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Protein

Protein kinase C and casein kinase substrate in neurons protein 2

Gene

PACSIN2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. Recruits DNM2 to caveolae, and thereby plays a role in caveola-mediated endocytosis.5 Publications

GO - Molecular functioni

  1. cytoskeletal protein binding Source: GO_Central
  2. identical protein binding Source: IntAct
  3. phosphatidic acid binding Source: UniProtKB
  4. transporter activity Source: ProtInc

GO - Biological processi

  1. actin cytoskeleton organization Source: ProtInc
  2. caveola assembly Source: UniProtKB
  3. caveolin-mediated endocytosis Source: UniProtKB
  4. cell projection morphogenesis Source: UniProtKB
  5. membrane tubulation Source: UniProtKB
  6. negative regulation of endocytosis Source: Ensembl
  7. protein localization to endosome Source: UniProtKB
  8. 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 2
Alternative name(s):
Syndapin-2
Syndapin-II
Gene namesi
Name:PACSIN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:8571. PACSIN2.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome. Recycling endosome membrane. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection By similarity. Membranecaveola
Note: Detected at the neck of flask-shaped caveolae. Localization to tubular recycling endosomes probably requires interaction with MICALL1 and EHD1.

GO - Cellular componenti

  1. caveola Source: UniProtKB
  2. cell-cell junction Source: Ensembl
  3. cytoplasm Source: HPA
  4. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  5. cytoskeleton Source: UniProtKB-SubCell
  6. cytosol Source: Ensembl
  7. early endosome Source: UniProtKB-SubCell
  8. extracellular vesicular exosome Source: UniProtKB
  9. extrinsic component of membrane Source: UniProtKB
  10. focal adhesion Source: UniProtKB
  11. intracellular membrane-bounded organelle Source: HPA
  12. membrane-bounded vesicle Source: GO_Central
  13. nucleoplasm Source: HPA
  14. recycling endosome membrane Source: UniProtKB
  15. ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32897.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Protein kinase C and casein kinase substrate in neurons protein 2PRO_0000161795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UNF0.
PaxDbiQ9UNF0.
PRIDEiQ9UNF0.

PTM databases

PhosphoSiteiQ9UNF0.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiQ9UNF0.
ExpressionAtlasiQ9UNF0. baseline and differential.
GenevestigatoriQ9UNF0.

Organism-specific databases

HPAiCAB009929.
HPA028852.
HPA049854.

Interactioni

Subunit structurei

Homodimer. May form heterooligomers with other PACSINs. Interacts (via NPF motifs) with EHD1 (via EH domain). Interacts with EHD3. Interacts (via the SH3 domain) with MICALL1. Interacts with RAC1. Interacts (via SH3 domain) with DNM1, SYN1, SYNJ1 and WASL. Interacts with CAV1. Interacts with TRPV4.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-742503,EBI-742503
DNM2P505704EBI-742503,EBI-346547
FASLGP480234EBI-742503,EBI-495538

Protein-protein interaction databases

BioGridi116413. 39 interactions.
IntActiQ9UNF0. 8 interactions.
MINTiMINT-5005738.
STRINGi9606.ENSP00000263246.

Structurei

Secondary structure

1
486
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 – 17042Combined sources
Turni171 – 1744Combined sources
Beta strandi175 – 1784Combined sources
Helixi185 – 1884Combined sources
Helixi190 – 21627Combined sources
Helixi219 – 25537Combined sources
Helixi261 – 27515Combined sources
Helixi279 – 29012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ABHX-ray2.00A/B1-305[»]
3ACOX-ray2.70A/B1-343[»]
3HAJX-ray2.78A/B1-486[»]
3Q0KX-ray2.60A/B/C/D16-304[»]
ProteinModelPortaliQ9UNF0.
SMRiQ9UNF0. Positions 16-303, 429-484.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UNF0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 7565FCHPROSITE-ProRule annotationAdd
BLAST
Domaini426 – 48661SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 306306F-BAR domainAdd
BLAST

Coiled coil

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi362 – 3643NPF1
Motifi405 – 4073NPF2
Motifi417 – 4193NPF3

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.4 Publications

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG283356.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9UNF0.
OMAiHHAACKE.
PhylomeDBiQ9UNF0.
TreeFamiTF313677.

