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Q9UNF0 (PACN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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 2
Alternative name(s):
Syndapin-2
Syndapin-II
Gene names
Name:PACSIN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.13 Ref.15 Ref.16 Ref.17

Subunit structure

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. Ref.13 Ref.17

Subcellular location

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. Ref.12 Ref.13 Ref.15 Ref.17

Tissue specificity

Widely expressed. Ref.7 Ref.8

Domain

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. Ref.12 Ref.16 Ref.18 Ref.19

Post-translational modification

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

Sequence similarities

Belongs to the PACSIN family.

Contains 1 FCH domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Endosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
SH3 domain
   LigandLipid-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Traceable author statement Ref.1. Source: ProtInc

caveola assembly

Inferred from mutant phenotype Ref.12. Source: UniProtKB

caveolin-mediated endocytosis

Inferred from mutant phenotype Ref.12. Source: UniProtKB

cell projection morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

membrane tubulation

Inferred from direct assay Ref.17. Source: UniProtKB

negative regulation of endocytosis

Inferred from electronic annotation. Source: Ensembl

protein localization to endosome

Inferred from mutant phenotype Ref.17. Source: UniProtKB

   Cellular_componentcaveola

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: Ensembl

early endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

extrinsic component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

recycling endosome membrane

Inferred from direct assay Ref.17. Source: UniProtKB

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 16189514Ref.19. Source: IntAct

phosphatidic acid binding

Inferred from direct assay Ref.17. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.17. Source: UniProtKB

transporter activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UNF0-1)

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.
Isoform 2 (identifier: Q9UNF0-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Protein kinase C and casein kinase substrate in neurons protein 2
PRO_0000161795

Regions

Domain11 – 7565FCH
Domain426 – 48661SH3
Region1 – 306306F-BAR domain
Coiled coil25 – 274250
Motif362 – 3643NPF1
Motif405 – 4073NPF2
Motif417 – 4193NPF3

Amino acid modifications

Modified residue531N6-acetyllysine By similarity

Natural variations

Alternative sequence344 – 38441Missing in isoform 2.
VSP_004517
Natural variant1751N → S.
Corresponds to variant rs35383004 [ dbSNP | Ensembl ].
VAR_053555
Natural variant2941M → I.
Corresponds to variant rs2746984 [ dbSNP | Ensembl ].
VAR_013711
Natural variant3241V → F.
Corresponds to variant rs1062913 [ dbSNP | Ensembl ].
VAR_013712

Experimental info

Sequence conflict1821L → F in AAD41781. Ref.1
Sequence conflict2561D → N in AAD41781. Ref.1
Sequence conflict3091N → I in AAD41781. Ref.1
Sequence conflict3361S → F in AAD41781. Ref.1
Sequence conflict378 – 3803DDT → EDI in AAD41781. Ref.1

Secondary structure

......................... 486
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 13, 2002. Version 2.
Checksum: 821DBEF65DAD1AA8

FASTA48655,739
        10         20         30         40         50         60 
MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCSD LMNCLHERAR IEKAYAQQLT 

        70         80         90        100        110        120 
EWARRWRQLV EKGPQYGTVE KAWMAFMSEA ERVSELHLEV KASLMNDDFE KIKNWQKEAF 

       130        140        150        160        170        180 
HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK EVEAAKKAHH AACKEEKLAI SREANSKADP 

       190        200        210        220        230        240 
SLNPEQLKKL QDKIEKCKQD VLKTKEKYEK SLKELDQGTP QYMENMEQVF EQCQQFEEKR 

       250        260        270        280        290        300 
LRFFREVLLE VQKHLDLSNV AGYKAIYHDL EQSIRAADAV EDLRWFRANH GPGMAMNWPQ 

       310        320        330        340        350        360 
FEEWSADLNR TLSRREKKKA TDGVTLTGIN QTGDQSLPSK PSSTLNVPSN PAQSAQSQSS 

       370        380        390        400        410        420 
YNPFEDEDDT GSTVSEKDDT KAKNVSSYEK TQSYPTDWSD DESNNPFSST DANGDSNPFD 

       430        440        450        460        470        480 
DDATSGTEVR VRALYDYEGQ EHDELSFKAG DELTKMEDED EQGWCKGRLD NGQVGLYPAN 


YVEAIQ 

« Hide

Isoform 2 [UniParc].

Checksum: 1DA87A2D42B5D5F9
Show »

FASTA44551,353

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS43023.1. [Q9UNF0-1]
CCDS54536.1. [Q9UNF0-2]
RefSeqNP_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]
UniGeneHs.162877.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9UNF0.
SMRQ9UNF0. Positions 16-303, 429-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116413. 33 interactions.
IntActQ9UNF0. 8 interactions.
MINTMINT-5005738.
STRING9606.ENSP00000263246.

PTM databases

PhosphoSiteQ9UNF0.

Polymorphism databases

DMDM22256968.

Proteomic databases

MaxQBQ9UNF0.
PaxDbQ9UNF0.
PRIDEQ9UNF0.

Protocols and materials databases

DNASU11252.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263246; ENSP00000263246; ENSG00000100266. [Q9UNF0-1]
ENST00000337959; ENSP00000338379; ENSG00000100266. [Q9UNF0-2]
ENST00000402229; ENSP00000385040; ENSG00000100266. [Q9UNF0-1]
ENST00000403744; ENSP00000385372; ENSG00000100266. [Q9UNF0-1]
ENST00000407585; ENSP00000385952; ENSG00000100266. [Q9UNF0-2]
GeneID11252.
KEGGhsa:11252.
UCSCuc003bdg.4. human. [Q9UNF0-1]

Organism-specific databases

CTD11252.
GeneCardsGC22M043243.
HGNCHGNC:8571. PACSIN2.
HPACAB009929.
HPA028852.
HPA049854.
MIM604960. gene.
neXtProtNX_Q9UNF0.
PharmGKBPA32897.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283356.
HOGENOMHOG000007245.
HOVERGENHBG053486.
InParanoidQ9UNF0.
OMACKQDVLK.
PhylomeDBQ9UNF0.
TreeFamTF313677.

Gene expression databases

ArrayExpressQ9UNF0.
BgeeQ9UNF0.
GenevestigatorQ9UNF0.

Family and domain databases

InterProIPR001060. FCH_dom.
IPR028521. PACSIN2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10959:SF2. PTHR10959:SF2. 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

ChiTaRSPACSIN2. human.
EvolutionaryTraceQ9UNF0.
GeneWikiPACSIN2.
GenomeRNAi11252.
NextBio42818.
PROQ9UNF0.
SOURCESearch...

Entry information

Entry namePACN2_HUMAN
AccessionPrimary (citable) accession number: Q9UNF0
Secondary accession number(s): O95921 expand/collapse secondary AC list , Q96HV9, Q9H0D3, Q9NPN1, Q9Y4V2
Entry history
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 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 22

Human chromosome 22: entries, gene names and cross-references to MIM