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Q9UKS6 (PACN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 3
Alternative name(s):
SH3 domain-containing protein 6511
Gene names
Name:PACSIN3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity By similarity. Ref.2

Subunit structure

Homodimer. May form heterooligomers with other PACSINs. Interacts (via SH3 domain) with DNM1, SYNJ1 and WASL. Interacts with TRPV4 By similarity.

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Detected at the inner aspect of the plasma membrane in myotubes By similarity. Ref.3

Tissue specificity

Widely expressed, with highest levels in heart and skeletal muscle, intermediate levels in placenta, liver and pancreas, and very low levels in brain, lung and kidney. Ref.2 Ref.3

Domain

The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. Ref.14

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Protein kinase C and casein kinase substrate in neurons protein 3
PRO_0000161800

Regions

Domain10 – 7364FCH
Domain363 – 42462SH3
Region1 – 304304F-BAR domain By similarity
Coiled coil23 – 272250 By similarity

Amino acid modifications

Modified residue2761Phosphoserine Ref.11
Modified residue3191Phosphoserine Ref.7 Ref.8 Ref.9 Ref.11
Modified residue3241Phosphothreonine Ref.9
Modified residue3271Phosphoserine Ref.9
Modified residue3541Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue3831Phosphoserine Ref.9 Ref.10 Ref.11

Natural variations

Natural variant611A → V. Ref.1
Corresponds to variant rs7106654 [ dbSNP | Ensembl ].
VAR_053556

Sequences

Sequence LengthMass (Da)Tools
Q9UKS6 [UniParc].

Last modified August 13, 2002. Version 2.
Checksum: 6DBD940AE6D1F352

FASTA42448,487
        10         20         30         40         50         60 
MAPEEDAGGE ALGGSFWEAG NYRRTVQRVE DGHRLCGDLV SCFQERARIE KAYAQQLADW 

        70         80         90        100        110        120 
ARKWRGTVEK GPQYGTLEKA WHAFFTAAER LSALHLEVRE KLQGQDSERV RAWQRGAFHR 

       130        140        150        160        170        180 
PVLGGFRESR AAEDGFRKAQ KPWLKRLKEV EASKKSYHAA RKDEKTAQTR ESHAKADSAV 

       190        200        210        220        230        240 
SQEQLRKLQE RVERCAKEAE KTKAQYEQTL AELHRYTPRY MEDMEQAFET CQAAERQRLL 

       250        260        270        280        290        300 
FFKDMLLTLH QHLDLSSSEK FHELHRDLHQ GIEAASDEED LRWWRSTHGP GMAMNWPQFE 

       310        320        330        340        350        360 
EWSLDTQRTI SRKEKGGRSP DEVTLTSIVP TRDGTAPPPQ SPGSPGTGQD EEWSDEESPR 

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


CVGA 

« Hide

References

« Hide 'large scale' references
[1]"Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1."
Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.
J. Biol. Chem. 274:31693-31699(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-61.
Tissue: Mammary carcinoma.
[2]"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, TISSUE SPECIFICITY.
[3]"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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Skin and Uterus.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-405.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; THR-324; SER-327; SER-354 AND SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-319; SER-354 AND SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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: DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF130979 mRNA. Translation: AAF04472.1.
AF149825 mRNA. Translation: AAG31023.1.
AF242530 mRNA. Translation: AAK29207.1.
AC090589 Genomic DNA. No translation available.
BC007914 mRNA. Translation: AAH07914.1.
BC011889 mRNA. Translation: AAH11889.1.
AK000577 mRNA. Translation: BAA91267.1.
CCDSCCDS31481.1.
RefSeqNP_001171903.1. NM_001184974.1.
NP_001171904.1. NM_001184975.1.
NP_057307.2. NM_016223.4.
UniGeneHs.334639.

3D structure databases

ProteinModelPortalQ9UKS6.
SMRQ9UKS6. Positions 12-302, 324-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118896. 30 interactions.
IntActQ9UKS6. 6 interactions.
MINTMINT-5002056.
STRING9606.ENSP00000298838.

PTM databases

PhosphoSiteQ9UKS6.

Polymorphism databases

DMDM22256967.

Proteomic databases

MaxQBQ9UKS6.
PaxDbQ9UKS6.
PRIDEQ9UKS6.

Protocols and materials databases

DNASU29763.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298838; ENSP00000298838; ENSG00000165912.
ENST00000528462; ENSP00000437252; ENSG00000165912.
ENST00000539589; ENSP00000440945; ENSG00000165912.
GeneID29763.
KEGGhsa:29763.
UCSCuc001ndw.3. human.

Organism-specific databases

CTD29763.
GeneCardsGC11M047199.
HGNCHGNC:8572. PACSIN3.
HPAHPA039480.
HPA043904.
MIM606513. gene.
neXtProtNX_Q9UKS6.
PharmGKBPA32898.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283356.
HOVERGENHBG053486.
InParanoidQ9UKS6.
OMAEQAFESC.
OrthoDBEOG75TMBJ.
PhylomeDBQ9UKS6.
TreeFamTF313677.

Gene expression databases

ArrayExpressQ9UKS6.
BgeeQ9UKS6.
CleanExHS_PACSIN3.
GenevestigatorQ9UKS6.

Family and domain databases

InterProIPR001060. FCH_dom.
IPR028523. PACSIN3.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10959:SF1. PTHR10959:SF1. 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

GeneWikiPACSIN3.
GenomeRNAi29763.
NextBio52258.
PROQ9UKS6.
SOURCESearch...

Entry information

Entry namePACN3_HUMAN
AccessionPrimary (citable) accession number: Q9UKS6
Secondary accession number(s): A6NH84, Q9H331, Q9NWV9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: August 13, 2002
Last modified: July 9, 2014
This is version 120 of the entry and version 2 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

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 11

Human chromosome 11: entries, gene names and cross-references to MIM