P60981 (DEST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Destrin

Alternative name(s):
Actin-depolymerizing factor
Short name=ADF

Gene names

Name:	DSTN
Synonyms:	ACTDP, DSN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner.
Tissue specificity	Widely distributed in various tissues.
Post-translational modification	ISGylated Probable. Ref.10
Sequence similarities	Belongs to the actin-binding proteins ADF family. Contains 1 ADF-H domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	actin filament severing Traceable author statement. Source: ProtInc actin polymerization or depolymerization Traceable author statement. Source: ProtInc
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 165	164	Destrin		PRO_0000214918
Regions
	Domain	4 – 153	150	ADF-H
	Motif	30 – 34	5	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7 Ref.11
	Modified residue	3	1	Phosphoserine Ref.9 Ref.11 Ref.12
	Modified residue	19	1	N6-acetyllysine Ref.13
	Modified residue	114	1	N6-acetyllysine Ref.13
Natural variations
	Natural variant	139	1	G → E in a colorectal cancer sample; somatic mutation. Ref.15		VAR_036459

Sequences

	Sequence		Length	Mass (Da)
	P60981 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8868A3167924100E	FASTA	165	18,506
	10 20 30 40 50 60 MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV 70 80 90 100 110 120 GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS 130 140 150 160 KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments." Hawkins M., Pope B., Maciver S.K., Weeds A.G. Biochemistry 32:9985-9993(1993) [PubMed: 8399167] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Lung.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13, ACETYLATION AT ALA-2. Tissue: Platelet.
[8]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 54-69, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets." Wong J.J., Pung Y.F., Sze N.S., Chin K.C. Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed: 16815975] [Abstract] Cited for: ISGYLATION.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY.
[13]	"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-19 AND LYS-114, MASS SPECTROMETRY.
[14]	"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].
[15]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-139.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S65738 mRNA. Translation: AAB28361.1. CR457042 mRNA. Translation: CAG33323.1. AK312645 mRNA. Translation: BAG35529.1. AL132765 Genomic DNA. Translation: CAC10585.1. CH471133 Genomic DNA. Translation: EAX10275.1. BC009477 mRNA. Translation: AAH09477.1.
IPI	IPI00473014.
PIR	A54184.
RefSeq	NP_001011546.1. NM_001011546.1. NP_006861.1. NM_006870.3.
UniGene	Hs.304192. Hs.705996.
3D structure databases
ProteinModelPortal	P60981.
SMR	P60981. Positions 2-165.
ModBase	Search...
Protein-protein interaction databases
IntAct	P60981. 2 interactions.
MINT	MINT-5001125.
STRING	P60981.
PTM databases
PhosphoSite	P60981.
Polymorphism databases
DMDM	46577586.
2D gel databases
OGP	P18282.
REPRODUCTION-2DPAGE	IPI00473014.
UCD-2DPAGE	P60981.
Proteomic databases
PRIDE	P60981.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000246069; ENSP00000246069; ENSG00000125868.
GeneID	11034.
KEGG	hsa:11034.
UCSC	uc002wpr.1. human.
Organism-specific databases
CTD	11034.
GeneCards	GC20P017550.
HGNC	HGNC:15750. DSTN.
HPA	CAB037094.
MIM	609114. gene.
neXtProt	NX_P60981.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11000.
GeneTree	ENSGT00440000033289.
HOGENOM	HBG628477.
HOVERGEN	HBG000381.
InParanoid	P60981.
OMA	QMLPEKD.
OrthoDB	EOG4FR0SR.
PhylomeDB	P60981.
Gene expression databases
ArrayExpress	P60981.
Bgee	P60981.
CleanEx	HS_DSTN.
Genevestigator	P60981.
GermOnline	ENSG00000125868. Homo sapiens.
Family and domain databases
InterPro	IPR002108. Actin-bd_cofilin/tropomyosin. IPR017904. ADF/Cofilin/Destrin. [Graphical view]
KO	K10363.
Pfam	PF00241. Cofilin_ADF. 1 hit. [Graphical view]
PRINTS	PR00006. COFILIN.
SMART	SM00102. ADF. 1 hit. [Graphical view]
PROSITE	PS51263. ADF_H. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	41930.
SOURCE	Search...

Entry information

Entry name

DEST_HUMAN

Accession

Primary (citable) accession number: P60981
Secondary accession number(s): B2R6N2 , P18282, Q5W166, Q6IAW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 86 of the entry and version 3 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.