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Q9UNF0 (PACN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 99. 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·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
Gene names
Name:PACSIN2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

May play a role in vesicle formation and transport. Ref.7

Subunit structure

Homo- and hetero-aggregates with other PACSINs. Binds dynamin 1, synaptojanin, synapsin 1 and the neural Wiskott-Aldrich syndrome protein (N-WASP) By similarity.

Subcellular location

Cytoplasmic vesicle By similarity. Note: Vesicle-like cytoplasmic distribution By similarity.

Tissue specificity

Ubiquitously expressed.

Post-translational modification

Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC) By similarity. Ref.8

Sequence similarities

Belongs to the PACSIN family.

Contains 1 FCH domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCytoplasmic vesicle
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
SH3 domain
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processactin cytoskeleton organization

Traceable author statement. Source: ProtInc

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontransporter activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

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
Coiled coil184 – 21936 Potential

Amino acid modifications

Modified residue1171N6-acetyllysine Ref.9
Modified residue3701Phosphothreonine Ref.8
Modified residue3721Phosphoserine Ref.8
Modified residue3731Phosphothreonine Ref.8
Modified residue3751Phosphoserine Ref.8

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: 10431838] [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: 11230166] [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: 15461802] [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: 10591208] [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: 15489334] [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: 11082044] [Abstract]
Cited for: FUNCTION.
[8]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-370; SER-372; THR-373 AND SER-375, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, MASS SPECTROMETRY.
[10]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
IPIIPI00027009.
IPI00221111.
RefSeqNP_001171899.1. NM_001184970.1.
NP_001171900.1. NM_001184971.1.
NP_009160.2. NM_007229.3.
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[»]
ProteinModelPortalQ9UNF0.
SMRQ9UNF0. Positions 16-303, 429-484.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9UNF0. 7 interactions.
MINTMINT-5005738.
STRINGQ9UNF0.

PTM databases

PhosphoSiteQ9UNF0.

Polymorphism databases

DMDM22256968.

Proteomic databases

PRIDEQ9UNF0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263246; ENSP00000263246; ENSG00000100266.
ENST00000402229; ENSP00000385040; ENSG00000100266.
ENST00000403744; ENSP00000385372; ENSG00000100266.
ENST00000436831; ENSP00000409214; ENSG00000100266.
GeneID11252.
KEGGhsa:11252.
UCSCuc003bde.2. human.
uc003bdf.2. human.

Organism-specific databases

CTD11252.
GeneCardsGC22M043243.
H-InvDBHIX0016548.
HGNCHGNC:8571. PACSIN2.
HPACAB009929.
HPA028852.
MIM604960. gene.
neXtProtNX_Q9UNF0.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06183.
GeneTreeENSGT00510000046376.
HOVERGENHBG053486.
InParanoidQ9UNF0.
OMAKAKNVSS.
PhylomeDBQ9UNF0.

Gene expression databases

ArrayExpressQ9UNF0.
BgeeQ9UNF0.
GenevestigatorQ9UNF0.
GermOnlineENSG00000100266. Homo sapiens.

Family and domain databases

InterProIPR001060. FCH.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SH3. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio42818.
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: January 25, 2012
This is version 99 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

Human chromosome 22

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families