Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neurabin-1

Gene

Ppp1r9a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction.

GO - Molecular functioni

  • actin filament binding Source: WormBase
  • GTPase binding Source: RGD
  • ion channel binding Source: RGD
  • protein complex binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • protein phosphatase 1 binding Source: RGD

GO - Biological processi

  • actin filament organization Source: Ensembl
  • aging Source: RGD
  • calcium-mediated signaling Source: Ensembl
  • cellular response to toxic substance Source: RGD
  • excitatory postsynaptic potential Source: RGD
  • negative regulation of long-term synaptic potentiation Source: RGD
  • negative regulation of spontaneous neurotransmitter secretion Source: RGD
  • negative regulation of stress fiber assembly Source: RGD
  • neuron development Source: RGD
  • neuron projection development Source: MGI
  • positive regulation of dendritic spine development Source: RGD
  • positive regulation of long term synaptic depression Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • positive regulation of protein kinase activity Source: RGD
  • regulation of actin filament polymerization Source: RGD
  • regulation of dendritic spine morphogenesis Source: RGD
  • regulation of filopodium assembly Source: RGD
  • regulation of synapse assembly Source: RGD
  • regulation of synapse structural plasticity Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Neurabin-1
Alternative name(s):
Neurabin-I
Neural tissue-specific F-actin-binding protein I
PP1bp175
Protein phosphatase 1 regulatory subunit 9A
p180
Gene namesi
Name:Ppp1r9a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi632280. Ppp1r9a.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: RGD
  • cell junction Source: UniProtKB-KW
  • cortical actin cytoskeleton Source: Ensembl
  • cytoskeleton Source: MGI
  • cytosol Source: RGD
  • dendrite Source: RGD
  • dendritic spine Source: RGD
  • dendritic spine neck Source: RGD
  • filopodium Source: RGD
  • growth cone Source: MGI
  • growth cone lamellipodium Source: RGD
  • lamellipodium Source: RGD
  • neuromuscular junction Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • postsynaptic density Source: RGD
  • synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi461 – 4611S → E: 35-fold decrease in inhibition of PP1-alpha. 1 Publication
Mutagenesisi516 – 5172GI → AA: Abolishes P70-S6K binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10951095Neurabin-1PRO_0000071508Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921PhosphoserineCombined sources
Modified residuei312 – 3121PhosphothreonineCombined sources
Modified residuei338 – 3381PhosphoserineBy similarity
Modified residuei372 – 3721PhosphoserineCombined sources
Modified residuei461 – 4611Phosphoserine; by PKA1 Publication
Modified residuei841 – 8411PhosphoserineBy similarity
Modified residuei916 – 9161PhosphoserineCombined sources
Modified residuei929 – 9291PhosphoserineCombined sources
Modified residuei957 – 9571PhosphoserineCombined sources
Modified residuei958 – 9581PhosphoserineCombined sources
Modified residuei961 – 9611PhosphoserineCombined sources
Modified residuei975 – 9751PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO35867.
PRIDEiO35867.

PTM databases

iPTMnetiO35867.
PhosphoSiteiO35867.

Expressioni

Tissue specificityi

Brain, and widely expressed in neural tissue. Highly concentrated in synapses of developed neurons. In developing neurons, concentrated in the lamellipodia of the growth cone.

Gene expression databases

GenevisibleiO35867. RN.

Interactioni

Subunit structurei

Possibly exists as a homodimer, homotrimer or a homotetramer. Interacts with F-actin, protein phosphatase 1 (PP1), neurabin-2, TGN38 and p70-S6K.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ppp1cbP621422EBI-7092421,EBI-352326
Ppp1ccP630882EBI-7092421,EBI-80049
Rps6kb1P679994EBI-7092421,EBI-2639458

GO - Molecular functioni

  • actin filament binding Source: WormBase
  • GTPase binding Source: RGD
  • ion channel binding Source: RGD
  • protein complex binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • protein phosphatase 1 binding Source: RGD

Protein-protein interaction databases

BioGridi250039. 2 interactions.
DIPiDIP-40850N.
IntActiO35867. 3 interactions.
MINTiMINT-107263.
STRINGi10116.ENSRNOP00000011756.

Structurei

Secondary structure

1
1095
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi440 – 4434Combined sources
Beta strandi465 – 4706Combined sources
Turni473 – 4753Combined sources
Helixi485 – 49814Combined sources
Beta strandi501 – 5099Combined sources
Beta strandi516 – 5227Combined sources
Beta strandi527 – 5293Combined sources
Beta strandi530 – 54011Combined sources
Helixi545 – 5495Combined sources
Beta strandi550 – 5523Combined sources
Beta strandi557 – 5615Combined sources
Helixi571 – 58010Combined sources
Beta strandi583 – 5919Combined sources
Helixi986 – 9883Combined sources
Helixi992 – 9943Combined sources
Helixi995 – 10006Combined sources
Turni1001 – 10033Combined sources
Helixi1004 – 10107Combined sources
Turni1011 – 10144Combined sources
Helixi1017 – 10215Combined sources
Helixi1025 – 10295Combined sources
Turni1030 – 10323Combined sources
Helixi1036 – 104712Combined sources
Helixi1049 – 10557Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FN5NMR-A502-592[»]
2GLENMR-A986-1056[»]
3HVQX-ray2.20C/D426-592[»]
ProteinModelPortaliO35867.
SMRiO35867. Positions 501-594, 986-1056.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35867.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini505 – 59389PDZPROSITE-ProRule annotationAdd
BLAST
Domaini989 – 105264SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 144144Actin-bindingAdd
BLAST
Regioni426 – 50378Interacts with protein phosphatase 1Add
BLAST
Regioni598 – 1091494Interacts with TGN38Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili598 – 62831Sequence analysisAdd
BLAST
Coiled coili674 – 825152Sequence analysisAdd
BLAST
Coiled coili1036 – 109156Sequence analysisAdd
BLAST

Domaini

Interacts with p70-S6K via its PDZ domain.
The PP1 binding region is natively unstructured, upon PP1 binding, it acquires structure, blocks a substrate-binding site, and restricts PP1 phosphatase specificity to a subset of substrates.

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1945. Eukaryota.
ENOG410Y7F2. LUCA.
GeneTreeiENSGT00390000010033.
HOGENOMiHOG000252962.
HOVERGENiHBG005213.
InParanoidiO35867.
KOiK17551.
OMAiSPKHSQC.
OrthoDBiEOG7XM2WV.
PhylomeDBiO35867.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR029994. Neurabin-1.
IPR001478. PDZ.
IPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PANTHERiPTHR16154:SF22. PTHR16154:SF22. 1 hit.
PfamiPF00595. PDZ. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35867-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKAESSGER TTLRSASPHR NAYRTEFQAL KSTFDKPKPD GEQKTKEGEG
60 70 80 90 100
SQQSRGRKYG SNVNRIKNLF MQMGMEPNEN AAIIAKTRGK GRPSSPQKRM
110 120 130 140 150
KPKEFVEKTD GSVVKLESSV SERISRFDTM HDGPSYAKFT ETRKMFERSG
160 170 180 190 200
HESGQNNRHS PKKEKAGEAE PQDEWGGSKS NRGSSDSLDS LSPRTEAVSP
210 220 230 240 250
TVSQLSAVFE NSESPGAITP GKAENSNYSV TGHYPLNLPS VTVTNLDTFG
260 270 280 290 300
RLKDSNSRPS SNKQATDTEE PEKSEAVPVP EVAQKGTSLA SLPSEERQLS
310 320 330 340 350
TEAEDVTAQP DTPDSTDKDS PGEPSAESQA MPKSNTLSRP KEPLEDAEAN
360 370 380 390 400
VVGSEAEQPQ RRDLTGGGDL TSPDASASSC GKEVPEDSNS FEGSHVYMHS
410 420 430 440 450
DYNVYRVRSR YNSDWGETGT EQDEGDDSDE NNYYQPDMEY SEIVGLPQEE
460 470 480 490 500
EIPANRKIKF SCAPIKVFNT YSNEDYDRRN DDVDPVAASA EYELEKRVEK
510 520 530 540 550
LELFPVELEK DEDGLGISII GMGVGADAGL EKLGIFVKTV TEGGAAQRDG
560 570 580 590 600
RIQVNDQIVE VDGISLVGVT QNFAATVLRN TKGNVRFVIG REKPGQVSEV
610 620 630 640 650
AQLISQTLEQ ERRQRELLER HYAQYDADDD ETGEYATDEE EDEVGPILPG
660 670 680 690 700
GDMAIEVFEL PENEDMFSPS DLDTSKLSHK FKELQIKHAV TEAEIQKLKT
710 720 730 740 750
KLQAAENEKV RWELEKNQLQ QNIEENKERM VKLESYWIEA QTLCHTVNEH
760 770 780 790 800
LKETQSQYQA LEKKYNKAKK LIKDFQQKEL DFIRRQEVER KKLEEVEKAH
810 820 830 840 850
LVEVQGLQVR IRDLEAEVFR LLKQNGTQVN NNNNIFERRP SPGEVSKGDT
860 870 880 890 900
MENVEVKQTS CQDGLSQDLN EAVPETERLD SKALKTRAQL SVKNRRQRPT
910 920 930 940 950
RTRLYDSVSS TDGEDSLERK NFTFNDDFSP SSTSSADLSG LGAEPKTPGL
960 970 980 990 1000
SQSLALSSDE SLDMIDDEIL DDGQSPKHTQ SQSRAVHEWS VQQVSHWLVG
1010 1020 1030 1040 1050
LSLDQYVSEF SAQNISGEQL LQLDGNKLKA LGMTSSQDRA LVKKKLKEMK
1060 1070 1080 1090
MSLEKARKAQ EKMEKQREKL RRKEQEQMQR KSKKSEKMTS TTEQP
Length:1,095
Mass (Da):122,735
Last modified:January 1, 1998 - v1
Checksum:i58E3650320B3BD61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72994 mRNA. Translation: AAC53454.1.
PIRiT43275.
RefSeqiNP_445925.1. NM_053473.2.
UniGeneiRn.10849.

Genome annotation databases

EnsembliENSRNOT00000011756; ENSRNOP00000011756; ENSRNOG00000008869.
GeneIDi84685.
KEGGirno:84685.
UCSCiRGD:632280. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72994 mRNA. Translation: AAC53454.1.
PIRiT43275.
RefSeqiNP_445925.1. NM_053473.2.
UniGeneiRn.10849.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FN5NMR-A502-592[»]
2GLENMR-A986-1056[»]
3HVQX-ray2.20C/D426-592[»]
ProteinModelPortaliO35867.
SMRiO35867. Positions 501-594, 986-1056.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250039. 2 interactions.
DIPiDIP-40850N.
IntActiO35867. 3 interactions.
MINTiMINT-107263.
STRINGi10116.ENSRNOP00000011756.

PTM databases

iPTMnetiO35867.
PhosphoSiteiO35867.

Proteomic databases

PaxDbiO35867.
PRIDEiO35867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011756; ENSRNOP00000011756; ENSRNOG00000008869.
GeneIDi84685.
KEGGirno:84685.
UCSCiRGD:632280. rat.

Organism-specific databases

CTDi55607.
RGDi632280. Ppp1r9a.

Phylogenomic databases

eggNOGiKOG1945. Eukaryota.
ENOG410Y7F2. LUCA.
GeneTreeiENSGT00390000010033.
HOGENOMiHOG000252962.
HOVERGENiHBG005213.
InParanoidiO35867.
KOiK17551.
OMAiSPKHSQC.
OrthoDBiEOG7XM2WV.
PhylomeDBiO35867.

Miscellaneous databases

EvolutionaryTraceiO35867.
NextBioi617270.
PROiO35867.

Gene expression databases

GenevisibleiO35867. RN.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR029994. Neurabin-1.
IPR001478. PDZ.
IPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PANTHERiPTHR16154:SF22. PTHR16154:SF22. 1 hit.
PfamiPF00595. PDZ. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Neurabin: a novel neural tissue-specific actin filament-binding protein involved in neurite formation."
    Nakanishi H., Obaishi H., Satoh A., Wada M., Mandai K., Satoh K., Nishioka H., Matsuura Y., Mizoguchi A., Takai Y.
    J. Cell Biol. 139:951-961(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 4-21; 180-211; 286-311; 467-482; 501-532; 710-715 AND 779-790.
    Tissue: Brain.
  2. "Neurabin is a synaptic protein linking p70 S6 kinase and the neuronal cytoskeleton."
    Burnett P.E., Blackshaw S., Lai M.M., Qureshi I.A., Burnett A.F., Sabatini D.M., Snyder S.H.
    Proc. Natl. Acad. Sci. U.S.A. 95:8351-8356(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Brain.
  3. "Brain actin-associated protein phosphatase 1 holoenzymes containing spinophilin, neurabin, and selected catalytic subunit isoforms."
    MacMillan L.B., Bass M.A., Cheng N., Howard E.F., Tamura M., Strack S., Wadzinski B.E., Colbran R.J.
    J. Biol. Chem. 274:35845-35854(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Brain.
  4. "Direct interaction of the trans-Golgi network membrane protein, TGN38, with the F-actin binding protein, neurabin."
    Stephens D.J., Banting G.
    J. Biol. Chem. 274:30080-30086(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGN38.
  5. "Regulation of neurabin I interaction with protein phosphatase 1 by phosphorylation."
    McAvoy T., Allen P.B., Obaishi H., Nakanishi H., Takai Y., Greengard P., Nairn A.C., Hemmings H.C. Jr.
    Biochemistry 38:12943-12949(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PP1, PHOSPHORYLATION AT SER-461, MUTAGENESIS.
    Strain: Sprague-Dawley.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; THR-312; SER-372; SER-916; SER-929; SER-957; SER-958; SER-961 AND SER-975, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites."
    Ragusa M.J., Dancheck B., Critton D.A., Nairn A.C., Page R., Peti W.
    Nat. Struct. Mol. Biol. 17:459-464(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 426-592 IN COMPLEX WITH HUMAN PP1CA.

Entry informationi

Entry nameiNEB1_RAT
AccessioniPrimary (citable) accession number: O35867
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.