; DOI=10.1124/jpet.102.033357;
RA   Williams C.P., Hu N., Shen W., Mashburn A.B., Murray K.T.;
RT   "Modulation of the human Kv1.5 channel by protein kinase C activation:
RT   role of the Kvbeta1.2 subunit.";
RL   J. Pharmacol. Exp. Ther. 302:545-550(2002).
RN   [8]
RP   INTERACTION WITH DLG1, AND MUTAGENESIS OF THR-15.
RX   PubMed=16466689; DOI=10.1016/j.bbrc.2006.01.110;
RA   Mathur R., Choi W.S., Eldstrom J., Wang Z., Kim J., Steele D.F.,
RA   Fedida D.;
RT   "A specific N-terminal residue in Kv1.5 is required for upregulation
RT   of the channel by SAP97.";
RL   Biochem. Biophys. Res. Commun. 342:1-8(2006).
RN   [9]
RP   INVOLVEMENT IN ATFB7.
RX   PubMed=16772329; DOI=10.1093/hmg/ddl143;
RA   Olson T.M., Alekseev A.E., Liu X.K., Park S., Zingman L.V.,
RA   Bienengraeber M., Sattiraju S., Ballew J.D., Jahangir A., Terzic A.;
RT   "Kv1.5 channelopathy due to KCNA5 loss-of-function mutation causes
RT   human atrial fibrillation.";
RL   Hum. Mol. Genet. 15:2185-2191(2006).
RN   [10]
RP   SUMOYLATION AT LYS-221 AND LYS-536, INTERACTION WITH UBE2I, AND
RP   MUTAGENESIS OF ILE-220; LYS-221; LEU-535 AND LYS-536.
RX   PubMed=17261810; DOI=10.1073/pnas.0606702104;
RA   Benson M.D., Li Q.J., Kieckhafer K., Dudek D., Whorton M.R.,
RA   Sunahara R.K., Iniguez-Lluhi J.A., Martens J.R.;
RT   "SUMO modification regulates inactivation of the voltage-gated
RT   potassium channel Kv1.5.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1805-1810(2007).
RN   [11]
RP   VARIANT [LARGE SCALE ANALYSIS] SER-300.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [12]
RP   VARIANTS HIS-42; MET-85; PRO-114; ARG-170 AND PRO-184.
RX   PubMed=24936649; DOI=10.1371/journal.pone.0100261;
RA   Pousada G., Baloira A., Vilarino C., Cifrian J.M., Valverde D.;
RT   "Novel mutations in BMPR2, ACVRL1 and KCNA5 genes and hemodynamic
RT   parameters in patients with pulmonary arterial hypertension.";
RL   PLoS ONE 9:E100261-E100261(2014).
CC   -!- FUNCTION: Voltage-gated potassium channel that mediates
CC       transmembrane potassium transport in excitable membranes. Forms
CC       tetrameric potassium-selective channels through which potassium
CC       ions pass in accordance with their electrochemical gradient. The
CC       channel alternates between opened and closed conformations in
CC       response to the voltage difference across the membrane. Can form
CC       functional homotetrameric channels and heterotetrameric channels
CC       that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5,
CC       and possibly other family members as well; channel properties
CC       depend on the type of alpha subunits that are part of the channel
CC       (PubMed:12130714). Channel properties are modulated by cytoplasmic
CC       beta subunits that regulate the subcellular location of the alpha
CC       subunits and promote rapid inactivation (PubMed:12130714).
CC       Homotetrameric channels display rapid activation and slow
CC       inactivation (PubMed:8505626, PubMed:12130714). May play a role in
CC       regulating the secretion of insulin in normal pancreatic islets.
CC       Isoform 2 exhibits a voltage-dependent recovery from inactivation
CC       and an excessive cumulative inactivation (PubMed:11524461).
CC       {ECO:0000269|PubMed:11524461, ECO:0000269|PubMed:12130714,
CC       ECO:0000269|PubMed:8505626}.
CC   -!- SUBUNIT: Homotetramer and heterotetramer of potassium channel
CC       proteins. Interacts with DLG1, which enhances channel currents.
CC       Forms a ternary complex with DLG1 and CAV3 (By similarity).
CC       Interacts with KCNAB1 (PubMed:12130714). Interacts with UBE2I
CC       (PubMed:17261810). {ECO:0000250|UniProtKB:P19024,
CC       ECO:0000269|PubMed:11524461, ECO:0000269|PubMed:12130714,
CC       ECO:0000269|PubMed:16466689, ECO:0000269|PubMed:17261810,
CC       ECO:0000269|PubMed:8505626}.
