CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017268
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ERC protein 2 
Protein Synonyms/Alias
 CAZ-associated structural protein 1; CAST1; Cast; Cytomatrix protein p110 
Gene Name
 Erc2 
Gene Synonyms/Alias
 Cast1; Cmbp 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
833TQQSLAEKEAHLANLacetylation[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
 Thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act together with BSN. May recruit liprin-alpha proteins to the CAZ. 
Sequence Annotation
 REGION 760 957 Involved in binding to RIMS1.
 MOD_RES 14 14 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Cell junction; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Phosphoprotein; Reference proteome; Synapse; Synaptosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 957 AA 
Protein Sequence
MYGSARTISN PEGSPSRSPR LPRSPRLGHR RTSSGGGGGT GKTLSMENIQ SLNAAYATSG 60
PMYLSDHEGV ASTTYPKGTM TLGRATNRAV YGGRVTAMGS SPNIASAGLS HTDVLSYTDQ 120
HGGLGGSSHH HHHQVPSMLR QVRDSTMLDL QAQLKELQRE NDLLRKELDI KDSKLGSSMN 180
SIKTFWSPEL KKERVLRKEE AARMSVLKEQ MRVSHEENQH LQLTIQALQD ELRTQRDLNH 240
LLQQESGNRG AEHFTIELTE ENFRRLQAEH DRQAKELFLL RKTLEEMELR IETQKQTLNA 300
RDESIKKLLE MLQSKGLPSK SLEDDNERTR RMAEAESQVS HLEVILDQKE KENIHLREEL 360
HRRSQLQPEP AKTKALQTVI EMKDTKIASL ERNIRDLEDE IQMLKANGVL NTEDREEEIK 420
QIEVYKSHSK FMKTKNDQLK QELSKKESEL LALQTKLETL SNQNSDCKQH IEVLKESLTA 480
KEQRAAILQT EVDALRLRLE EKESFLNKKT KQLQDLTEEK GTLAGEIRDM KDMLEVKERK 540
INVLQKKIEN LQEQLRDKDK QLTNLKDRVK SLQTDSSNTD TALATLEEAL SEKERIIERL 600
KEQRERDDRE RLEEIESFRK ENKDLKEKVN ALQAELTEKE SSLIDLKEHA SSLASAGLKR 660
DSKLKSLEIA IEQKKEECNK LEAQLKKAHN IEDDSRMNPE FADRLKQLDK EASYYRDECG 720
KAQAEVDRLL EILKEVENEK NDKDKKIAEL ESLTLRHMKD QNKKVANLKH NQQLEKKKNA 780
QLLEEVRRRE FSMVDNSQHL QIEELMNALE KTRQELDATK ARLASTQQSL AEKEAHLANL 840
RMERRKQLEE ILEMKQEALL AAISEKDANI ALLELSASKK KKTQEEVMAL KREKDRLVHQ 900
LKQQTQNRMK LMADNYDDDH HHYHHHHHHH HHRSPGRSQH SNHRPSPDQD DEEGIWA 957 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005783; C:endoplasmic reticulum; NAS:UniProtKB.
 GO:0030426; C:growth cone; IDA:UniProtKB.
 GO:0043025; C:neuronal cell body; IDA:RGD.
 GO:0014069; C:postsynaptic density; IDA:RGD.
 GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0043195; C:terminal bouton; IDA:RGD.
 GO:0030165; F:PDZ domain binding; NAS:UniProtKB.
 GO:0032403; F:protein complex binding; IDA:RGD.
 GO:0007416; P:synapse assembly; NAS:UniProtKB. 
Interpro
 IPR019323; CAZ_cplx_RIM-bd_prot. 
Pfam
 PF10174; Cast 
SMART
  
PROSITE
  
PRINTS