Protein kinase C and casein kinase II substrate protein 3

Contribute

Send feedback

Read comments (?) or add your own

Q99JB8 (PACN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein kinase C and casein kinase II substrate protein 3

Gene names

Name:

Pacsin3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in endocytosis. Ref.1
Subunit structure	May form homo- and heterooligomers with other PACSINs. Interacts with DNM1, SYNJ1 and WASL through its SH3 domain. Ref.1
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Detected at the inner aspect of the plasma membrane in myotubes. Ref.1
Tissue specificity	Highly expressed in skeletal muscle, heart and lung; also detected in brain, kidney and uterus (at protein level). Ref.1
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.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Coiled coil SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of endocytosis Inferred from direct assay Ref.1. Source: MGI positive regulation of membrane protein ectodomain proteolysis Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cytoskeletal protein binding Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 424

424

Protein kinase C and casein kinase II substrate protein 3

PRO_0000161801

Regions

Domain

10 – 73

FCH

Domain

363 – 424

SH3

Coiled coil

174 – 217

Potential

Amino acid modifications

Modified residue

276

Phosphoserine Ref.4

Modified residue

319

Phosphoserine Ref.5 Ref.8

Modified residue

324

Phosphothreonine By similarity

Modified residue

327

Phosphoserine By similarity

Modified residue

354

Phosphoserine Ref.4 Ref.6 Ref.7 Ref.9

Modified residue

383

Phosphoserine By similarity

Experimental info

Mutagenesis

415

P → L: Loss of DNM1-, SYNJ1- and WASL-binding. Loss of effect on transferrin endocytosis. Ref.1

Sequence conflict

360

R → G in AAG31022. Ref.1

Secondary structure

424

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q99JB8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 00475BC0321485B7
Show »

FASTA

424

48,585

        10         20         30         40         50         60 
MAPEEDAGGE VLGGSFWEAG NYRRTVQRVE DGHRLCGDLV SCFQERARIE KAYAQQLADW 

        70         80         90        100        110        120 
ARKWRGAVEK GPQYGTLEKA WHAFFTAAER LSELHLEVRE KLHGPDSERV RTWQRGAFHR 

       130        140        150        160        170        180 
PVLGGFRESR AAEDGFRKAQ KPWLKRLKEV EASKKSYHTA RKDEKTAQTR ESHAKADSSM 

       190        200        210        220        230        240 
SQEQLRKLQE RVGRCTKEAE KMKTQYEQTL AELNRYTPRY MEDMEQAFES CQAAERQRLL 

       250        260        270        280        290        300 
FFKDVLLTLH QHLDLSSSDK FHELHRDLQQ SIEAASDEED LRWWRSTHGP GMAMNWPQFE 

       310        320        330        340        350        360 
EWSLDTQRAI SRKEKGGRSP DEVTLTSIVP TRDGTAPPPQ SPSSPGSGQD EDWSDEESPR 

       370        380        390        400        410        420 
KVATGVRVRA LYDYAGQEAD ELSFRAGEEL LKMSEEDEQG WCQGQLQSGR IGLYPANYVE 


CVGA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis." Modregger J., Ritter B., Witter B., Paulsson M., Plomann M. J. Cell Sci. 113:4511-4521(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DNM1; SYNJ1 AND WASL, HOMOOLIGOMERIZATION, HETEROOLIGOMERIZATION WITH PACSIN1 AND PACSIN2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-415. Strain: C57BL/6J.
[2]	"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].
[3]	"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: Neuron.
[4]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-354, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, MASS SPECTROMETRY. Tissue: Brain cortex.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, MASS SPECTROMETRY. Tissue: Melanoma.
[9]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF149824 mRNA. Translation: AAG31022.1.
AF242531 mRNA. Translation: AAK29208.1.
BC003884 mRNA. Translation: AAH03884.1.

IPI

IPI00319933.

RefSeq

NP_083009.1. NM_028733.3.
NP_112019.2. NM_030880.2.

UniGene

Mm.236650.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3M3W	X-ray	2.60	A/B	1-320	[»]
3QE6	X-ray	2.60	A/B	1-304	[»]
3SYV	X-ray	3.10	A/B/C/D/E/F/G/H	1-341	[»]

ProteinModelPortal

Q99JB8.

SMR

Q99JB8. Positions 12-302, 324-420.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99JB8. 2 interactions.

PTM databases

PhosphoSite

Q99JB8.

Proteomic databases

PaxDb

Q99JB8.

PRIDE

Q99JB8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000028694; ENSMUSP00000028694; ENSMUSG00000027257.
ENSMUST00000059566; ENSMUSP00000054391; ENSMUSG00000027257.
ENSMUST00000111349; ENSMUSP00000106981; ENSMUSG00000027257.
ENSMUST00000168916; ENSMUSP00000129175; ENSMUSG00000027257.

GeneID

80708.

KEGG

mmu:80708.

Organism-specific databases

CTD

29763.

MGI

MGI:1891410. Pacsin3.

Phylogenomic databases

eggNOG

NOG283356.

GeneTree

ENSGT00510000046376.

HOGENOM

HOG000007245.

HOVERGEN

HBG053486.

InParanoid

Q99JB8.

OMA

EQAFESC.

OrthoDB

EOG44QT13.

Gene expression databases

ArrayExpress

Q99JB8.

Bgee

Q99JB8.

Genevestigator

Q99JB8.

GermOnline

ENSMUSG00000027257. Mus musculus.

Family and domain databases

InterPro

IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

350063.

SOURCE

Search...

Entry information

Entry name

PACN3_MOUSE

Accession

Primary (citable) accession number: Q99JB8
Secondary accession number(s): Q9EQP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 2002
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents