CALM2_RAT
ID CALM2_RAT Reviewed; 149 AA.
AC P0DP30; P02593; P62161; P70667; P99014; Q61379; Q61380;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Calmodulin-2 {ECO:0000250|UniProtKB:P0DP24};
GN Name=Calm2 {ECO:0000312|RGD:2258};
GN Synonyms=Cam2, Camb, CaMII {ECO:0000303|PubMed:2527998};
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].
RX PubMed=2445749; DOI=10.1016/s0021-9258(18)49306-4;
RA Sengupta B., Friedberg F., Detera-Wadleigh S.D.;
RT "Molecular analysis of human and rat calmodulin complementary DNA clones.
RT Evidence for additional active genes in these species.";
RL J. Biol. Chem. 262:16663-16670(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3037336; DOI=10.1128/mcb.7.5.1873-1880.1987;
RA Nojima H., Kishi K., Sokabe H.;
RT "Multiple calmodulin mRNA species are derived from two distinct genes.";
RL Mol. Cell. Biol. 7:1873-1880(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SHR;
RX PubMed=2527998; DOI=10.1016/0022-2836(89)90388-4;
RA Nojima H.;
RT "Structural organization of multiple rat calmodulin genes.";
RL J. Mol. Biol. 208:269-282(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT
RP LYS-116.
RC TISSUE=Testis;
RX PubMed=201628; DOI=10.1016/s0021-9258(17)38210-8;
RA Dedman J.R., Jackson R.L., Schreiber W.E., Means A.R.;
RT "Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide
RT phosphodiesterase from rat testis with other Ca2+-binding proteins.";
RL J. Biol. Chem. 253:343-346(1978).
RN [6]
RP PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [7]
RP INTERACTION WITH CEACAM1.
RX PubMed=8576129; DOI=10.1074/jbc.271.3.1393;
RA Edlund M., Blikstad I., Obrink B.;
RT "Calmodulin binds to specific sequences in the cytoplasmic domain of C-CAM
RT and down-regulates C-CAM self-association.";
RL J. Biol. Chem. 271:1393-1399(1996).
RN [8]
RP PHOSPHORYLATION AT THR-45.
RX PubMed=12392717; DOI=10.1016/s0003-9861(02)00514-3;
RA Ishida A., Kameshita I., Okuno S., Kitani T., Fujisawa H.;
RT "Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase
RT IV.";
RL Arch. Biochem. Biophys. 407:72-82(2002).
RN [9]
RP INTERACTION WITH RRAD.
RX PubMed=18056528; DOI=10.1161/circulationaha.107.707257;
RA Chang L., Zhang J., Tseng Y.-H., Xie C.-Q., Ilany J., Bruning J.C., Sun Z.,
RA Zhu X., Cui T., Youker K.A., Yang Q., Day S.M., Kahn C.R., Chen Y.E.;
RT "Rad GTPase deficiency leads to cardiac hypertrophy.";
RL Circulation 116:2976-2983(2007).
RN [10]
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND SER-102, 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: Calmodulin mediates the control of a large number of enzymes,
CC ion channels, aquaporins and other proteins through calcium-binding.
CC Among the enzymes to be stimulated by the calmodulin-calcium complex
CC are a number of protein kinases and phosphatases. Together with CCP110
CC and centrin, is involved in a genetic pathway that regulates the
CC centrosome cycle and progression through cytokinesis. Mediates calcium-
CC dependent inactivation of CACNA1C. Positively regulates calcium-
CC activated potassium channel activity of KCNN2.
CC {ECO:0000250|UniProtKB:P62158}.
CC -!- SUBUNIT: Interacts with CEP97, CCP110, TTN/titin and SRY (By
CC similarity). Interacts with MYO5A and RRAD (PubMed:18056528). Interacts
CC with USP6; the interaction is calcium dependent (By similarity).
CC Interacts with CDK5RAP2 (By similarity). Interacts with SCN5A (By
CC similarity). Interacts with RYR1 (By similarity). Interacts with FCHO1
CC (By similarity). Interacts with MIP in a 1:2 stoichiometry; the
CC interaction with the cytoplasmic domains from two MIP subunits promotes
CC MIP water channel closure (By similarity). Interacts with ORAI1; this
CC may play a role in the regulation of ORAI1-mediated calcium transport
CC (By similarity). Interacts with SYT7 (By similarity). Interacts with
CC MYO10 and MYO1C (By similarity). Interacts with CEACAM1 (via
CC cytoplasmic domain); this interaction is in a calcium dependent manner
CC and reduces homophilic cell adhesion through dissociation of dimer
CC (PubMed:8576129). Interacts with RYR2; regulates RYR2 calcium-release
CC channel activity (By similarity). Interacts with PCP4; regulates
CC calmodulin calcium-binding (By similarity). Interacts with the
CC heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-
CC independent, constitutive and participates in the proper assembly of a
CC functional heterotetrameric M channel (By similarity).
CC {ECO:0000250|UniProtKB:P0DP24, ECO:0000250|UniProtKB:P0DP29,
CC ECO:0000250|UniProtKB:P62157, ECO:0000250|UniProtKB:P62158,
CC ECO:0000250|UniProtKB:P62204, ECO:0000269|PubMed:18056528,
CC ECO:0000269|PubMed:8576129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm,
CC cytoskeleton, spindle pole. Note=Distributed throughout the cell during
CC interphase, but during mitosis becomes dramatically localized to the
CC spindle poles and the spindle microtubules. {ECO:0000250}.
CC -!- PTM: Ubiquitination results in a strongly decreased activity.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation results in a decreased activity.
CC {ECO:0000269|PubMed:12392717}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC {ECO:0000250|UniProtKB:P0DP24}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; M19312; AAA40862.1; -; mRNA.
DR EMBL; M17069; AAA40863.1; -; mRNA.
DR EMBL; X13833; CAA32062.1; -; Genomic_DNA.
DR EMBL; X13834; CAA32062.1; JOINED; Genomic_DNA.
DR EMBL; X13835; CAA32062.1; JOINED; Genomic_DNA.
DR EMBL; BC058485; AAH58485.1; -; mRNA.
DR RefSeq; NP_036650.1; NM_012518.3.
DR RefSeq; NP_059022.1; NM_017326.3.
DR RefSeq; NP_114175.1; NM_031969.2.
DR PDB; 6ALE; X-ray; 2.50 A; R=5-148.
DR PDBsum; 6ALE; -.
DR AlphaFoldDB; P0DP30; -.
DR SMR; P0DP30; -.
DR iPTMnet; P0DP30; -.
DR jPOST; P0DP30; -.
DR PRIDE; P0DP30; -.
DR Ensembl; ENSRNOT00000064679; ENSRNOP00000063822; ENSRNOG00000004060.
DR GeneID; 24242; -.
DR GeneID; 24244; -.
DR GeneID; 50663; -.
DR KEGG; rno:24242; -.
DR KEGG; rno:24244; -.
DR KEGG; rno:50663; -.
DR CTD; 801; -.
DR CTD; 805; -.
DR CTD; 808; -.
DR RGD; 2258; Calm2.
DR VEuPathDB; HostDB:ENSRNOG00000016770; -.
DR OMA; SCDRHPP; -.
DR OrthoDB; 1386217at2759; -.
DR PRO; PR:P0DP30; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004060; Expressed in Ammon's horn and 19 other tissues.
DR ExpressionAtlas; P0DP30; baseline and differential.
DR GO; GO:0034704; C:calcium channel complex; ISO:RGD.
DR GO; GO:1902494; C:catalytic complex; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:1990722; C:DAPK1-calmodulin complex; ISO:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0043209; C:myelin sheath; IDA:CAFA.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0030017; C:sarcomere; ISO:RGD.
DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR GO; GO:0000922; C:spindle pole; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0010856; F:adenylate cyclase activator activity; ISO:RGD.
DR GO; GO:0008179; F:adenylate cyclase binding; IDA:RGD.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0031997; F:N-terminal myristoylation domain binding; ISO:RGD.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IDA:RGD.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
DR GO; GO:0072542; F:protein phosphatase activator activity; ISO:RGD.
DR GO; GO:0031432; F:titin binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IDA:RGD.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:RGD.
DR GO; GO:0016240; P:autophagosome membrane docking; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:RGD.
DR GO; GO:0005513; P:detection of calcium ion; ISO:RGD.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IMP:CAFA.
DR GO; GO:0090151; P:establishment of protein localization to mitochondrial membrane; IMP:CAFA.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; ISO:RGD.
DR GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; ISO:RGD.
DR GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:1901842; P:negative regulation of high voltage-gated calcium channel activity; ISO:RGD.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0140056; P:organelle localization by membrane tethering; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:1904094; P:positive regulation of autophagic cell death; ISO:RGD.
DR GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; ISO:RGD.
DR GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:RGD.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:RGD.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISO:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:RGD.
DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:RGD.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; IMP:RGD.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0002834; P:regulation of response to tumor cell; ISO:RGD.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IDA:RGD.
DR GO; GO:1901339; P:regulation of store-operated calcium channel activity; IC:RGD.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IMP:CAFA.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:CAFA.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Metal-binding; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:201628, ECO:0000269|Ref.10"
FT CHAIN 2..149
FT /note="Calmodulin-2"
FT /id="PRO_0000439939"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 117..149
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 77..149
FT /note="Necessary and sufficient for interaction with PCP4"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:201628, ECO:0000269|Ref.10"
FT MOD_RES 22
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT MOD_RES 45
FT /note="Phosphothreonine; by CaMK4"
FT /evidence="ECO:0000269|PubMed:12392717"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT MOD_RES 100
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:201628"
FT MOD_RES 116
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62157"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:6ALE"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:6ALE"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:6ALE"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:6ALE"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:6ALE"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:6ALE"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:6ALE"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:6ALE"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:6ALE"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:6ALE"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:6ALE"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:6ALE"
SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK
