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Protein

Protein kinase C and casein kinase substrate in neurons protein 2

Gene

PACSIN2

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. May also play a role in the formation of caveolae at the cell membrane and thereby may play a role in caveola-mediated endocytosis (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C and casein kinase substrate in neurons protein 2
Alternative name(s):
Focal adhesion protein of 52 kDa
Short name:
FAP52
Gene namesi
Name:PACSIN2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Protein kinase C and casein kinase substrate in neurons protein 2PRO_0000161798Add
BLAST

Post-translational modificationi

Phosphorylated on serine residues.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO13154.
PRIDEiO13154.

Expressioni

Tissue specificityi

Detected in intestine, cardiac muscle, lung and brain (at protein level). Expressed in all tissues tested, including, gizzard, liver, cardiac muscle, skeletal muscle and skin.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000022861.

Structurei

Secondary structure

1
448
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni21 – 244Combined sources
Helixi25 – 7248Combined sources
Helixi77 – 10630Combined sources
Helixi108 – 11912Combined sources
Beta strandi126 – 1283Combined sources
Helixi129 – 17446Combined sources
Turni175 – 1784Combined sources
Helixi184 – 25572Combined sources
Turni257 – 2593Combined sources
Helixi261 – 27515Combined sources
Helixi279 – 29012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BNEX-ray2.57A/B1-448[»]
ProteinModelPortaliO13154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 282272F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini388 – 44861SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili25 – 274250By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi367 – 3693NPF1
Motifi379 – 3813NPF2

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 (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

eggNOGiNOG283356.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiO13154.
PhylomeDBiO13154.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR028521. PACSIN2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10959:SF2. PTHR10959:SF2. 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.

O13154-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCND LMNCIHERAR
60 70 80 90 100
IEKVYAQQLT EWAKRWKQLV EKGPQYGTVE RAWCAFMSEA EKVSELHLEV
110 120 130 140 150
KGSLMNEDFE KIKNWQKEAF HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK
160 170 180 190 200
EVEAAKKAYH AACKEEKLAI SRETNSKADP ALNPEQLKKL QDKVERSKQD
210 220 230 240 250
VLKTKAKYEK SLKELDNATP QYMENMEQVF EQCQQFEEKR LRFFREVLLE
260 270 280 290 300
VQKHLDLSNV ASYKNIYREL EQNIKTADAV EDLRWFRANQ GPGMSMNWPQ
310 320 330 340 350
FEDDEWSADL NRTLSRREKK KASDGVTLTG INQTGDQVSQ PNKHSSVSSY
360 370 380 390 400
EKNQSYPTDW SDEESNNPFS STDAKGDTNP FDEDTSPVME VRVRALYDYE
410 420 430 440
GQEQDELSFK AGDELTKMEN EDEQGWCKGR LDNGQVGLYP ANYVEPIQ
Length:448
Mass (Da):51,971
Last modified:July 1, 1997 - v1
Checksum:i344218153F8698EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50798 mRNA. Translation: CAA90678.1.
RefSeqiNP_001152983.1. NM_001159511.1.
NP_990420.1. NM_205089.1.
UniGeneiGga.3831.

Genome annotation databases

GeneIDi395975.
KEGGigga:395975.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50798 mRNA. Translation: CAA90678.1.
RefSeqiNP_001152983.1. NM_001159511.1.
NP_990420.1. NM_205089.1.
UniGeneiGga.3831.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BNEX-ray2.57A/B1-448[»]
ProteinModelPortaliO13154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000022861.

Proteomic databases

PaxDbiO13154.
PRIDEiO13154.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi395975.
KEGGigga:395975.

Organism-specific databases

CTDi11252.

Phylogenomic databases

eggNOGiNOG283356.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiO13154.
PhylomeDBiO13154.

Miscellaneous databases

NextBioi20816040.
PROiO13154.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR028521. PACSIN2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10959:SF2. PTHR10959:SF2. 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...

Publicationsi

  1. "FAP52, a novel, SH3 domain-containing focal adhesion protein."
    Merilaeinen J., Lehto V.-P., Wasenius V.-M.
    J. Biol. Chem. 272:23278-23284(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Brain.

Entry informationi

Entry nameiPACN2_CHICK
AccessioniPrimary (citable) accession number: O13154
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: July 1, 1997
Last modified: March 4, 2015
This is version 97 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, Reference proteome

Documents

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

External Data

Dasty 3

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 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.