CC   -!- INTERACTION:
CC       P35609:ACTN2; NbExp=6; IntAct=EBI-6426121, EBI-77797;
CC       Q14160:SCRIB; NbExp=2; IntAct=EBI-6426121, EBI-357345;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12130714,
CC       ECO:0000269|PubMed:8505626}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P22460-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P22460-2; Sequence=VSP_037110;
CC   -!- TISSUE SPECIFICITY: Pancreatic islets and insulinoma.
CC   -!- DOMAIN: The amino terminus may be important in determining the
CC       rate of inactivation of the channel while the C-terminal PDZ-
CC       binding motif may play a role in modulation of channel activity
CC       and/or targeting of the channel to specific subcellular
CC       compartments.
CC   -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
CC       and is characterized by a series of positively charged amino acids
CC       at every third position. Channel opening and closing is effected
CC       by a conformation change that affects the position and orientation
CC       of the voltage-sensor paddle formed by S3 and S4 within the
CC       membrane. A transmembrane electric field that is positive inside
CC       would push the positively charged S4 segment outwards, thereby
CC       opening the pore, while a field that is negative inside would pull
CC       the S4 segment inwards and close the pore. Changes in the position
CC       and orientation of S4 are then transmitted to the activation gate
CC       formed by the inner helix bundle via the S4-S5 linker region.
CC       {ECO:0000250|UniProtKB:P63142}.
CC   -!- PTM: Sumoylated on Lys-221, and Lys-536, preferentially with
CC       SUMO3. Sumoylation regulates the voltage sensitivity of the
CC       channel. {ECO:0000269|PubMed:17261810}.
CC   -!- DISEASE: Atrial fibrillation, familial, 7 (ATFB7) [MIM:612240]: A
CC       familial form of atrial fibrillation, a common sustained cardiac
CC       rhythm disturbance. Atrial fibrillation is characterized by
CC       disorganized atrial electrical activity and ineffective atrial
CC       contraction promoting blood stasis in the atria and reduces
CC       ventricular filling. It can result in palpitations, syncope,
CC       thromboembolic stroke, and congestive heart failure.
CC       {ECO:0000269|PubMed:16772329}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
CC       (TC 1.A.1.2) subfamily. Kv1.5/KCNA5 sub-subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA60146.1; Type=Frameshift; Positions=579; Evidence={ECO:0000305};
DR   EMBL; M60451; AAA61276.1; -; mRNA.
DR   EMBL; M55513; AAA36422.1; -; mRNA.
DR   EMBL; M83254; AAA60146.1; ALT_FRAME; mRNA.
DR   EMBL; BC096357; AAH96357.1; -; mRNA.
DR   EMBL; BC096358; AAH96358.3; -; mRNA.
DR   EMBL; BC099665; AAH99665.3; -; mRNA.
DR   EMBL; BC099666; AAH99666.3; -; mRNA.
DR   CCDS; CCDS8536.1; -. [P22460-1]
DR   PIR; A56031; A56031.
DR   RefSeq; NP_002225.2; NM_002234.3. [P22460-1]
DR   UniGene; Hs.150208; -.
DR   UniGene; Hs.741439; -.
DR   ProteinModelPortal; P22460; -.
DR   SMR; P22460; -.
DR   BioGrid; 109943; 58.
DR   DIP; DIP-42010N; -.
DR   IntAct; P22460; 10.
DR   MINT; MINT-200758; -.
DR   STRING; 9606.ENSP00000252321; -.
DR   BindingDB; P22460; -.
DR   ChEMBL; CHEMBL4306; -.
DR   DrugBank; DB06637; Dalfampridine.
DR   GuidetoPHARMACOLOGY; 542; -.
DR   TCDB; 1.A.1.2.4; the voltage-gated ion channel (vic) superfamily.
DR   iPTMnet; P22460; -.
DR   PhosphoSitePlus; P22460; -.
DR   BioMuta; KCNA5; -.
DR   DMDM; 146345443; -.
DR   PaxDb; P22460; -.
DR   PeptideAtlas; P22460; -.
DR   PRIDE; P22460; -.
DR   Ensembl; ENST00000252321; ENSP00000252321; ENSG00000130037. [P22460-1]
DR   GeneID; 3741; -.
DR   KEGG; hsa:3741; -.
DR   UCSC; uc001qni.5; human. [P22460-1]
DR   CTD; 3741; -.
DR   DisGeNET; 3741; -.
DR   EuPathDB; HostDB:ENSG00000130037.4; -.
DR   GeneCards; KCNA5; -.
DR   HGNC; HGNC:6224; KCNA5.
DR   HPA; CAB022562; -.
DR   HPA; HPA021516; -.
DR   MalaCards; KCNA5; -.
DR   MIM; 176267; gene.
DR   MIM; 612240; phenotype.
DR   neXtProt; NX_P22460; -.
DR   OpenTargets; ENSG00000130037; -.
DR   Orphanet; 334; Familial atrial fibrillation.
