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Protein

Protein kinase C and casein kinase substrate in neurons protein 1

Gene

PACSIN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity3 Publications

GO - Molecular functioni

  • phospholipid binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciZFISH:HS04782-MONOMER.
ReactomeiR-HSA-8856828. Clathrin-mediated endocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C and casein kinase substrate in neurons protein 1
Alternative name(s):
Syndapin-1
Gene namesi
Name:PACSIN1
Synonyms:KIAA1379
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:8570. PACSIN1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi125I → E: Reduces membrane-binding. Abolishes membrane tubulation. 1 Publication1
Mutagenesisi126M → E: Reduces membrane-binding. Abolishes membrane tubulation. 1 Publication1

Organism-specific databases

DisGeNETi29993.
OpenTargetsiENSG00000124507.
PharmGKBiPA32896.

Polymorphism and mutation databases

DMDMi22256962.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001617921 – 444Protein kinase C and casein kinase substrate in neurons protein 1Add BLAST444

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2PhosphoserineBy similarity1
Modified residuei79PhosphoserineBy similarity1
Modified residuei184PhosphothreonineBy similarity1
Modified residuei346PhosphoserineBy similarity1
Modified residuei348PhosphoserineBy similarity1
Modified residuei349PhosphoserineBy similarity1
Modified residuei361PhosphoserineBy similarity1
Modified residuei365PhosphoserineBy similarity1
Modified residuei394PhosphotyrosineBy similarity1
Modified residuei405PhosphoserineBy similarity1
Modified residuei430PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BY11.
MaxQBiQ9BY11.
PaxDbiQ9BY11.
PeptideAtlasiQ9BY11.
PRIDEiQ9BY11.

PTM databases

iPTMnetiQ9BY11.
PhosphoSitePlusiQ9BY11.
SwissPalmiQ9BY11.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000124507.
CleanExiHS_PACSIN1.
ExpressionAtlasiQ9BY11. baseline and differential.
GenevisibleiQ9BY11. HS.

Organism-specific databases

HPAiCAB009929.
HPA028852.
HPA055491.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FASLGP480234EBI-721769,EBI-495538
HTTP428583EBI-721769,EBI-466029
PACSIN2Q9UNF07EBI-721769,EBI-742503
PACSIN3Q9UKS65EBI-721769,EBI-77926
POT1Q9NUX52EBI-721769,EBI-752420

Protein-protein interaction databases

BioGridi119018. 44 interactors.
IntActiQ9BY11. 21 interactors.
MINTiMINT-4538742.
STRINGi9606.ENSP00000244458.

Structurei

Secondary structure

1444
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni22 – 25Combined sources4
Helixi26 – 73Combined sources48
Helixi78 – 107Combined sources30
Helixi109 – 120Combined sources12
Beta strandi127 – 129Combined sources3
Helixi130 – 170Combined sources41
Turni176 – 179Combined sources4
Helixi193 – 256Combined sources64
Helixi258 – 260Combined sources3
Turni262 – 264Combined sources3
Helixi265 – 275Combined sources11
Helixi280 – 291Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9BY11.
SMRiQ9BY11.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BY11.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 283F-BARPROSITE-ProRule annotationAdd BLAST271
Domaini385 – 444SH3PROSITE-ProRule annotationAdd BLAST60

