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Protein

Protein kinase C and casein kinase substrate in neurons protein 3

Gene

PACSIN3

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

Functioni

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).By similarity

GO - Molecular functioni

  1. calcium channel inhibitor activity Source: UniProtKB
  2. cytoskeletal protein binding Source: UniProtKB
  3. lipid binding Source: UniProtKB
  4. phospholipid binding Source: GO_Central

GO - Biological processi

  1. cytoskeleton organization Source: GO_Central
  2. endocytosis Source: UniProtKB-KW
  3. membrane tubulation Source: UniProtKB
  4. negative regulation of calcium ion transport Source: UniProtKB
  5. negative regulation of endocytosis Source: UniProtKB
  6. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  7. regulation of endocytosis Source: GO_Central
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 3
Alternative name(s):
SH3 domain-containing protein 6511
Gene namesi
Name:PACSIN3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8572. PACSIN3.

Subcellular locationi

Cytoplasm 1 Publication. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Note: Detected at the inner aspect of the plasma membrane in myotubes.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endosome Source: GO_Central
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: GO_Central
  5. membrane-bounded vesicle Source: GO_Central
  6. nucleoplasm Source: HPA
  7. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32898.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Protein kinase C and casein kinase substrate in neurons protein 3PRO_0000161800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei276 – 2761Phosphoserine2 Publications
Modified residuei319 – 3191Phosphoserine5 Publications
Modified residuei324 – 3241Phosphothreonine1 Publication
Modified residuei327 – 3271Phosphoserine1 Publication
Modified residuei354 – 3541Phosphoserine4 Publications
Modified residuei383 – 3831Phosphoserine3 Publications

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UKS6.
PaxDbiQ9UKS6.
PRIDEiQ9UKS6.

PTM databases

PhosphoSiteiQ9UKS6.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ9UKS6.
CleanExiHS_PACSIN3.
ExpressionAtlasiQ9UKS6. baseline and differential.
GenevestigatoriQ9UKS6.

Organism-specific databases

HPAiHPA039480.
HPA043904.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAM15Q134443EBI-77926,EBI-77818
ADAM9Q134432EBI-77926,EBI-77903
FASLGP480234EBI-77926,EBI-495538
SOS1Q078892EBI-77926,EBI-297487
SOS2Q078902EBI-77926,EBI-298181

Protein-protein interaction databases

BioGridi118896. 36 interactions.
IntActiQ9UKS6. 6 interactions.
MINTiMINT-5002056.
STRINGi9606.ENSP00000298838.

Structurei

3D structure databases

ProteinModelPortaliQ9UKS6.
SMRiQ9UKS6. Positions 12-302, 324-420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 280271F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini363 – 42462SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili23 – 272250By similarityAdd
BLAST

Domaini

The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation.1 Publication

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.
GeneTreeiENSGT00510000046376.
HOVERGENiHBG053486.
InParanoidiQ9UKS6.
OMAiAFESCQA.
OrthoDBiEOG75TMBJ.
PhylomeDBiQ9UKS6.
TreeFamiTF313677.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR028523. PACSIN3.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10959:SF1. PTHR10959:SF1. 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.

Q9UKS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPEEDAGGE ALGGSFWEAG NYRRTVQRVE DGHRLCGDLV SCFQERARIE
60 70 80 90 100
KAYAQQLADW ARKWRGTVEK GPQYGTLEKA WHAFFTAAER LSALHLEVRE
110 120 130 140 150
KLQGQDSERV RAWQRGAFHR PVLGGFRESR AAEDGFRKAQ KPWLKRLKEV
160 170 180 190 200
EASKKSYHAA RKDEKTAQTR ESHAKADSAV SQEQLRKLQE RVERCAKEAE
210 220 230 240 250
KTKAQYEQTL AELHRYTPRY MEDMEQAFET CQAAERQRLL FFKDMLLTLH
260 270 280 290 300
QHLDLSSSEK FHELHRDLHQ GIEAASDEED LRWWRSTHGP GMAMNWPQFE
310 320 330 340 350
EWSLDTQRTI SRKEKGGRSP DEVTLTSIVP TRDGTAPPPQ SPGSPGTGQD
360 370 380 390 400
EEWSDEESPR KAATGVRVRA LYDYAGQEAD ELSFRAGEEL LKMSEEDEQG
410 420
WCQGQLQSGR IGLYPANYVE CVGA
Length:424
Mass (Da):48,487
Last modified:August 13, 2002 - v2
Checksum:i6DBD940AE6D1F352
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611A → V.1 Publication
Corresponds to variant rs7106654 [ dbSNP | Ensembl ].
VAR_053556

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31481.1.
RefSeqiNP_001171903.1. NM_001184974.1.
NP_001171904.1. NM_001184975.1.
NP_057307.2. NM_016223.4.
UniGeneiHs.334639.

Genome annotation databases

EnsembliENST00000298838; ENSP00000298838; ENSG00000165912.
ENST00000539589; ENSP00000440945; ENSG00000165912.
GeneIDi29763.
KEGGihsa:29763.
UCSCiuc001ndw.3. human.

Polymorphism databases

DMDMi22256967.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31481.1.
RefSeqiNP_001171903.1. NM_001184974.1.
NP_001171904.1. NM_001184975.1.
NP_057307.2. NM_016223.4.
UniGeneiHs.334639.

3D structure databases

ProteinModelPortaliQ9UKS6.
SMRiQ9UKS6. Positions 12-302, 324-420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118896. 36 interactions.
IntActiQ9UKS6. 6 interactions.
MINTiMINT-5002056.
STRINGi9606.ENSP00000298838.

PTM databases

PhosphoSiteiQ9UKS6.

Polymorphism databases

DMDMi22256967.

Proteomic databases

MaxQBiQ9UKS6.
PaxDbiQ9UKS6.
PRIDEiQ9UKS6.

Protocols and materials databases

DNASUi29763.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298838; ENSP00000298838; ENSG00000165912.
ENST00000539589; ENSP00000440945; ENSG00000165912.
GeneIDi29763.
KEGGihsa:29763.
UCSCiuc001ndw.3. human.

Organism-specific databases

CTDi29763.
GeneCardsiGC11M047199.
HGNCiHGNC:8572. PACSIN3.
HPAiHPA039480.
HPA043904.
MIMi606513. gene.
neXtProtiNX_Q9UKS6.
PharmGKBiPA32898.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG283356.
GeneTreeiENSGT00510000046376.
HOVERGENiHBG053486.
InParanoidiQ9UKS6.
OMAiAFESCQA.
OrthoDBiEOG75TMBJ.
PhylomeDBiQ9UKS6.
TreeFamiTF313677.

Miscellaneous databases

GeneWikiiPACSIN3.
GenomeRNAii29763.
NextBioi52258.
PROiQ9UKS6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UKS6.
CleanExiHS_PACSIN3.
ExpressionAtlasiQ9UKS6. baseline and differential.
GenevestigatoriQ9UKS6.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR028523. PACSIN3.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10959:SF1. PTHR10959:SF1. 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

« Hide 'large scale' publications
  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(1998) [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(1999) [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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. 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(2003) [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.
    , 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(2003) [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(2005) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. 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(2008) [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(2009) [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. 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(2010) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-319 AND SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPACN3_HUMAN
AccessioniPrimary (citable) accession number: Q9UKS6
Secondary accession number(s): A6NH84, Q9H331, Q9NWV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: August 13, 2002
Last modified: March 4, 2015
This is version 125 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. 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.