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Q9BY11 (PACN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C and casein kinase substrate in neurons protein 1
Alternative name(s):
Syndapin-1
Gene names
Name:PACSIN1
Synonyms:KIAA1379
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission By similarity. Binds to membranes via its F-BAR domain and mediates membrane tubulation. Ref.6 Ref.7 Ref.8

Subunit structure

May form heterooligomers with other PACSINs. Interacts with MAPT. Interacts with TRPV4 By similarity. Interacts (via SH3 domain) with SYNJ1 and WASL. Interacts with DNM2 and DNM3. Interacts with both COBL and DBNL. Identified in a complex composed of COBL, PACSIN1 and WASL. Interacts with EHD1 and EHD3 By similarity. Homodimer. Interacts (via SH3 domain) with DNM1; the interaction is reduced by DNM1 phosphorylation. Ref.6 Ref.7

Subcellular location

Cytoplasm By similarity. Cell projection By similarity. Cell junctionsynapsesynaptosome By similarity. Cell projectionruffle membrane By similarity. Membrane; Peripheral membrane protein. Cytoplasmic vesicle membrane; Peripheral membrane protein By similarity. Cell junctionsynapse By similarity. Cytoplasmcytosol By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Colocalizes with MAPT in axons. In primary neuronal cultures, present at a high level in presynaptic nerve terminals and in the cell body. Colocalizes with DNM1 at vesicular structures in the cell body and neurites By similarity. Associates with membranes via its F-BAR domain. Ref.6 Ref.7

Tissue specificity

Highly expressed in brain and, at much lower levels, in heart and pancreas. Ref.1

Domain

The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain. DNM1 binding abolishes autoinhibition By similarity. Ref.6 Ref.7 Ref.8

Post-translational modification

Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC) Probable.

Sequence similarities

Belongs to the PACSIN family.

Contains 1 FCH domain.

Contains 1 SH3 domain.

Sequence caution

The sequence BAA92617.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Membrane
Synapse
Synaptosome
   Coding sequence diversityPolymorphism
   DomainCoiled coil
SH3 domain
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processestablishment of protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

membrane tubulation

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of endocytosis

Inferred from electronic annotation. Source: Ensembl

neuron projection morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of dendrite development

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentCOPI-coated vesicle

Inferred from electronic annotation. Source: Ensembl

axon terminus

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay. Source: LIFEdb

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

ruffle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

synapse

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionphospholipid binding

Inferred from direct assay Ref.7. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16318909PubMed 17161366PubMed 17500595. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Protein kinase C and casein kinase substrate in neurons protein 1
PRO_0000161792

Regions

Domain13 – 7664FCH
Domain385 – 44460SH3
Region1 – 307307F-BAR domain
Coiled coil26 – 275250

Amino acid modifications

Modified residue791Phosphoserine By similarity
Modified residue1841Phosphothreonine By similarity
Modified residue3941Phosphotyrosine By similarity

Natural variations

Natural variant3341A → V.
Corresponds to variant rs41312309 [ dbSNP | Ensembl ].
VAR_053554

Experimental info

Mutagenesis1251I → E: Reduces membrane-binding. Abolishes membrane tubulation. Ref.7
Mutagenesis1261M → E: Reduces membrane-binding. Abolishes membrane tubulation. Ref.7

Secondary structure

...................... 444
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BY11 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 6AAF801873770975

FASTA44450,966
        10         20         30         40         50         60 
MSSSYDEASL APEETTDSFW EVGNYKRTVK RIDDGHRLCN DLMNCVQERA KIEKAYGQQL 

        70         80         90        100        110        120 
TDWAKRWRQL IEKGPQYGSL ERAWGAIMTE ADKVSELHQE VKNNLLNEDL EKVKNWQKDA 

       130        140        150        160        170        180 
YHKQIMGGFK ETKEAEDGFR KAQKPWAKKM KELEAAKKAY HLACKEEKLA MTREMNSKTE 

       190        200        210        220        230        240 
QSVTPEQQKK LQDKVDKCKQ DVQKTQEKYE KVLEDVGKTT PQYMENMEQV FEQCQQFEEK 

