CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023173
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Neurabin-1 
Protein Synonyms/Alias
 Neurabin-I; Neural tissue-specific F-actin-binding protein I; Protein phosphatase 1 regulatory subunit 9A 
Gene Name
 PPP1R9A 
Gene Synonyms/Alias
 KIAA1222 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
777LIKDFQQKELDFIKRubiquitination[1]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473
Functional Description
 Binds to actin filaments (F-actin) and shows cross- linking activity. Binds along the sides of the F-actin. May be involved in neurite formation. Inhibits protein phosphatase 1- alpha activity (By similarity). 
Sequence Annotation
 DOMAIN 504 592 PDZ.
 DOMAIN 988 1051 SAM.
 REGION 1 144 Actin-binding.
 REGION 425 502 Interacts with protein phosphatase 1 (By
 REGION 597 1090 Interacts with TGN38 (By similarity).
 MOD_RES 338 338 Phosphoserine.
 MOD_RES 460 460 Phosphoserine; by PKA (By similarity).
 MOD_RES 840 840 Phosphoserine.  
Keyword
 3D-structure; Actin-binding; Alternative splicing; Cell junction; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; Neurogenesis; Phosphoprotein; Polymorphism; Reference proteome; Synapse; Synaptosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1098 AA 
Protein Sequence
MLKTESSGER TTLRSASPHR NAYRTEFQAL KSTFDKPKSD GEQKTKEGEG SQQSRGRKYG 60
SNVNRIKNLF MQMGMEPNEN AAVIAKTRGK GGHSSPQRRM KPKEFLEKTD GSVVKLESSV 120
SERISRFDTM YDGPSYSKFT ETRKMFERSV HESGQNNRYS PKKEKAGGSE PQDEWGGSKS 180
NRGSTDSLDS LSSRTEAVSP TVSQLSAVFE NTDSPSAIIS EKAENNEYSV TGHYPLNLPS 240
VTVTNLDTFG HLKDSNSWPP SNKRGVDTED AHKSNATPVP EVASKSTSLA SIPGEEIQQS 300
KEPEDSTSNQ QTPDSIDKDG PEEPCAESKA MPKSEIPSPQ SQLLEDAEAN LVGREAAKQQ 360
RKELAGGDFT SPDASASSCG KEVPEDSNNF DGSHVYMHSD YNVYRVRSRY NSDWGETGTE 420
QDEEEDSDEN SYYQPDMEYS EIVGLPEEEE IPANRKIKFS SAPIKVFNTY SNEDYDRRND 480
EVDPVAASAE YELEKRVEKL ELFPVELEKD EDGLGISIIG MGVGADAGLE KLGIFVKTVT 540
EGGAAQRDGR IQVNDQIVEV DGISLVGVTQ NFAATVLRNT KGNVRFVIGR EKPGQVSEVA 600
QLISQTLEQE RRQRELLEQH YAQYDADDDE TGEYATDEEE DEVGPVLPGS DMAIEVFELP 660
ENEDMFSPSE LDTSKLSHKF KELQIKHAVT EAEIQKLKTK LQAAENEKVR WELEKTQLQQ 720
NIEENKERML KLESYWIEAQ TLCHTVNEHL KETQSQYQAL EKKYNKAKKL IKDFQQKELD 780
FIKRQEAERK KIEDLEKAHL VEVQGLQVRI RDLEAEVFRL LKQNGTQVNN NNNIFERRTS 840
LGEVSKGDTM ENLDGKQTSC QDGLSQDLNE AVPETERLDS KALKTRAQLS VKNRRQRPSR 900
TRLYDSVSST DGEDSLERKN FTFNDDFSPS STSSADLSGL GAEPKTPGLS QSLALSSDES 960
LDMIDDEILD DGQSPKHSQC QNRAVQEWSV QQVSHWLMSL NLEQYVSEFS AQNITGEQLL 1020
QLDGNKLKAL GMTASQDRAV VKKKLKEMKM SLEKARKAQE KMEKQREKLR RKEQEQMQRK 1080
SKKTEKMTST TAEGAGEQ 1098 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0030864; C:cortical actin cytoskeleton; IEA:Compara.
 GO:0043197; C:dendritic spine; IEA:Compara.
 GO:0030175; C:filopodium; IEA:Compara.
 GO:0030426; C:growth cone; IEA:Compara.
 GO:0045202; C:synapse; IEA:UniProtKB-KW.
 GO:0007015; P:actin filament organization; IEA:Compara.
 GO:0019722; P:calcium-mediated signaling; IEA:Compara.
 GO:0031175; P:neuron projection development; IEA:Compara. 
Interpro
 IPR001478; PDZ.
 IPR001660; SAM.
 IPR013761; SAM/pointed.
 IPR011510; SAM_2. 
Pfam
 PF00595; PDZ
 PF07647; SAM_2 
SMART
 SM00228; PDZ
 SM00454; SAM 
PROSITE
 PS50106; PDZ
 PS50105; SAM_DOMAIN 
PRINTS