P51398 (RT29_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
28S ribosomal protein S29, mitochondrial
Short name=MRP-S29
Short name=S29mt

Alternative name(s):
Death-associated protein 3
Short name=DAP-3
Ionizing radiation resistance conferring protein

Gene names

Name:	DAP3
Synonyms:	MRPS29

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	398 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	Involved in mediating interferon-gamma-induced cell death.
Subunit structure	Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. Interacts with KIAA0141. Interacts with NOA1. Ref.12 Ref.14
Subcellular location	Mitochondrion Ref.10 Ref.14.
Tissue specificity	Ubiquitous.
Sequence caution	The sequence AAA57443.1 differs from that shown. Reason: Frameshift at position 349.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic mitochondrial changes Inferred from electronic annotation. Source: Compara apoptotic signaling pathway Traceable author statement Ref.2. Source: ProtInc
Cellular_component	mitochondrial ribosome Inferred from electronic annotation. Source: InterPro mitochondrion Inferred from direct assay Ref.14. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA small ribosomal subunit Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NOA1	Q8NC60	5	EBI-355912,EBI-717871

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P51398-1)

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: P51398-2)

The sequence of this isoform differs from the canonical sequence as follows:
     16-56: Missing.

Isoform 3 (identifier: P51398-3)

The sequence of this isoform differs from the canonical sequence as follows:
     57-90: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 18	18	Mitochondrion Probable
	Chain	19 – 398	380	28S ribosomal protein S29, mitochondrial		PRO_0000087717
Amino acid modifications
	Modified residue	175	1	N6-acetyllysine Ref.13
	Modified residue	207	1	N6-acetyllysine Ref.13
Natural variations
	Alternative sequence	16 – 56	41	Missing in isoform 2.		VSP_042790
	Alternative sequence	57 – 90	34	Missing in isoform 3.		VSP_044639
	Natural variant	240	1	V → F. Corresponds to variant rs57692591 [ dbSNP | Ensembl ].		VAR_061811
Experimental info
	Sequence conflict	157	1	D → Y in BAG63624. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 778AF183FA04DEC8	FASTA	398	45,566
	10 20 30 40 50 60 MMLKGITRLI SRIHKLDPGR FLHMGTQARQ SIAAHLDNQV PVESPRAISR TNENDPAKHG 70 80 90 100 110 120 DQHEGQHYNI SPQDLETVFP HGLPPRFVMQ VKTFSEACLM VRKPALELLH YLKNTSFAYP 130 140 150 160 170 180 AIRYLLYGEK GTGKTLSLCH VIHFCAKQDW LILHIPDAHL WVKNCRDLLQ SSYNKQRFDQ 190 200 210 220 230 240 PLEASTWLKN FKTTNERFLN QIKVQEKYVW NKRESTEKGS PLGEVVEQGI TRVRNATDAV 250 260 270 280 290 300 GIVLKELKRQ SSLGMFHLLV AVDGINALWG RTTLKREDKS PIAPEELALV HNLRKMMKND 310 320 330 340 350 360 WHGGAIVSAL SQTGSLFKPR KAYLPQELLG KEGFDALDPF IPILVSNYNP KEFESCIQYY 370 380 390 LENNWLQHEK APTEEGKKEL LFLSNANPSL LERHCAYL
	Isoform 2 [UniParc]. Checksum: 20E08FFBBF9C2E57	FASTA	357	41,044
	10 20 30 40 50 60 MMLKGITRLI SRIHKAKHGD QHEGQHYNIS PQDLETVFPH GLPPRFVMQV KTFSEACLMV 70 80 90 100 110 120 RKPALELLHY LKNTSFAYPA IRYLLYGEKG TGKTLSLCHV IHFCAKQDWL ILHIPDAHLW 130 140 150 160 170 180 VKNCRDLLQS SYNKQRFDQP LEASTWLKNF KTTNERFLNQ IKVQEKYVWN KRESTEKGSP 190 200 210 220 230 240 LGEVVEQGIT RVRNATDAVG IVLKELKRQS SLGMFHLLVA VDGINALWGR TTLKREDKSP 250 260 270 280 290 300 IAPEELALVH NLRKMMKNDW HGGAIVSALS QTGSLFKPRK AYLPQELLGK EGFDALDPFI 310 320 330 340 350 PILVSNYNPK EFESCIQYYL ENNWLQHEKA PTEEGKKELL FLSNANPSLL ERHCAYL
	Isoform 3 [UniParc]. Checksum: A51F7F4E1B0B12B0	FASTA	364	41,673
	10 20 30 40 50 60 MMLKGITRLI SRIHKLDPGR FLHMGTQARQ SIAAHLDNQV PVESPRAISR TNENDPVKTF 70 80 90 100 110 120 SEACLMVRKP ALELLHYLKN TSFAYPAIRY LLYGEKGTGK TLSLCHVIHF CAKQDWLILH 130 140 150 160 170 180 IPDAHLWVKN CRDLLQSSYN KQRFDQPLEA STWLKNFKTT NERFLNQIKV QEKYVWNKRE 190 200 210 220 230 240 STEKGSPLGE VVEQGITRVR NATDAVGIVL KELKRQSSLG MFHLLVAVDG INALWGRTTL 250 260 270 280 290 300 KREDKSPIAP EELALVHNLR KMMKNDWHGG AIVSALSQTG SLFKPRKAYL PQELLGKEGF 310 320 330 340 350 360 DALDPFIPIL VSNYNPKEFE SCIQYYLENN WLQHEKAPTE EGKKELLFLS NANPSLLERH CAYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The molecular genetics of human diseases with defective DNA damage processing." Henning K.A. Thesis (1993), University of Stanford, United States Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Cervix carcinoma.
[2]	"Isolation of DAP3, a novel mediator of interferon-gamma-induced cell death." Kissil J.L., Deiss L.P., Bayewitch M., Raveh T., Khaspekov G., Kimchi A. J. Biol. Chem. 270:27932-27936(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Testis.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Colon endothelium.
