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Protein

28S ribosomal protein S29, mitochondrial

Gene

DAP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in mediating interferon-gamma-induced cell death.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. apoptotic mitochondrial changes Source: Ensembl
  2. apoptotic signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_267602. Mitochondrial translation termination.
REACT_267677. Mitochondrial translation elongation.
REACT_267680. Mitochondrial translation initiation.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DAP3
Synonyms:MRPS29
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2673. DAP3.

Subcellular locationi

Mitochondrion 2 Publications

GO - Cellular componenti

  1. mitochondrial ribosome Source: InterPro
  2. mitochondrion Source: UniProtKB
  3. nucleolus Source: HPA
  4. nucleoplasm Source: HPA
  5. nucleus Source: HPA
  6. small ribosomal subunit Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27141.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1818Mitochondrion1 PublicationAdd
BLAST
Chaini19 – 39838028S ribosomal protein S29, mitochondrialPRO_0000087717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei175 – 1751N6-acetyllysine1 Publication
Modified residuei207 – 2071N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP51398.
PaxDbiP51398.
PeptideAtlasiP51398.
PRIDEiP51398.

PTM databases

PhosphoSiteiP51398.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP51398.
CleanExiHS_DAP3.
ExpressionAtlasiP51398. baseline and differential.
GenevestigatoriP51398.

Organism-specific databases

HPAiHPA006076.
HPA023687.

Interactioni

Subunit structurei

Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. Interacts with KIAA0141. Interacts with NOA1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NOA1Q8NC605EBI-355912,EBI-717871

Protein-protein interaction databases

BioGridi113587. 50 interactions.
IntActiP51398. 12 interactions.
MINTiMINT-1149113.
STRINGi9606.ENSP00000341692.

Structurei

3D structure databases

ProteinModelPortaliP51398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG260931.
GeneTreeiENSGT00390000015248.
HOGENOMiHOG000046851.
HOVERGENiHBG025946.
InParanoidiP51398.
KOiK17408.
OMAiMVKNDWH.
OrthoDBiEOG7GQXVS.
PhylomeDBiP51398.
TreeFamiTF313726.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR019368. Ribosomal_S23/S29_mit.
IPR008092. Ribosomal_S29_mit.
[Graphical view]
PfamiPF10236. DAP3. 1 hit.
[Graphical view]
PRINTSiPR01716. DEATHASSOCP3.
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P51398-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MMLKGITRLI SRIHKLDPGR FLHMGTQARQ SIAAHLDNQV PVESPRAISR
60 70 80 90 100
TNENDPAKHG DQHEGQHYNI SPQDLETVFP HGLPPRFVMQ VKTFSEACLM
110 120 130 140 150
VRKPALELLH YLKNTSFAYP AIRYLLYGEK GTGKTLSLCH VIHFCAKQDW
160 170 180 190 200
LILHIPDAHL WVKNCRDLLQ SSYNKQRFDQ PLEASTWLKN FKTTNERFLN
210 220 230 240 250
QIKVQEKYVW NKRESTEKGS PLGEVVEQGI TRVRNATDAV GIVLKELKRQ
260 270 280 290 300
SSLGMFHLLV AVDGINALWG RTTLKREDKS PIAPEELALV HNLRKMMKND
310 320 330 340 350
WHGGAIVSAL SQTGSLFKPR KAYLPQELLG KEGFDALDPF IPILVSNYNP
360 370 380 390
KEFESCIQYY LENNWLQHEK APTEEGKKEL LFLSNANPSL LERHCAYL
Length:398
Mass (Da):45,566
Last modified:October 1, 1996 - v1
Checksum:i778AF183FA04DEC8
GO
Isoform 2 (identifier: P51398-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:357
Mass (Da):41,044
Checksum:i20E08FFBBF9C2E57
GO
Isoform 3 (identifier: P51398-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:364
Mass (Da):41,673
Checksum:iA51F7F4E1B0B12B0
GO

Sequence cautioni

The sequence AAA57443.1 differs from that shown. Reason: Frameshift at position 349. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571D → Y in BAG63624. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti240 – 2401V → F.
Corresponds to variant rs57692591 [ dbSNP | Ensembl ].
VAR_061811

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei16 – 5641Missing in isoform 2. 1 PublicationVSP_042790Add
BLAST
Alternative sequencei57 – 9034Missing in isoform 3. 1 PublicationVSP_044639Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1120.1. [P51398-1]
CCDS55646.1. [P51398-3]
CCDS55647.1. [P51398-2]
PIRiG01589.
RefSeqiNP_001186778.1. NM_001199849.1. [P51398-1]
NP_001186779.1. NM_001199850.1. [P51398-3]
NP_001186780.1. NM_001199851.1. [P51398-2]
NP_004623.1. NM_004632.3. [P51398-1]
NP_387506.1. NM_033657.2. [P51398-1]
XP_005245537.1. XM_005245480.1. [P51398-3]
XP_005245538.1. XM_005245481.1. [P51398-2]
UniGeneiHs.516746.

Genome annotation databases

EnsembliENST00000343043; ENSP00000341692; ENSG00000132676. [P51398-1]
ENST00000368336; ENSP00000357320; ENSG00000132676. [P51398-1]
ENST00000421487; ENSP00000412605; ENSG00000132676. [P51398-3]
ENST00000471642; ENSP00000476592; ENSG00000132676. [P51398-2]
ENST00000535183; ENSP00000445003; ENSG00000132676. [P51398-2]
GeneIDi7818.
KEGGihsa:7818.
UCSCiuc001flq.3. human. [P51398-1]
uc010pgl.2. human. [P51398-2]

Polymorphism databases

DMDMi1706299.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1120.1. [P51398-1]
CCDS55646.1. [P51398-3]
CCDS55647.1. [P51398-2]
PIRiG01589.
RefSeqiNP_001186778.1. NM_001199849.1. [P51398-1]
NP_001186779.1. NM_001199850.1. [P51398-3]
NP_001186780.1. NM_001199851.1. [P51398-2]
NP_004623.1. NM_004632.3. [P51398-1]
NP_387506.1. NM_033657.2. [P51398-1]
XP_005245537.1. XM_005245480.1. [P51398-3]
XP_005245538.1. XM_005245481.1. [P51398-2]
UniGeneiHs.516746.

3D structure databases

ProteinModelPortaliP51398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113587. 50 interactions.
IntActiP51398. 12 interactions.
MINTiMINT-1149113.
STRINGi9606.ENSP00000341692.

PTM databases

PhosphoSiteiP51398.

Polymorphism databases

DMDMi1706299.

Proteomic databases

MaxQBiP51398.
PaxDbiP51398.
PeptideAtlasiP51398.
PRIDEiP51398.

Protocols and materials databases

DNASUi7818.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343043; ENSP00000341692; ENSG00000132676. [P51398-1]
ENST00000368336; ENSP00000357320; ENSG00000132676. [P51398-1]
ENST00000421487; ENSP00000412605; ENSG00000132676. [P51398-3]
ENST00000471642; ENSP00000476592; ENSG00000132676. [P51398-2]
ENST00000535183; ENSP00000445003; ENSG00000132676. [P51398-2]
GeneIDi7818.
KEGGihsa:7818.
UCSCiuc001flq.3. human. [P51398-1]
uc010pgl.2. human. [P51398-2]

Organism-specific databases

CTDi7818.
GeneCardsiGC01P155657.
HGNCiHGNC:2673. DAP3.
HPAiHPA006076.
HPA023687.
MIMi602074. gene.
neXtProtiNX_P51398.
PharmGKBiPA27141.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG260931.
GeneTreeiENSGT00390000015248.
HOGENOMiHOG000046851.
HOVERGENiHBG025946.
InParanoidiP51398.
KOiK17408.
OMAiMVKNDWH.
OrthoDBiEOG7GQXVS.
PhylomeDBiP51398.
TreeFamiTF313726.

Enzyme and pathway databases

ReactomeiREACT_267602. Mitochondrial translation termination.
REACT_267677. Mitochondrial translation elongation.
REACT_267680. Mitochondrial translation initiation.

Miscellaneous databases

GeneWikiiDAP3.
GenomeRNAii7818.
NextBioi30217.
PROiP51398.
SOURCEiSearch...

Gene expression databases

BgeeiP51398.
CleanExiHS_DAP3.
ExpressionAtlasiP51398. baseline and differential.
GenevestigatoriP51398.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR019368. Ribosomal_S23/S29_mit.
IPR008092. Ribosomal_S29_mit.
[Graphical view]
PfamiPF10236. DAP3. 1 hit.
[Graphical view]
PRINTSiPR01716. DEATHASSOCP3.
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: SUBCELLULAR LOCATION, TRANSIT PEPTIDE CLEAVAGE SITE.
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRT29_HUMAN
AccessioniPrimary (citable) accession number: P51398
Secondary accession number(s): B4DP59
, B4DY62, E7EM60, Q13044, Q68CT7, Q96Q20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.