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.
PROSITEiPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UNF0-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCSD LMNCLHERAR
60 70 80 90 100
IEKAYAQQLT EWARRWRQLV EKGPQYGTVE KAWMAFMSEA ERVSELHLEV
110 120 130 140 150
KASLMNDDFE KIKNWQKEAF HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK
160 170 180 190 200
EVEAAKKAHH AACKEEKLAI SREANSKADP SLNPEQLKKL QDKIEKCKQD
210 220 230 240 250
VLKTKEKYEK SLKELDQGTP QYMENMEQVF EQCQQFEEKR LRFFREVLLE
260 270 280 290 300
VQKHLDLSNV AGYKAIYHDL EQSIRAADAV EDLRWFRANH GPGMAMNWPQ
310 320 330 340 350
FEEWSADLNR TLSRREKKKA TDGVTLTGIN QTGDQSLPSK PSSTLNVPSN
360 370 380 390 400
PAQSAQSQSS YNPFEDEDDT GSTVSEKDDT KAKNVSSYEK TQSYPTDWSD
410 420 430 440 450
DESNNPFSST DANGDSNPFD DDATSGTEVR VRALYDYEGQ EHDELSFKAG
460 470 480
DELTKMEDED EQGWCKGRLD NGQVGLYPAN YVEAIQ
Length:486
Mass (Da):55,739
Last modified:August 13, 2002 - v2
Checksum:i821DBEF65DAD1AA8
GO
Isoform 2 (identifier: Q9UNF0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     344-384: Missing.

Show »
Length:445
Mass (Da):51,353
Checksum:i1DA87A2D42B5D5F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821L → F in AAD41781. (PubMed:10431838)Curated
Sequence conflicti256 – 2561D → N in AAD41781. (PubMed:10431838)Curated
Sequence conflicti309 – 3091N → I in AAD41781. (PubMed:10431838)Curated
Sequence conflicti336 – 3361S → F in AAD41781. (PubMed:10431838)Curated
Sequence conflicti378 – 3803DDT → EDI in AAD41781. (PubMed:10431838)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti175 – 1751N → S.
Corresponds to variant rs35383004 [ dbSNP | Ensembl ].
VAR_053555
Natural varianti294 – 2941M → I.
Corresponds to variant rs2746984 [ dbSNP | Ensembl ].
VAR_013711
Natural varianti324 – 3241V → F.
Corresponds to variant rs1062913 [ dbSNP | Ensembl ].
VAR_013712

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei344 – 38441Missing in isoform 2. 2 PublicationsVSP_004517Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF128536 mRNA. Translation: AAD41781.1.
AL136845 mRNA. Translation: CAB66779.1.
CR456536 mRNA. Translation: CAG30422.1.
AL022476, AL049758 Genomic DNA. Translation: CAI20163.1.
AL049758, AL022476 Genomic DNA. Translation: CAI20948.1.
BC008037 mRNA. Translation: AAH08037.1.
AL389984 mRNA. Translation: CAB97538.1.
CCDSiCCDS43023.1. [Q9UNF0-1]
CCDS54536.1. [Q9UNF0-2]
RefSeqiNP_001171899.1. NM_001184970.1. [Q9UNF0-1]
NP_001171900.1. NM_001184971.1. [Q9UNF0-2]
NP_009160.2. NM_007229.3. [Q9UNF0-1]
XP_005261376.1. XM_005261319.2. [Q9UNF0-2]
XP_006724180.1. XM_006724117.1. [Q9UNF0-1]
XP_006724181.1. XM_006724118.1. [Q9UNF0-1]
XP_006724182.1. XM_006724119.1. [Q9UNF0-1]
UniGeneiHs.162877.

Genome annotation databases

EnsembliENST00000263246; ENSP00000263246; ENSG00000100266. [Q9UNF0-1]
ENST00000337959; ENSP00000338379; ENSG00000100266. [Q9UNF0-2]
ENST00000402229; ENSP00000385040; ENSG00000100266. [Q9UNF0-1]
ENST00000403744; ENSP00000385372; ENSG00000100266. [Q9UNF0-1]
ENST00000407585; ENSP00000385952; ENSG00000100266. [Q9UNF0-2]
GeneIDi11252.
KEGGihsa:11252.
UCSCiuc003bdg.4. human. [Q9UNF0-1]

Polymorphism databases

DMDMi22256968.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF128536 mRNA. Translation: AAD41781.1.
AL136845 mRNA. Translation: CAB66779.1.
CR456536 mRNA. Translation: CAG30422.1.
AL022476, AL049758 Genomic DNA. Translation: CAI20163.1.
AL049758, AL022476 Genomic DNA. Translation: CAI20948.1.
BC008037 mRNA. Translation: AAH08037.1.
AL389984 mRNA. Translation: CAB97538.1.
CCDSiCCDS43023.1. [Q9UNF0-1]
CCDS54536.1. [Q9UNF0-2]
RefSeqiNP_001171899.1. NM_001184970.1. [Q9UNF0-1]
NP_001171900.1. NM_001184971.1. [Q9UNF0-2]
NP_009160.2. NM_007229.3. [Q9UNF0-1]
XP_005261376.1. XM_005261319.2. [Q9UNF0-2]
XP_006724180.1. XM_006724117.1. [Q9UNF0-1]
XP_006724181.1. XM_006724118.1. [Q9UNF0-1]
XP_006724182.1. XM_006724119.1. [Q9UNF0-1]
UniGeneiHs.162877.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ABHX-ray2.00A/B1-305[»]
3ACOX-ray2.70A/B1-343[»]
3HAJX-ray2.78A/B1-486[»]
3Q0KX-ray2.60A/B/C/D16-304[»]
ProteinModelPortaliQ9UNF0.
SMRiQ9UNF0. Positions 16-303, 429-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116413. 39 interactions.
IntActiQ9UNF0. 8 interactions.
MINTiMINT-5005738.
STRINGi9606.ENSP00000263246.