       250        260        270        280        290        300 
RLVFLKEVLL DIKRHLNLAE NSSYIHVYRE LEQAIRGADA QEDLRWFRST SGPGMPMNWP 

       310        320        330        340        350        360 
QFEEWNPDLP HTTTKKEKQP KKAEGVALTN ATGAVESTSQ AGDRGSVSSY DRGQPYATEW 

       370        380        390        400        410        420 
SDDESGNPFG GSETNGGANP FEDDSKGVRV RALYDYDGQE QDELSFKAGD ELTKLGEEDE 

       430        440 
QGWCRGRLDS GQLGLYPANY VEAI 

« Hide

References

« Hide 'large scale' references
[1]"PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family."
Sumoy L., Pluvinet R., Andreu N., Estivill X., Escarceller M.
Gene 262:199-205(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Versatile membrane deformation potential of activated pacsin."
Goh S.L., Wang Q., Byrnes L.J., Sondermann H.
PLoS ONE 7:E51628-E51628(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DNM1, SUBCELLULAR LOCATION, DOMAIN.
[7]"Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin."
Wang Q., Navarro M.V., Peng G., Molinelli E., Goh S.L., Judson B.L., Rajashankar K.R., Sondermann H.
Proc. Natl. Acad. Sci. U.S.A. 106:12700-12705(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 1-325, FUNCTION, LIPID-BINDING, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-125 AND MET-126, DOMAIN.
[8]"Rigidity of wedge loop in PACSIN 3 protein is a key factor in dictating diameters of tubules."
Bai X., Meng G., Luo M., Zheng X.
J. Biol. Chem. 287:22387-22396(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 14-308, FUNCTION, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF242529 mRNA. Translation: AAK29206.1.
AB037800 mRNA. Translation: BAA92617.2. Different initiation.
AL834211 mRNA. Translation: CAD38895.1.
BC040228 mRNA. Translation: AAH40228.1.
CCDSCCDS4793.1.
RefSeqNP_001186512.1. NM_001199583.2.
NP_065855.1. NM_020804.4.
UniGeneHs.520087.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HAHX-ray2.77A/B1-325[»]
3HAIX-ray2.88A/B/C/D1-308[»]
3Q84X-ray2.80A/B/G/H/M/N14-308[»]
3QNIX-ray2.80A/B1-307[»]
ProteinModelPortalQ9BY11.
SMRQ9BY11. Positions 15-308, 388-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119018. 34 interactions.
IntActQ9BY11. 18 interactions.
MINTMINT-4538742.
STRING9606.ENSP00000244458.

PTM databases

PhosphoSiteQ9BY11.

Polymorphism databases

DMDM22256962.

Proteomic databases

MaxQBQ9BY11.
PaxDbQ9BY11.
PRIDEQ9BY11.

Protocols and materials databases

DNASU29993.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244458; ENSP00000244458; ENSG00000124507.
ENST00000538621; ENSP00000439639; ENSG00000124507.
GeneID29993.
KEGGhsa:29993.
UCSCuc003ojo.4. human.

Organism-specific databases

CTD29993.
GeneCardsGC06P036299.
HGNCHGNC:8570. PACSIN1.
HPACAB009929.
HPA028852.
HPA055491.
MIM606512. gene.
neXtProtNX_Q9BY11.
PharmGKBPA32896.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283356.
HOGENOMHOG000007245.
HOVERGENHBG053486.
InParanoidQ9BY11.
OMAAMTREAN.
OrthoDBEOG75TMBJ.
PhylomeDBQ9BY11.
TreeFamTF313677.

Gene expression databases

ArrayExpressQ9BY11.
BgeeQ9BY11.
CleanExHS_PACSIN1.
GenevestigatorQ9BY11.

Family and domain databases

InterProIPR001060. FCH_dom.
IPR028518. PACSIN1.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10959:SF7. PTHR10959:SF7. 1 hit.
PfamPF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BY11.
GeneWikiPACSIN1.
GenomeRNAi29993.
NextBio52788.
PROQ9BY11.
SOURCESearch...

Entry information

Entry namePACN1_HUMAN
AccessionPrimary (citable) accession number: Q9BY11
Secondary accession number(s): Q9P2G8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM