ID CDK5_BOVIN Reviewed; 292 AA. AC Q02399; Q0VCN5; Q6LBE2; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 2. DT 27-MAR-2024, entry version 189. DE RecName: Full=Cyclin-dependent kinase 5 {ECO:0000250|UniProtKB:Q00535}; DE EC=2.7.11.1; DE AltName: Full=Cell division protein kinase 5 {ECO:0000305}; DE AltName: Full=Cyclin-dependent-like kinase 5; DE AltName: Full=Proline-directed protein kinase 33 kDa subunit {ECO:0000303|PubMed:1464604}; DE Short=PDPK {ECO:0000303|PubMed:1464604}; DE AltName: Full=Serine/threonine-protein kinase PSSALRE {ECO:0000250|UniProtKB:Q03114}; DE AltName: Full=Tau protein kinase II catalytic subunit {ECO:0000303|PubMed:8253190}; DE Short=TPKII catalytic subunit {ECO:0000303|PubMed:8253190}; GN Name=CDK5 {ECO:0000250|UniProtKB:Q00535}; GN Synonyms=CDKN5 {ECO:0000250|UniProtKB:Q00535}, PSSALRE GN {ECO:0000250|UniProtKB:P49615}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 14-20 AND 218-251. RC TISSUE=Brain; RX PubMed=1464604; DOI=10.1016/s0021-9258(18)35696-5; RA Lew J., Winkfein R.J., Paudel H.K., Wang J.H.; RT "Brain proline-directed protein kinase is a neurofilament kinase which RT displays high sequence homology to p34cdc2."; RL J. Biol. Chem. 267:25922-25926(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=8253190; DOI=10.1016/0014-5793(93)80723-8; RA Kobayashi S., Ishiguro K., Omori A., Takamatsu M., Arioka M., Imahori K., RA Uchida T.; RT "A cdc2-related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit RT of tau protein kinase II, a proline-directed protein kinase associated with RT microtubule."; RL FEBS Lett. 335:171-175(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal cerebellum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Proline-directed serine/threonine-protein kinase essential CC for neuronal cell cycle arrest and differentiation and may be involved CC in apoptotic cell death in neuronal diseases by triggering abortive CC cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins. CC Phosphorylates SRC, NOS3, VIM/vimentin, p35/CDK5R1, MEF2A, SIPA1L1, CC SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5, SYN1, DNM1, AMPH, SYNJ1, CDK16, CC RAC1, RHOA, CDC42, TONEBP/NFAT5, MAPT/TAU, MAP1B, histone H1, p53/TP53, CC HDAC1, APEX1, PTK2/FAK1, huntingtin/HTT, ATM, MAP2, NEFH and NEFM. CC Regulates several neuronal development and physiological processes CC including neuronal survival, migration and differentiation, axonal and CC neurite growth, synaptogenesis, oligodendrocyte differentiation, CC synaptic plasticity and neurotransmission, by phosphorylating key CC proteins. Negatively regulates the CACNA1B/CAV2.2 -mediated Ca(2+) CC release probability at hippocampal neuronal soma and synaptic terminals CC (By similarity). Activated by interaction with CDK5R1 (p35) and CDK5R2 CC (p39), especially in postmitotic neurons, and promotes CDK5R1 (p35) CC expression in an autostimulation loop. Phosphorylates many downstream CC substrates such as Rho and Ras family small GTPases (e.g. PAK1, RAC1, CC RHOA, CDC42) or microtubule-binding proteins (e.g. MAPT/TAU, MAP2, CC MAP1B), and modulates actin dynamics to regulate neurite growth and/or CC spine morphogenesis. Phosphorylates also exocytosis associated proteins CC such as MCAM/MUC18, SEPT5, SYN1, and CDK16/PCTAIRE1 as well as CC endocytosis associated proteins such as DNM1, AMPH and SYNJ1 at CC synaptic terminals. In the mature central nervous system (CNS), CC regulates neurotransmitter movements by phosphorylating substrates CC associated with neurotransmitter release and synapse plasticity; CC synaptic vesicle exocytosis, vesicles fusion with the presynaptic CC membrane, and endocytosis. Promotes cell survival by activating anti- CC apoptotic proteins BCL2 and STAT3, and negatively regulating of CC JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response to CC genotoxic and oxidative stresses enhances its stabilization by CC preventing ubiquitin ligase-mediated proteasomal degradation, and CC induces transactivation of p53/TP53 target genes, thus regulating CC apoptosis. Phosphorylation of p35/CDK5R1 enhances its stabilization by CC preventing calpain-mediated proteolysis producing p25/CDK5R1 and CC avoiding ubiquitin ligase-mediated proteasomal degradation. During