ID A9CP04_HUMAN Unreviewed; 699 AA. AC A9CP04; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 02-SEP-2026, entry version 106. DE RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027}; DE EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027}; GN Name=Par1b {ECO:0000313|EMBL:BAF96440.1}; 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 {ECO:0000313|EMBL:BAF96440.1}; RN [1] {ECO:0000313|EMBL:BAF96440.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18045904; DOI=10.1523/JNEUROSCI.3986-07.2007; RA Terabayashi T., Itoh T.J., Yamaguchi H., Yoshimura Y., Funato Y., Ohno S., RA Miki H.; RT "Polarity-regulating kinase partitioning-defective 1/microtubule affinity- RT regulating kinase 2 negatively regulates development of dendrites on RT hippocampal neurons."; RL J. Neurosci. 27:13098-13107(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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 Evidence={ECO:0000256|ARBA:ARBA00048679, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[tau protein] + ATP = O-phospho-L-seryl-[tau protein] CC + ADP + H(+); Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA- CC COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; CC Evidence={ECO:0000256|ARBA:ARBA00048291}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[tau protein] + ATP = O-phospho-L-threonyl-[tau CC protein] + ADP + H(+); Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, CC Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.26; Evidence={ECO:0000256|ARBA:ARBA00048878}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell CC projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cytoplasm, CC cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Lateral cell membrane CC {ECO:0000256|ARBA:ARBA00004124}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}. 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; AB271694; BAF96440.1; -; mRNA. DR AlphaFoldDB; A9CP04; -. DR IntAct; A9CP04; 1. DR PeptideAtlas; A9CP04; -. DR ChiTaRS; MARK2; human. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC. DR CDD; cd12201; MARK2_C; 1. DR CDD; cd14072; STKc_MARK; 1. DR CDD; cd14406; UBA_MARK2; 1. DR FunFam; 1.10.510.10:FF:001032; KP78b, isoform A; 1. DR FunFam; 1.10.8.10:FF:000013; Non-specific serine/threonine protein kinase; 1. DR FunFam; 3.30.200.20:FF:000003; Non-specific serine/threonine protein kinase; 1. DR FunFam; 3.30.310.80:FF:000001; Non-specific serine/threonine protein kinase; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR001772; KA1_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR049508; MARK1-4_cat. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR015940; UBA. DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1. DR PANTHER; PTHR24346:SF56; SERINE_THREONINE-PROTEIN KINASE MARK2; 1. DR Pfam; PF02149; KA1; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00627; UBA; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00165; UBA; 1. DR SUPFAM; SSF103243; KA1-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50032; KA1; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50030; UBA; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cell projection {ECO:0000256|ARBA:ARBA00023273}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212}; KW Developmental protein {ECO:0000256|ARBA:ARBA00022473}; KW Differentiation {ECO:0000256|ARBA:ARBA00022782}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00159}; Lipid-binding {ECO:0000256|ARBA:ARBA00023121}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PROSITE-ProRule:PRU00159}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00159}; Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}. FT DOMAIN 20..271 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 290..329 FT /note="UBA" FT /evidence="ECO:0000259|PROSITE:PS50030" FT DOMAIN 650..699 FT /note="KA1" FT /evidence="ECO:0000259|PROSITE:PS50032" FT REGION 340..553 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 384..398 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 399..411 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 433..452 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 142 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10027" FT BINDING 49 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 699 AA; 78423 MW; 914A23238FD74AC4 CRC64; MIRGRNSATS ADEQPHIGNY RLLKTIGKGN FAKVKLARHI LTGKEVAVKI IDKTQLNSSS LQKLFREVRI MKVLNHPNIV KLFEVIETEK TLYLVMEYAS GGEVFDYLVA HGRMKEKEAR AKFRQIVSAV QYCHQKFIVH RDLKAENLLL DADMNIKIAD FGFSNEFTFG NKLDTFCGSP PYAAPELFQG KKYDGPEVDV WSLGVILYTL VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK FLILNPSKRG TLEQIMKDRW MNVGHEDDEL KPYVEPLPDY KDPRRTELMV SMGYTREEIQ DSLVGQRYNE VMATYLLLGY KSSELEGDTI TLKPRPSADL TNSSAPSPSH KVQRSVSANP KQRRFSDQAG PAIPTSNSYS KKTQSNNAEN KRPEEDRESG RKASSTAKVP ASPLPGLERK KTTPTPSTNS VLSTSTNRSR NSPLLERASL GQASGLPPTE GNCEVPRPST APQRVPVASP SAHNISSSGG APDRTNFPRG VSSRSTFHAG QLRQVRDQQN LPYGVTPASP SGHSQGRRGA SGSIFSKFTS KFVRRNLNEP ESKDRVETLR PHVVGSGGND KEKEEFREAK PRSLRFTWSM KTTSSMEPNE MMREIRKVLD ANSCQSELHE KYMLLCMHGT PGHEDFVQWE MEVCKLPRLS LNGVRFKRIS GTSMAFKNIA SKIANELKL //