PTM databases

PhosphoSiteiQ9UNF0.

Polymorphism databases

DMDMi22256968.

Proteomic databases

MaxQBiQ9UNF0.
PaxDbiQ9UNF0.
PRIDEiQ9UNF0.

Protocols and materials databases

DNASUi11252.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263246; ENSP00000263246; ENSG00000100266. [Q9UNF0-1]
ENST00000337959; ENSP00000338379; ENSG00000100266. [Q9UNF0-2]
ENST00000402229; ENSP00000385040; ENSG00000100266. [Q9UNF0-1]
ENST00000403744; ENSP00000385372; ENSG00000100266. [Q9UNF0-1]
ENST00000407585; ENSP00000385952; ENSG00000100266. [Q9UNF0-2]
GeneIDi11252.
KEGGihsa:11252.
UCSCiuc003bdg.4. human. [Q9UNF0-1]

Organism-specific databases

CTDi11252.
GeneCardsiGC22M043243.
HGNCiHGNC:8571. PACSIN2.
HPAiCAB009929.
HPA028852.
HPA049854.
MIMi604960. gene.
neXtProtiNX_Q9UNF0.
PharmGKBiPA32897.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG283356.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9UNF0.
OMAiHHAACKE.
PhylomeDBiQ9UNF0.
TreeFamiTF313677.

Miscellaneous databases

ChiTaRSiPACSIN2. human.
EvolutionaryTraceiQ9UNF0.
GeneWikiiPACSIN2.
GenomeRNAii11252.
NextBioi42818.
PROiQ9UNF0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UNF0.
ExpressionAtlasiQ9UNF0. baseline and differential.
GenevestigatoriQ9UNF0.

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.
PROSITEiPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter proteins."
    Ritter B., Modregger J., Paulsson M., Plomann M.
    FEBS Lett. 454:356-362(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain and Retina.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [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] (ISOFORM 1).
    Tissue: Skin.
  6. The European IMAGE consortium
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 335-486 (ISOFORM 2).
  7. "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: TISSUE SPECIFICITY.
  8. "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: TISSUE SPECIFICITY.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting."
    Senju Y., Itoh Y., Takano K., Hamada S., Suetsugu S.
    J. Cell Sci. 124:2032-2040(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, SUBCELLULAR LOCATION.
  13. "The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration."
    de Kreuk B.J., Nethe M., Fernandez-Borja M., Anthony E.C., Hensbergen P.J., Deelder A.M., Plomann M., Hordijk P.L.
    J. Cell Sci. 124:2375-2388(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAC1.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "The F-BAR protein PACSIN2 regulates epidermal growth factor receptor internalization."
    de Kreuk B.J., Anthony E.C., Geerts D., Hordijk P.L.
    J. Biol. Chem. 287:43438-43453(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  16. "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: FUNCTION, DOMAIN.
  17. "Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis."
    Giridharan S.S., Cai B., Vitale N., Naslavsky N., Caplan S.
    Mol. Biol. Cell 24:1776-1790(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEMBRANE TUBULATION, LIPID-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH EHD1; EHD3 AND MICALL1.
  18. "Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin."
    Wang Q., Navarro M.V., Peng G., Molinelli E., Goh S.L., Judson B.L., Rajashankar K.R., Sondermann H.
    Proc. Natl. Acad. Sci. U.S.A. 106:12700-12705(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS), DOMAIN.
  19. "Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II."
    Shimada A., Takano K., Shirouzu M., Hanawa-Suetsugu K., Terada T., Toyooka K., Umehara T., Yamamoto M., Yokoyama S., Suetsugu S.
    FEBS Lett. 584:1111-1118(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-305, DOMAIN.
  20. "Rigidity of wedge loop in PACSIN 3 protein is a key factor in dictating diameters of tubules."
    Bai X., Meng G., Luo M., Zheng X.
    J. Biol. Chem. 287:22387-22396(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 16-304.

Entry informationi

Entry nameiPACN2_HUMAN
AccessioniPrimary (citable) accession number: Q9UNF0
Secondary accession number(s): O95921
, Q96HV9, Q9H0D3, Q9NPN1, Q9Y4V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: August 13, 2002
Last modified: February 4, 2015
This is version 129 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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

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.