CC aberrant cell-cycle activity and DNA damage, p25/CDK5 activity elicits CC cell-cycle activity and double-strand DNA breaks that precedes neuronal CC death by deregulating HDAC1. DNA damage triggered phosphorylation of CC huntingtin/HTT in nuclei of neurons protects neurons against CC polyglutamine expansion as well as DNA damage mediated toxicity. CC Phosphorylation of PXN reduces its interaction with PTK2/FAK1 in CC matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) CC differentiation. Negative regulator of Wnt/beta-catenin signaling CC pathway. Activator of the GAIT (IFN-gamma-activated inhibitor of CC translation) pathway, which suppresses expression of a post- CC transcriptional regulon of proinflammatory genes in myeloid cells; CC phosphorylates the linker domain of glutamyl-prolyl tRNA synthetase CC (EPRS) in a IFN-gamma-dependent manner, the initial event in assembly CC of the GAIT complex. Phosphorylation of SH3GLB1 is required for CC autophagy induction in starved neurons. Phosphorylation of TONEBP/NFAT5 CC in response to osmotic stress mediates its rapid nuclear localization. CC MEF2 is inactivated by phosphorylation in nucleus in response to CC neurotoxin, thus leading to neuronal apoptosis. APEX1 AP- CC endodeoxyribonuclease is repressed by phosphorylation, resulting in CC accumulation of DNA damage and contributing to neuronal death. NOS3 CC phosphorylation down regulates NOS3-derived nitrite (NO) levels. SRC CC phosphorylation mediates its ubiquitin-dependent degradation and thus CC leads to cytoskeletal reorganization. May regulate endothelial cell CC migration and angiogenesis via the modulation of lamellipodia CC formation. Involved in dendritic spine morphogenesis by mediating the CC EFNA1-EPHA4 signaling. The complex p35/CDK5 participates in the CC regulation of the circadian clock by modulating the function of CLOCK CC protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates CC the transcriptional activity of the CLOCK-BMAL1 heterodimer in CC association with altered stability and subcellular distribution (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q03114}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; CC -!- ACTIVITY REGULATION: Inhibited by 2-(1-ethyl-2-hydroxyethylamino)-6- CC benzylamino-9-isopropylpurine (roscovitine), 1-isopropyl-4-aminobenzyl- CC 6-ether-linked benzimidazoles, resveratrol, AT-7519 and olomoucine. CC Activated by CDK5R1 (p35) and CDK5R2 (p39) during the development of CC the nervous system; degradation of CDK5R1 (p35) and CDK5R2 (p39) by CC proteasome result in down regulation of kinase activity, during this CC process, CDK5 phosphorylates p35 and induces its ubiquitination and CC subsequent degradation. Kinase activity is mainly determined by the CC amount of p35 available and subcellular location; reversible CC association to plasma membrane inhibits activity. Long-term CC inactivation as well as CDK5R1 (p25)-mediated hyperactivation of CDK5 CC triggers cell death. The pro-death activity of hyperactivated CDK5 is CC suppressed by membrane association of CDK5, via myristoylation of p35. CC Brain-derived neurotrophic factor, glial-derived neurotrophic factor, CC nerve growth factor (NGF), retinoic acid, laminin and neuregulin CC promote activity. Neurotoxicity enhances nuclear activity, thus leading CC to MEF2 phosphorylation and inhibition prior to apoptosis of cortical CC neurons. Repression by GSTP1 via p25/p35 translocation prevents CC neurodegeneration (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Heterodimer composed of a catalytic subunit CDK5 and a CC regulatory subunit CDK5R1 (p25) and macromolecular complex composed of CC at least CDK5, CDK5R1 (p35) and CDK5RAP1 or CDK5RAP2 or CDK5RAP3. Only CC the heterodimer shows kinase activity. Under neurotoxic stress and CC neuronal injury conditions, p35 is cleaved by calpain to generate p25 CC that hyperactivates CDK5, that becomes functionally disabled and often CC toxic. Found in a trimolecular complex with CABLES1 and ABL1. Interacts CC with CABLES1 and CABLES2 (By similarity). Interacts with AATK and CC GSTP1. Binds to HDAC1 when in complex with p25. Interaction with CC myristoylation p35 promotes CDK5 association with membranes. Both CC