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Q9UNF0

- PACN2_HUMAN

UniProt

Q9UNF0 - PACN2_HUMAN

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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: 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. identical protein binding Source: IntAct
  2. phosphatidic acid binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. transporter activity Source: ProtInc
Complete GO annotation...

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
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 EHD1.4 Publications

GO - Cellular componenti

  1. caveola Source: UniProtKB
  2. cytoplasm Source: HPA
  3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  4. cytoskeleton Source: UniProtKB-SubCell
  5. cytosol Source: Ensembl
  6. early endosome Source: UniProtKB-SubCell
  7. extracellular vesicular exosome Source: UniProt
  8. extrinsic component of membrane Source: UniProtKB
  9. intracellular membrane-bounded organelle Source: HPA
  10. nucleus Source: HPA
  11. recycling endosome membrane Source: UniProtKB
  12. 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 2
PRO_0000161795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysine By 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

ArrayExpressiQ9UNF0.
BgeeiQ9UNF0.
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. 33 interactions.
IntActiQ9UNF0. 8 interactions.
MINTiMINT-5005738.
STRINGi9606.ENSP00000263246.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni21 – 244
Helixi25 – 7248
Helixi77 – 10630
Helixi108 – 11912
Beta strandi126 – 1283
Helixi129 – 16941
Helixi172 – 1776
Helixi185 – 1884
Helixi189 – 1913
Turni192 – 1954
Helixi197 – 25559
Helixi257 – 2593
Helixi263 – 27513
Helixi279 – 29012

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ9UNF0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 7565FCH
Add
BLAST
Domaini426 – 48661SH3
Add
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili25 – 274250
Add
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.
Contains 1 FCH domain.
Contains 1 SH3 domain.

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG283356.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9UNF0.
OMAiCKQDVLK.
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

MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCSD LMNCLHERAR    50
IEKAYAQQLT EWARRWRQLV EKGPQYGTVE KAWMAFMSEA ERVSELHLEV 100
KASLMNDDFE KIKNWQKEAF HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK 150
EVEAAKKAHH AACKEEKLAI SREANSKADP SLNPEQLKKL QDKIEKCKQD 200
VLKTKEKYEK SLKELDQGTP QYMENMEQVF EQCQQFEEKR LRFFREVLLE 250
VQKHLDLSNV AGYKAIYHDL EQSIRAADAV EDLRWFRANH GPGMAMNWPQ 300
FEEWSADLNR TLSRREKKKA TDGVTLTGIN QTGDQSLPSK PSSTLNVPSN 350
PAQSAQSQSS YNPFEDEDDT GSTVSEKDDT KAKNVSSYEK TQSYPTDWSD 400
DESNNPFSST DANGDSNPFD DDATSGTEVR VRALYDYEGQ EHDELSFKAG 450
DELTKMEDED EQGWCKGRLD NGQVGLYPAN YVEAIQ 486
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

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.
VSP_004517Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821L → F in AAD41781. 1 Publication
Sequence conflicti256 – 2561D → N in AAD41781. 1 Publication
Sequence conflicti309 – 3091N → I in AAD41781. 1 Publication
Sequence conflicti336 – 3361S → F in AAD41781. 1 Publication
Sequence conflicti378 – 3803DDT → EDI in AAD41781. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS43023.1. [Q9UNF0-1 ]
CCDS54536.1. [Q9UNF0-2 ]
RefSeqi NP_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 ]
UniGenei Hs.162877.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ABH X-ray 2.00 A/B 1-305 [» ]
3ACO X-ray 2.70 A/B 1-343 [» ]
3HAJ X-ray 2.78 A/B 1-486 [» ]
3Q0K X-ray 2.60 A/B/C/D 16-304 [» ]
ProteinModelPortali Q9UNF0.
SMRi Q9UNF0. Positions 16-303, 429-484.
ModBasei Search...

Protein-protein interaction databases

BioGridi 116413. 33 interactions.
IntActi Q9UNF0. 8 interactions.
MINTi MINT-5005738.
STRINGi 9606.ENSP00000263246.

PTM databases

PhosphoSitei Q9UNF0.

Polymorphism databases

DMDMi 22256968.

Proteomic databases

MaxQBi Q9UNF0.
PaxDbi Q9UNF0.
PRIDEi Q9UNF0.

Protocols and materials databases

DNASUi 11252.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263246 ; ENSP00000263246 ; ENSG00000100266 . [Q9UNF0-1 ]
ENST00000337959 ; ENSP00000338379 ; ENSG00000100266 . [Q9UNF0-2 ]
ENST00000402229 ; ENSP00000385040 ; ENSG00000100266 . [Q9UNF0-1 ]
ENST00000403744 ; ENSP00000385372 ; ENSG00000100266 . [Q9UNF0-1 ]
ENST00000407585 ; ENSP00000385952 ; ENSG00000100266 . [Q9UNF0-2 ]
GeneIDi 11252.
KEGGi hsa:11252.
UCSCi uc003bdg.4. human. [Q9UNF0-1 ]

Organism-specific databases

CTDi 11252.
GeneCardsi GC22M043243.
HGNCi HGNC:8571. PACSIN2.
HPAi CAB009929.
HPA028852.
HPA049854.
MIMi 604960. gene.
neXtProti NX_Q9UNF0.
PharmGKBi PA32897.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG283356.
HOGENOMi HOG000007245.
HOVERGENi HBG053486.
InParanoidi Q9UNF0.
OMAi CKQDVLK.
PhylomeDBi Q9UNF0.
TreeFami TF313677.

Miscellaneous databases

ChiTaRSi PACSIN2. human.
EvolutionaryTracei Q9UNF0.
GeneWikii PACSIN2.
GenomeRNAii 11252.
NextBioi 42818.
PROi Q9UNF0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UNF0.
Bgeei Q9UNF0.
Genevestigatori Q9UNF0.

Family and domain databases

InterProi IPR001060. FCH_dom.
IPR028521. PACSIN2.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR10959:SF2. PTHR10959:SF2. 1 hit.
Pfami PF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
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

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

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