Q9UKS6 (PACN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein kinase C and casein kinase substrate in neurons protein 3

Alternative name(s):
SH3 domain-containing protein 6511

Gene names

Name:

PACSIN3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in endocytosis By similarity. Ref.2
Subunit structure	May form homo- and heterooligomers with other PACSINs By similarity. Interacts with DNM1, SYNJ1 and WASL through its SH3 domain By similarity.
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Detected at the inner aspect of the plasma membrane in myotubes By similarity. Ref.3
Tissue specificity	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. Ref.2 Ref.3
Post-translational modification	Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC) Probable.
Sequence similarities	Belongs to the PACSIN family. Contains 1 FCH domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil SH3 domain
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of endocytosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of membrane protein ectodomain proteolysis Inferred from mutant phenotype PubMed 15280379. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cytoskeletal protein binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADAM15	Q13444	2	EBI-77926,EBI-77818
ADAM9	Q13443	2	EBI-77926,EBI-77903
SOS1	Q07889	2	EBI-77926,EBI-297487
SOS2	Q07890	2	EBI-77926,EBI-298181

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 424	424	Protein kinase C and casein kinase substrate in neurons protein 3		PRO_0000161800
Regions
	Domain	10 – 73	64	FCH
	Domain	363 – 424	62	SH3
	Coiled coil	167 – 217	51	Potential
Amino acid modifications
	Modified residue	276	1	Phosphoserine Ref.11
	Modified residue	319	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.11
	Modified residue	324	1	Phosphothreonine Ref.9
	Modified residue	327	1	Phosphoserine Ref.9
	Modified residue	354	1	Phosphoserine Ref.9 Ref.11 Ref.13
	Modified residue	383	1	Phosphoserine Ref.9 Ref.10 Ref.11
Natural variations
	Natural variant	61	1	A → V. Ref.1 Corresponds to variant rs7106654 [ dbSNP | Ensembl ].		VAR_053556

Sequences

	Sequence		Length	Mass (Da)
	Q9UKS6 [UniParc]. Last modified August 13, 2002. Version 2. Checksum: 6DBD940AE6D1F352	FASTA	424	48,487
	10 20 30 40 50 60 MAPEEDAGGE ALGGSFWEAG NYRRTVQRVE DGHRLCGDLV SCFQERARIE KAYAQQLADW 70 80 90 100 110 120 ARKWRGTVEK GPQYGTLEKA WHAFFTAAER LSALHLEVRE KLQGQDSERV RAWQRGAFHR 130 140 150 160 170 180 PVLGGFRESR AAEDGFRKAQ KPWLKRLKEV EASKKSYHAA RKDEKTAQTR ESHAKADSAV 190 200 210 220 230 240 SQEQLRKLQE RVERCAKEAE KTKAQYEQTL AELHRYTPRY MEDMEQAFET CQAAERQRLL 250 260 270 280 290 300 FFKDMLLTLH QHLDLSSSEK FHELHRDLHQ GIEAASDEED LRWWRSTHGP GMAMNWPQFE 310 320 330 340 350 360 EWSLDTQRTI SRKEKGGRSP DEVTLTSIVP TRDGTAPPPQ SPGSPGTGQD EEWSDEESPR 370 380 390 400 410 420 KAATGVRVRA LYDYAGQEAD ELSFRAGEEL LKMSEEDEQG WCQGQLQSGR IGLYPANYVE CVGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1999) [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(2000) [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(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [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]. 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(2004) [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(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, MASS SPECTROMETRY. 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(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; THR-324; SER-327; SER-354 AND SER-383, MASS SPECTROMETRY. 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(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, MASS SPECTROMETRY. 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(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-319; SER-354 AND SER-383, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[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(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00329572.
RefSeq	NP_001171903.1. NM_001184974.1. NP_001171904.1. NM_001184975.1. NP_057307.2. NM_016223.4.
UniGene	Hs.334639.
3D structure databases
ProteinModelPortal	Q9UKS6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UKS6. 5 interactions.
MINT	MINT-5002056.
STRING	9606.ENSP00000298838.
PTM databases
PhosphoSite	Q9UKS6.
Polymorphism databases
DMDM	22256967.
Proteomic databases
PaxDb	Q9UKS6.
PRIDE	Q9UKS6.
Protocols and materials databases
DNASU	29763.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000298838; ENSP00000298838; ENSG00000165912. ENST00000528462; ENSP00000437252; ENSG00000165912. ENST00000539589; ENSP00000440945; ENSG00000165912.
GeneID	29763.
KEGG	hsa:29763.
UCSC	uc001ndw.3. human.
Organism-specific databases
CTD	29763.
GeneCards	GC11M047199.
HGNC	HGNC:8572. PACSIN3.
HPA	HPA039480. HPA043904.
MIM	606513. gene.
neXtProt	NX_Q9UKS6.
PharmGKB	PA32898.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG283356.
HOVERGEN	HBG053486.
InParanoid	Q9UKS6.
OMA	EQAFESC.
OrthoDB	EOG44QT13.
Gene expression databases
ArrayExpress	Q9UKS6.
Bgee	Q9UKS6.
CleanEx	HS_PACSIN3.
Genevestigator	Q9UKS6.
GermOnline	ENSG00000165912. Homo sapiens.
Family and domain databases
InterPro	IPR001060. FCH_dom. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00611. FCH. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00452. SH3DOMAIN.
SMART	SM00055. FCH. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS50133. FCH. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	29763.
NextBio	52258.
SOURCE	Search...

Entry information

Entry name

PACN3_HUMAN

Accession

Primary (citable) accession number: Q9UKS6
Secondary accession number(s): A6NH84, Q9H331, Q9NWV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 2002
Last sequence update:	August 13, 2002
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.