CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-035821
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Protein Kank1 
Protein Synonyms/Alias
  
Gene Name
 Kank1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
149RHNLHVTKTLMETRRacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
  
Sequence Annotation
  
Keyword
 ANK repeat; Complete proteome; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1353 AA 
Protein Sequence
MAVLLENADG VLNGDRNKEK KDPYFVETPY GFQLDLDFVK YVDDIQKGNT IKKLNIQKRR 60
KPSGPCAEVR AIPGPQGVWT STESLSSSNS DDSKQCPSFL LARSHVTSTP IPRPPAPLET 120
SPTFAISENR QLLPPPSPQL PRHNLHVTKT LMETRRRLEQ ERVTMQMAPG EFRRPRLASF 180
GGMGSTSSLP SFMGSGNHSS AMHQLQNGYQ GNGDYSSYVP AVPTTSSMGS SVRHSPLSSG 240
ISTPVTNVSP MHLQHIREQM AIALKRLKEL EEQVRTIPVL QVKISVLQEE KRQLASQLKN 300
QRAASQNEAC GVRKRSYSAG NASQLELLSR ARRGGGELYI DYEEEEMESV EQSTQRIREF 360
RQLTADMQAL EQKIQDSSCE ATPELRENGQ CASRERKSVA VGSDENMNDI VVYHRDFRSR 420
KDTAVGTVTE TRNFGISVTE AMLGVITEAD KEIELQQQTI EALKEKIYRL EVQLKETTHD 480
QEMTKLKQEL QAAGSRKKVD KAIMAQPLVF SKLVEALVPT REQMVGSHVD TMDSCVGTSV 540
QTSSVGTSCH PDRKNQVVGP ELPMNWWVVK ERVGTHDRCV GRSVETCNRS VGVEVSVCET 600
GSNTEASGSD LTLLKTNLNL KDVRSIGCGD CSVDVIVCLP KECTSRSMNT EAVGQGEAAV 660
MAVPHTTDQH TSTNLERVDQ GTNTEVTTLV ESCTNTLLST LDKQTSTQNV EMRTVAIGEG 720
RVRDINPSTK TRSVGVGTVL SGSSDFDKPC AVKTKESGVG QINIHDNYLV GLKMRTIACG 780
PPQLTVGLIG SRRSVGVGNE PVGDLLEDPL QPQVPSGMMT GLDHYIERVQ KLLAEQQTLL 840
AENYSELAEA FGEPHSQIGS LNSQLISTLS SINSVMKSAS TEELRNPDFQ KSSLGKIAGN 900
HLECTCKCGG LRSGGLVNVQ TSQPEVETET TEGKRGCEQF LTQGNTLPPV NLTDDQIATG 960
LYVCPNNENT LKSIMKKSDG NKDSNGAKKN LQFIGVNGGY ETTSSDDSSS GGSSSSESDD 1020
ECDTNGYPPE EEEEEEEEEE DHDTRGMAEG RHAVNIEGFQ SARVEDEVQV PECEPEKEEI 1080
RERYELSEKM LSACSLLKYN INDPKALASK DMRICLNTLQ HEWFRVSSQK SAVPAMVGDY 1140
IAAFEAVSPD VLRYIINMAD GNGNTALHYS VSHSNFQIVK LLLDADVCNV DHQNKAGYTP 1200
IMLAALAAVE AEKDMQVVEE LFSCGDVNAK ASQAGQTALM LAVSHGRIDM VKGLLACGAD 1260
VNIQDDEGST ALMCASEHGH VEIVKLLLAQ PGCSGHLEDN DGSTALSIAL EAGHKDIAVL 1320
LYAHLNFSKA QSPSTPRLGR KTSPGPTHRG SFD 1353 
Gene Ontology
 GO:0032587; C:ruffle membrane; IEA:Compara.
 GO:0030837; P:negative regulation of actin filament polymerization; IEA:Compara.
 GO:0030336; P:negative regulation of cell migration; IEA:Compara.
 GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Compara.
 GO:2000393; P:negative regulation of lamellipodium morphogenesis; IEA:Compara.
 GO:0010977; P:negative regulation of neuron projection development; IEA:Compara.
 GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Compara.
 GO:1900028; P:negative regulation of ruffle assembly; IEA:Compara.
 GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IEA:Compara.
 GO:0035413; P:positive regulation of catenin import into nucleus; IEA:Compara.
 GO:0030177; P:positive regulation of Wnt receptor signaling pathway; IEA:Compara.
 GO:0090303; P:positive regulation of wound healing; IEA:Compara.
 GO:2000114; P:regulation of establishment of cell polarity; IEA:Compara. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR021939; KN_motif. 
Pfam
 PF12796; Ank_2
 PF12075; KN_motif 
SMART
 SM00248; ANK 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT 
PRINTS