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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].
[8]	"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).
[9]	"The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders." Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S., Watanabe K., Tanaka T. Genomics 77:65-70(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-235.
[10]	"A conserved N-terminal sequence targets human DAP3 to mitochondria." Morgan C.J., Jacques C., Savagner F., Tourmen Y., Mirebeau D.P., Malthiery Y., Reynier P. Biochem. Biophys. Res. Commun. 280:177-181(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TRANSIT PEPTIDE.
[11]	"The small subunit of the mammalian mitochondrial ribosome: identification of the full complement of ribosomal proteins present." Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L. J. Biol. Chem. 276:19363-19374(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[12]	"hNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis." Tang T., Zheng B., Chen S.H., Murphy A.N., Kudlicka K., Zhou H., Farquhar M.G. J. Biol. Chem. 284:5414-5424(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NOA1.
[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.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-175 AND LYS-207, MASS SPECTROMETRY.
[14]	"Identification of DELE, a novel DAP3-binding protein which is crucial for death receptor-mediated apoptosis induction." Harada T., Iwai A., Miyazaki T. Apoptosis 15:1247-1255(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KIAA0141.
[15]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U18321 mRNA. Translation: AAA57443.1. Frameshift. X83544 mRNA. Translation: CAA58535.1. AK293117 mRNA. Translation: BAF85806.1. AK298201 mRNA. Translation: BAG60471.1. AK302281 mRNA. Translation: BAG63624.1. BT019494 mRNA. Translation: AAV38301.1. CR749790 mRNA. Translation: CAH18651.1. AL162734 Genomic DNA. Translation: CAH71647.1. CH471121 Genomic DNA. Translation: EAW53044.1. CH471121 Genomic DNA. Translation: EAW53045.1. CH471121 Genomic DNA. Translation: EAW53047.1. CH471121 Genomic DNA. Translation: EAW53048.1. CH471121 Genomic DNA. Translation: EAW53049.1. CH471121 Genomic DNA. Translation: EAW53051.1. BC107487 mRNA. Translation: AAI07488.1. BC107488 mRNA. Translation: AAI07489.1.
IPI	IPI00018120. IPI00910684.
PIR	G01589.
RefSeq	NP_001186778.1. NM_001199849.1. NP_001186779.1. NM_001199850.1. NP_001186780.1. NM_001199851.1. NP_004623.1. NM_004632.3. NP_387506.1. NM_033657.2.
UniGene	Hs.516746.
3D structure databases
ProteinModelPortal	P51398.
SMR	P51398. Positions 122-154.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51398. 8 interactions.
MINT	MINT-1149113.
STRING	9606.ENSP00000341692.
PTM databases
PhosphoSite	P51398.
Polymorphism databases
DMDM	1706299.
Proteomic databases
PaxDb	P51398.
PeptideAtlas	P51398.
PRIDE	P51398.
Protocols and materials databases
DNASU	7818.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000343043; ENSP00000341692; ENSG00000132676. ENST00000368336; ENSP00000357320; ENSG00000132676. ENST00000421487; ENSP00000412605; ENSG00000132676. ENST00000535183; ENSP00000445003; ENSG00000132676.
GeneID	7818.
KEGG	hsa:7818.
UCSC	uc001flq.3. human. uc010pgl.2. human. uc010pgm.2. human.
Organism-specific databases
CTD	7818.
GeneCards	GC01P155657.
HGNC	HGNC:2673. DAP3.
HPA	HPA006076. HPA023687.
MIM	602074. gene.
neXtProt	NX_P51398.
PharmGKB	PA27141.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG260931.
HOGENOM	HOG000046851.
HOVERGEN	HBG025946.
InParanoid	P51398.
OMA	NERFLNQ.
OrthoDB	EOG4K9BCH.
PhylomeDB	P51398.
Enzyme and pathway databases
Pathway_Interaction_DB	trail_pathway. TRAIL signaling pathway.
Gene expression databases
ArrayExpress	P51398.
Bgee	P51398.
CleanEx	HS_DAP3.
Genevestigator	P51398.
GermOnline	ENSG00000132676. Homo sapiens.
Family and domain databases
InterPro	IPR019368. Ribosomal_S23/S29_mit. IPR008092. Ribosomal_S29_mit. [Graphical view]
Pfam	PF10236. DAP3. 1 hit. [Graphical view]
PRINTS	PR01716. DEATHASSOCP3.
ProtoNet	Search...
Other
GenomeRNAi	7818.
NextBio	30217.
SOURCE	Search...

Entry information

Entry name

RT29_HUMAN

Accession

Primary (citable) accession number: P51398
Secondary accession number(s): B4DP59 , B4DY62, E7EM60, Q13044, Q68CT7, Q96Q20

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 118 of the entry and version 1 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.