DR   PharmGKB; PA208; -.
DR   eggNOG; KOG1545; Eukaryota.
DR   eggNOG; COG1226; LUCA.
DR   GeneTree; ENSGT00760000118846; -.
DR   HOGENOM; HOG000231015; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; P22460; -.
DR   KO; K04878; -.
DR   OMA; LPRNEFQ; -.
DR   OrthoDB; EOG091G10NU; -.
DR   PhylomeDB; P22460; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR   GeneWiki; KCNA5; -.
DR   GenomeRNAi; 3741; -.
DR   PRO; PR:P22460; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000130037; -.
DR   CleanEx; HS_KCNA5; -.
DR   Genevisible; P22460; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR   GO; GO:0046691; C:intracellular canaliculus; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0051393; F:alpha-actinin binding; IPI:BHF-UCL.
DR   GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
DR   GO; GO:0015271; F:outward rectifier potassium channel activity; IDA:BHF-UCL.
DR   GO; GO:0019870; F:potassium channel inhibitor activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR   GO; GO:0005102; F:receptor binding; IEA:Ensembl.
DR   GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR   GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; IMP:BHF-UCL.
DR   GO; GO:0086087; F:voltage-gated potassium channel activity involved in bundle of His cell action potential repolarization; IMP:BHF-UCL.
DR   GO; GO:0086090; F:voltage-gated potassium channel activity involved in SA node cell action potential repolarization; IMP:BHF-UCL.
DR   GO; GO:0086014; P:atrial cardiac muscle cell action potential; IMP:BHF-UCL.
DR   GO; GO:0060081; P:membrane hyperpolarization; IMP:BHF-UCL.
DR   GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; IMP:BHF-UCL.
DR   GO; GO:0086050; P:membrane repolarization during bundle of His cell action potential; IMP:BHF-UCL.
DR   GO; GO:0086052; P:membrane repolarization during SA node cell action potential; IMP:BHF-UCL.
DR   GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0043267; P:negative regulation of potassium ion transport; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:2000288; P:positive regulation of myoblast proliferation; IEA:Ensembl.
DR   GO; GO:0071435; P:potassium ion export; IDA:BHF-UCL.
DR   GO; GO:0055075; P:potassium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0006813; P:potassium ion transport; IDA:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR   GO; GO:0050796; P:regulation of insulin secretion; TAS:BHF-UCL.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
DR   GO; GO:0043266; P:regulation of potassium ion transport; IMP:BHF-UCL.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR   InterPro; IPR004052; K_chnl_volt-dep_Kv1.5.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR028325; VG_K_chnl.
DR   PANTHER; PTHR11537; PTHR11537; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01512; KV15CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Atrial fibrillation; Cell membrane;
KW   Complete proteome; Ion channel; Ion transport; Isopeptide bond;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism;
KW   Potassium; Potassium channel; Potassium transport; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation; Voltage-gated channel.
FT   CHAIN         1    613       Potassium voltage-gated channel subfamily
FT                                A member 5.
FT                                /FTId=PRO_0000053985.
FT   TOPO_DOM      1    247       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    248    269       Helical; Name=Segment S1.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    270    323       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    324    345       Helical; Name=Segment S2.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    346    356       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    357    377       Helical; Name=Segment S3.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    378    395       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    396    416       Helical; Voltage-sensor; Name=Segment S4.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    417    431       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    432    453       Helical; Name=Segment S5.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    454    467       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   INTRAMEM    468    479       Helical; Name=Pore helix.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   INTRAMEM    480    487       {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    488    494       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    495    523       Helical; Name=Segment S6.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    524    613       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   REPEAT       61     71       1.
FT   REPEAT       72     82       2.
FT   REGION       61     82       2 X 11 AA tandem repeat of D-[SP]-G-V-R-
FT                                P-L-P-P-L-P.
FT   REGION      418    431       S4-S5 linker.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   MOTIF       480    485       Selectivity filter.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   MOTIF       611    613       PDZ-binding. {ECO:0000250}.
FT   COMPBIAS     94     99       Poly-Glu.
FT   COMPBIAS    382    387       Poly-Gly.
FT   MOD_RES     557    557       Phosphoserine; by PKA. {ECO:0000255}.
FT   LIPID       346    346       S-palmitoyl cysteine. {ECO:0000255}.
FT   CROSSLNK    221    221       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000269|PubMed:17261810}.
FT   CROSSLNK    536    536       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000269|PubMed:17261810}.
FT   VAR_SEQ       1    209       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_037110.
FT   VARIANT      42     42       L -> H (found in a patient with pulmonary
FT                                arterial hypertension; unknown
FT                                pathological significance).
FT                                {ECO:0000269|PubMed:24936649}.
FT                                /FTId=VAR_079602.
FT   VARIANT      85     85       L -> M. {ECO:0000269|PubMed:24936649}.
FT                                /FTId=VAR_079603.
FT   VARIANT     114    114       T -> P (found in a patient with pulmonary
FT                                arterial hypertension; unknown
FT                                pathological significance).
FT                                {ECO:0000269|PubMed:24936649}.
FT                                /FTId=VAR_079604.
FT   VARIANT     170    170       P -> R (found in a patient with pulmonary
FT                                arterial hypertension; unknown
FT                                pathological significance).
FT                                {ECO:0000269|PubMed:24936649}.
FT                                /FTId=VAR_079605.
FT   VARIANT     184    184       R -> P (found in a patient with pulmonary
FT                                arterial hypertension; unknown
FT                                pathological significance).
FT                                {ECO:0000269|PubMed:24936649}.
FT                                /FTId=VAR_079606.
FT   VARIANT     228    228       P -> S (in dbSNP:rs1056464).
FT                                /FTId=VAR_053856.
FT   VARIANT     300    300       G -> S (in a breast cancer sample;
FT                                somatic mutation; dbSNP:rs148708451).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035770.
FT   VARIANT     578    578       R -> K (in dbSNP:rs12720445).
FT                                /FTId=VAR_054786.
FT   MUTAGEN      15     15       T->A: Loss of DLG1 effect on channel
FT                                current. {ECO:0000269|PubMed:16466689}.
FT   MUTAGEN     220    220       I->N: Reduces sumoylation; when
FT                                associated with N-535.
FT                                {ECO:0000269|PubMed:17261810}.
FT   MUTAGEN     221    221       K->R: Abolishes sumoylation; when
FT                                associated with R-536.
FT                                {ECO:0000269|PubMed:17261810}.
FT   MUTAGEN     535    535       L->N: Reduces sumoylation; when
FT                                associated with N-220.
FT                                {ECO:0000269|PubMed:17261810}.
FT   MUTAGEN     536    536       K->R: Abolishes sumoylation; when
FT                                associated with R-221.
FT                                {ECO:0000269|PubMed:17261810}.
FT   CONFLICT     55     55       Missing (in Ref. 1; AAA61276).
FT                                {ECO:0000305}.
FT   CONFLICT    138    138       L -> Q (in Ref. 2; AAA36422).
FT                                {ECO:0000305}.
FT   CONFLICT    154    154       R -> P (in Ref. 1; AAA61276 and 2;
FT                                AAA36422). {ECO:0000305}.
FT   CONFLICT    187    188       RP -> G (in Ref. 1; AAA61276).
FT                                {ECO:0000305}.
FT   CONFLICT    214    214       R -> G (in Ref. 2; AAA36422).
FT                                {ECO:0000305}.
FT   CONFLICT    228    228       P -> V (in Ref. 2; AAA36422).
FT                                {ECO:0000305}.
FT   CONFLICT    282    282       L -> V (in Ref. 3; AAA60146).
FT                                {ECO:0000305}.
FT   CONFLICT    307    307       P -> A (in Ref. 1; AAA61276).
FT                                {ECO:0000305}.
SQ   SEQUENCE   613 AA;  67228 MW;  A5B02B27F8396E3D CRC64;
     MEIALVPLEN GGAMTVRGGD EARAGCGQAT GGELQCPPTA GLSDGPKEPA PKGRGAQRDA
     DSGVRPLPPL PDPGVRPLPP LPEELPRPRR PPPEDEEEEG DPGLGTVEDQ ALGTASLHHQ
     RVHINISGLR FETQLGTLAQ FPNTLLGDPA KRLRYFDPLR NEYFFDRNRP SFDGILYYYQ
     SGGRLRRPVN VSLDVFADEI RFYQLGDEAM ERFREDEGFI KEEEKPLPRN EFQRQVWLIF
     EYPESSGSAR AIAIVSVLVI LISIITFCLE TLPEFRDERE LLRHPPAPHQ PPAPAPGANG
     SGVMAPPSGP TVAPLLPRTL ADPFFIVETT CVIWFTFELL VRFFACPSKA GFSRNIMNII
     DVVAIFPYFI TLGTELAEQQ PGGGGGGQNG QQAMSLAILR VIRLVRVFRI FKLSRHSKGL
     QILGKTLQAS MRELGLLIFF LFIGVILFSS AVYFAEADNQ GTHFSSIPDA FWWAVVTMTT
     VGYGDMRPIT VGGKIVGSLC AIAGVLTIAL PVPVIVSNFN YFYHRETDHE EPAVLKEEQG
     TQSQGPGLDR GVQRKVSGSR GSFCKAGGTL ENADSARRGS CPLEKCNVKA KSNVDLRRSL
     YALCLDTSRE TDL
//
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