isoforms 1 and 2 interacts with beta-catenin/CTNNB1. Interacts with CC delta-catenin/CTNND2 and APEX1. Interacts with P53/TP53 in neurons (By CC similarity). Interacts with EPHA4; may mediate the activation of NGEF CC by EPHA4. Interacts with PTK2/FAK1. The complex p35/CDK5 interacts with CC CLOCK (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00535}. Cytoplasm CC {ECO:0000250|UniProtKB:P49615}. Cell membrane CC {ECO:0000250|UniProtKB:Q00535}; Peripheral membrane protein CC {ECO:0000250}. Perikaryon {ECO:0000250}. Cell projection, lamellipodium CC {ECO:0000250|UniProtKB:P49615}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:P49615}. Nucleus {ECO:0000250}. Postsynaptic CC density {ECO:0000250|UniProtKB:Q03114}. Synapse CC {ECO:0000250|UniProtKB:Q03114}. Note=In axonal growth cone with CC extension to the peripheral lamellipodia (By similarity). Under CC neurotoxic stress and neuronal injury conditions, CDK5R1 (p35) is CC cleaved by calpain to generate CDK5R1 (p25) in response to increased CC intracellular calcium. The elevated level of p25, when in complex with CC CDK5, leads to its subcellular misallocation as well as its CC hyperactivation. Colocalizes with CTNND2 in the cell body of neuronal CC cells, and with CTNNB1 in the cell-cell contacts and plasma membrane of CC undifferentiated and differentiated neuroblastoma cells. Reversibly CC attached to the plasma membrane in an inactive form when complexed to CC dephosphorylated p35 or CDK5R2 (p39), p35 phosphorylation releases this CC attachment and activates CDK5 (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylation on Tyr-15 by ABL1 and FYN, and on Ser-159 by CC casein kinase 1 promotes kinase activity. By contrast, phosphorylation CC at Thr-14 inhibits activity (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylation at Ser-159 is essential for maximal catalytic CC activity. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. 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; L04798; AAA30606.1; -; mRNA. DR EMBL; X82440; CAA57821.1; -; mRNA. DR EMBL; BC120083; AAI20084.1; -; mRNA. DR RefSeq; NP_776442.1; NM_174017.2. DR AlphaFoldDB; Q02399; -. DR SMR; Q02399; -. DR BioGRID; 158435; 2. DR CORUM; Q02399; -. DR IntAct; Q02399; 3. DR STRING; 9913.ENSBTAP00000010212; -. DR BindingDB; Q02399; -. DR ChEMBL; CHEMBL5169144; -. DR iPTMnet; Q02399; -. DR PaxDb; 9913-ENSBTAP00000010212; -. DR Ensembl; ENSBTAT00000010212.6; ENSBTAP00000010212.5; ENSBTAG00000007766.6. DR GeneID; 281066; -. DR KEGG; bta:281066; -. DR CTD; 1020; -. DR VEuPathDB; HostDB:ENSBTAG00000007766; -. DR VGNC; VGNC:27127; CDK5. DR eggNOG; KOG0662; Eukaryota. DR GeneTree; ENSGT00940000160805; -. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; Q02399; -. DR OMA; WPGISQY; -. DR OrthoDB; 244018at2759; -. DR TreeFam; TF101023; -. DR BRENDA; 2.7.11.22; 908. DR Reactome; R-BTA-180024; DARPP-32 events. DR Reactome; R-BTA-399956; CRMPs in Sema3A signaling. DR Reactome; R-BTA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Proteomes; UP000009136; Chromosome 4. DR Bgee; ENSBTAG00000007766; Expressed in oocyte and 105 other cell types or tissues. DR GO; GO:0030424; C:axon; ISS:AgBase. DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; ISS:AgBase. DR GO; GO:0005829; C:cytosol; ISS:AgBase. DR GO; GO:0030425; C:dendrite; ISS:AgBase. DR GO; GO:0030175; C:filopodium; ISS:AgBase. DR GO; GO:0030426; C:growth cone; ISS:AgBase. DR GO; GO:0030027; C:lamellipodium; ISS:AgBase. DR GO; GO:0016020; C:membrane; ISS:AgBase. DR GO; GO:0031594; C:neuromuscular junction; ISS:AgBase. DR GO; GO:0043025; C:neuronal cell body; ISS:AgBase. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISS:AgBase. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB. DR GO; GO:0016533; C:protein kinase 5 complex; IEA:Ensembl. DR GO; GO:0030549; F:acetylcholine receptor activator activity; ISS:AgBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0005176; F:ErbB-2 class receptor binding; ISS:AgBase. DR GO; GO:0043125; F:ErbB-3 class receptor binding; ISS:UniProtKB. DR GO; GO:0035173; F:histone kinase activity; TAS:UniProtKB. DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl. DR GO; GO:0016301; F:kinase activity; ISS:AgBase. DR GO; GO:0002039; F:p53 binding; IEA:Ensembl. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:AgBase. DR GO; GO:0050321; F:tau-protein kinase activity; ISS:AgBase. DR GO; GO:0007409; P:axonogenesis; ISS:AgBase. DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl. DR GO; GO:0070509; P:calcium ion import; IEA:Ensembl. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0016477; P:cell migration; ISS:AgBase. DR GO; GO:0007160; P:cell-matrix adhesion; ISS:AgBase. DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl. DR GO; GO:0021697; P:cerebellar cortex formation; IEA:Ensembl. DR GO; GO:0022038; P:corpus callosum development; IEA:Ensembl. DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl. DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl. DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl. DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl. DR GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl. DR GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl. DR GO; GO:0030517; P:negative regulation of axon extension; IEA:Ensembl. DR GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IEA:Ensembl. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl. DR GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl. DR GO; GO:0031914; P:negative regulation of synaptic plasticity; IEA:Ensembl. DR GO; GO:0051402; P:neuron apoptotic process; IBA:GO_Central. DR GO; GO:0030182; P:neuron differentiation; ISS:AgBase. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0031175; P:neuron projection development; ISS:AgBase. DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IEA:Ensembl. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl. DR GO; GO:0035418; P:protein localization to synapse; IEA:Ensembl. DR GO; GO:0032801; P:receptor catabolic process; IEA:Ensembl. DR GO; GO:0043113; P:receptor clustering; IEA:Ensembl. DR GO; GO:0030334; P:regulation of cell migration; ISS:AgBase. DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB. DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB. DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0014044; P:Schwann cell development; IEA:Ensembl. DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl. DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl. DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl. DR GO; GO:0001963; P:synaptic transmission, dopaminergic; IEA:Ensembl. DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl. DR GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central. DR GO; GO:0008542; P:visual learning; IEA:Ensembl. DR CDD; cd07839; STKc_CDK5; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF46; CYCLIN-DEPENDENT KINASE 5; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW Acetylation; Apoptosis; ATP-binding; Biological rhythms; Cell cycle; KW Cell division; Cell membrane; Cell projection; Cytoplasm; KW Direct protein sequencing; Kinase; Membrane; Neurodegeneration; KW Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Synapse; Transferase. FT CHAIN 1..292 FT /note="Cyclin-dependent kinase 5" FT /id="PRO_0000085783" FT DOMAIN 4..286 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 126 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 10..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 15 FT /note="Phosphotyrosine; by ABL1, EPHA4 and FYN" FT /evidence="ECO:0000250|UniProtKB:Q00535" FT MOD_RES 17 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q00535" FT MOD_RES 56 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q00535" FT MOD_RES 72 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q00535" FT MOD_RES 159 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q00535" FT CONFLICT 61 FT /note="K -> E (in Ref. 3; AAI20084)" FT /evidence="ECO:0000305" FT CONFLICT 151 FT /note="F -> L (in Ref. 3; AAI20084)" FT /evidence="ECO:0000305" FT CONFLICT 169 FT /note="P -> S (in Ref. 1; AAA30606)" FT /evidence="ECO:0000305" SQ SEQUENCE 292 AA; 33288 MW; 4CB11CED9017D535 CRC64; MQKYEKLEKI GEGTYGTVFK AKNRETHEIV ALKRVRLDDD DEGVPSSALR EICLLKELKH KNIVRLHDVL HSDKKLTLVF EFCDQDLKKY FDSCNGDLDP EIVKSFLFQL LKGLGFCHSR NVLHRDLKPQ NLLINRNGEL KLADFGLARA FGIPVRCYSA EVVTLWYRPP DVLFGAKLYS TSIDMWSAGC IFAELANAGR PLFPGNDVDD QLKRIFRLLG TPTEEQWPAM TKLPDYKPYP MYPATTSLVN VVPKLNATGR DLLQNLLKCN PVQRISAEEA LQHPYFSDFC PP //