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili26 – 275Add BLAST250

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the PACSIN family.Curated
Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiKOG2856. Eukaryota.
ENOG410XRX2. LUCA.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9BY11.
KOiK20123.
OMAiQSNTPEQ.
OrthoDBiEOG091G0AS9.
PhylomeDBiQ9BY11.
TreeFamiTF313677.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028518. PACSIN1.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23065:SF16. PTHR23065:SF16. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BY11-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSYDEASL APEETTDSFW EVGNYKRTVK RIDDGHRLCN DLMNCVQERA
60 70 80 90 100
KIEKAYGQQL TDWAKRWRQL IEKGPQYGSL ERAWGAIMTE ADKVSELHQE
110 120 130 140 150
VKNNLLNEDL EKVKNWQKDA YHKQIMGGFK ETKEAEDGFR KAQKPWAKKM
160 170 180 190 200
KELEAAKKAY HLACKEEKLA MTREMNSKTE QSVTPEQQKK LQDKVDKCKQ
210 220 230 240 250
DVQKTQEKYE KVLEDVGKTT PQYMENMEQV FEQCQQFEEK RLVFLKEVLL
260 270 280 290 300
DIKRHLNLAE NSSYIHVYRE LEQAIRGADA QEDLRWFRST SGPGMPMNWP
310 320 330 340 350
QFEEWNPDLP HTTTKKEKQP KKAEGVALTN ATGAVESTSQ AGDRGSVSSY
360 370 380 390 400
DRGQPYATEW SDDESGNPFG GSETNGGANP FEDDSKGVRV RALYDYDGQE
410 420 430 440
QDELSFKAGD ELTKLGEEDE QGWCRGRLDS GQLGLYPANY VEAI
Length:444
Mass (Da):50,966
Last modified:June 1, 2001 - v1
Checksum:i6AAF801873770975
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_053554334A → V.Corresponds to variant rs41312309dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF242529 mRNA. Translation: AAK29206.1.
AB037800 mRNA. Translation: BAA92617.2. Different initiation.
AL834211 mRNA. Translation: CAD38895.1.
BC040228 mRNA. Translation: AAH40228.1.
CCDSiCCDS4793.1.
RefSeqiNP_001186512.1. NM_001199583.2.
NP_065855.1. NM_020804.4.
XP_011512843.1. XM_011514541.1.
UniGeneiHs.520087.

Genome annotation databases

EnsembliENST00000244458; ENSP00000244458; ENSG00000124507.
ENST00000538621; ENSP00000439639; ENSG00000124507.
ENST00000620693; ENSP00000484060; ENSG00000124507.
GeneIDi29993.
KEGGihsa:29993.
UCSCiuc003ojo.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF242529 mRNA. Translation: AAK29206.1.
AB037800 mRNA. Translation: BAA92617.2. Different initiation.
AL834211 mRNA. Translation: CAD38895.1.
BC040228 mRNA. Translation: AAH40228.1.
CCDSiCCDS4793.1.
RefSeqiNP_001186512.1. NM_001199583.2.
NP_065855.1. NM_020804.4.
XP_011512843.1. XM_011514541.1.
UniGeneiHs.520087.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9BY11.
SMRiQ9BY11.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119018. 44 interactors.
IntActiQ9BY11. 21 interactors.
MINTiMINT-4538742.
STRINGi9606.ENSP00000244458.

PTM databases

iPTMnetiQ9BY11.
PhosphoSitePlusiQ9BY11.
SwissPalmiQ9BY11.

Polymorphism and mutation databases

DMDMi22256962.

Proteomic databases

EPDiQ9BY11.
MaxQBiQ9BY11.
PaxDbiQ9BY11.
PeptideAtlasiQ9BY11.
PRIDEiQ9BY11.

Protocols and materials databases

DNASUi29993.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000244458; ENSP00000244458; ENSG00000124507.
ENST00000538621; ENSP00000439639; ENSG00000124507.
ENST00000620693; ENSP00000484060; ENSG00000124507.
GeneIDi29993.
KEGGihsa:29993.
UCSCiuc003ojo.5. human.

Organism-specific databases

CTDi29993.
DisGeNETi29993.
GeneCardsiPACSIN1.
HGNCiHGNC:8570. PACSIN1.
HPAiCAB009929.
HPA028852.
HPA055491.
MIMi606512. gene.
neXtProtiNX_Q9BY11.
OpenTargetsiENSG00000124507.
PharmGKBiPA32896.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2856. Eukaryota.
ENOG410XRX2. LUCA.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9BY11.
KOiK20123.
OMAiQSNTPEQ.
OrthoDBiEOG091G0AS9.
PhylomeDBiQ9BY11.
TreeFamiTF313677.

Enzyme and pathway databases

BioCyciZFISH:HS04782-MONOMER.
ReactomeiR-HSA-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

EvolutionaryTraceiQ9BY11.
GeneWikiiPACSIN1.
GenomeRNAii29993.
PROiQ9BY11.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000124507.
CleanExiHS_PACSIN1.
ExpressionAtlasiQ9BY11. baseline and differential.
GenevisibleiQ9BY11. HS.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028518. PACSIN1.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23065:SF16. PTHR23065:SF16. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPACN1_HUMAN
AccessioniPrimary (citable) accession number: Q9BY11
Secondary accession number(s): Q9P2G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.