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Protein

28S ribosomal protein S35, mitochondrial

Gene

MRPS35

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. structural constituent of ribosome Source: GO_Central

GO - Biological processi

  1. DNA damage response, detection of DNA damage Source: UniProtKB
  2. mitochondrial translation Source: Reactome
  3. mitochondrial translational elongation Source: Reactome
  4. mitochondrial translational initiation Source: Reactome
  5. mitochondrial translational termination Source: Reactome
  6. organelle organization Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_267634. Mitochondrial translation initiation.
REACT_268133. Mitochondrial translation elongation.
REACT_268261. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
28S ribosomal protein S35, mitochondrial
Short name:
MRP-S35
Short name:
S35mt
Alternative name(s):
28S ribosomal protein S28, mitochondrial
Short name:
MRP-S28
Short name:
S28mt
Gene namesi
Name:MRPS35Imported
Synonyms:MRPS281 Publication
ORF Names:HDCMD11P, MDS023, PSEC0213
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:16635. MRPS35.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. mitochondrial inner membrane Source: Reactome
  3. mitochondrial small ribosomal subunit Source: UniProtKB
  4. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31022.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 32328S ribosomal protein S35, mitochondrialPRO_0000046055
Transit peptidei1 – ?MitochondrionCurated

Proteomic databases

MaxQBiP82673.
PaxDbiP82673.
PRIDEiP82673.

PTM databases

PhosphoSiteiP82673.

Expressioni

Gene expression databases

BgeeiP82673.
CleanExiHS_MRPS28.
HS_MRPS35.
ExpressionAtlasiP82673. baseline and differential.
GenevestigatoriP82673.

Organism-specific databases

HPAiHPA038513.

Interactioni

Subunit structurei

Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins.By similarity

Protein-protein interaction databases

BioGridi121919. 31 interactions.
IntActiP82673. 6 interactions.
MINTiMINT-6773400.

Structurei

3D structure databases

ProteinModelPortaliP82673.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili257 – 32165Sequence AnalysisAdd
BLAST

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

eggNOGiNOG267668.
GeneTreeiENSGT00390000003443.
HOVERGENiHBG082941.
InParanoidiP82673.
KOiK17413.
OMAiTEWPSAL.
OrthoDBiEOG7QG44D.
PhylomeDBiP82673.
TreeFamiTF318686.

Family and domain databases

InterProiIPR019349. Ribosomal_S24/S35_mit.
[Graphical view]
PfamiPF10213. MRP-S28. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1Curated (identifier: P82673-1) [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
MAAAALPAWL SLQSRARTLR AFSTAVYSAT PVPTPSLPER TPGNERPPRR
60 70 80 90 100
KALPPRTEKM AVDQDWPSVY PVAAPFKPSA VPLPVRMGYP VKKGVPMAKE
110 120 130 140 150
GNLELLKIPN FLHLTPVAIK KHCEALKDFC TEWPAALDSD EKCEKHFPIE
160 170 180 190 200
IDSTDYVSSG PSVRNPRARV VVLRVKLSSL NLDDHAKKKL IKLVGERYCK
210 220 230 240 250
TTDVLTIKTD RCPLRRQNYD YAVYLLTVLY HESWNTEEWE KSKTEADMEE
260 270 280 290 300
YIWENSSSER NILETLLQMK AAEKNMEINK EELLGTKEIE EYKKSVVSLK
310 320
NEEENENSIS QYKESVKRLL NVT
Length:323
Mass (Da):36,844
Last modified:September 30, 2000 - v1
Checksum:iB29F819E914F2B49
GO
Isoform 2Curated (identifier: P82673-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     176-194: KLSSLNLDDHAKKKLIKLV → PFKEAELRLCSVSTNSVIP
     195-323: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:194
Mass (Da):21,390
Checksum:i69648AE388E7995A
GO

Sequence cautioni

The sequence AAG14958.1 differs from that shown. Reason: Frameshift at position 97. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61L → I.
Corresponds to variant rs35475802 [ dbSNP | Ensembl ].
VAR_052051

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei176 – 19419KLSSL…LIKLV → PFKEAELRLCSVSTNSVIP in isoform 2. 1 PublicationVSP_054096Add
BLAST
Alternative sequencei195 – 323129Missing in isoform 2. 1 PublicationVSP_054097Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182422 mRNA. Translation: AAG14958.1. Frameshift.
AK075378 mRNA. Translation: BAC11579.1.
AK075515 mRNA. Translation: BAC11664.1.
BC015862 mRNA. Translation: AAH15862.2.
BC017086 mRNA. Translation: AAH17086.1.
BC028346 mRNA. Translation: AAH28346.2.
BC063515 mRNA. Translation: AAH63515.1.
BC109372 mRNA. Translation: AAI09373.1.
AL512733 mRNA. Translation: CAC21665.1.
AF068296 mRNA. Translation: AAF65185.1.
CCDSiCCDS53769.1. [P82673-2]
CCDS8714.1. [P82673-1]
RefSeqiNP_001177793.1. NM_001190864.1. [P82673-2]
NP_068593.2. NM_021821.3. [P82673-1]
UniGeneiHs.714076.

Genome annotation databases

EnsembliENST00000081029; ENSP00000081029; ENSG00000061794. [P82673-1]
ENST00000538315; ENSP00000445390; ENSG00000061794. [P82673-2]
GeneIDi60488.
KEGGihsa:60488.
UCSCiuc001rih.3. human. [P82673-1]

Polymorphism databases

DMDMi74708095.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182422 mRNA. Translation: AAG14958.1. Frameshift.
AK075378 mRNA. Translation: BAC11579.1.
AK075515 mRNA. Translation: BAC11664.1.
BC015862 mRNA. Translation: AAH15862.2.
BC017086 mRNA. Translation: AAH17086.1.
BC028346 mRNA. Translation: AAH28346.2.
BC063515 mRNA. Translation: AAH63515.1.
BC109372 mRNA. Translation: AAI09373.1.
AL512733 mRNA. Translation: CAC21665.1.
AF068296 mRNA. Translation: AAF65185.1.
CCDSiCCDS53769.1. [P82673-2]
CCDS8714.1. [P82673-1]
RefSeqiNP_001177793.1. NM_001190864.1. [P82673-2]
NP_068593.2. NM_021821.3. [P82673-1]
UniGeneiHs.714076.

3D structure databases

ProteinModelPortaliP82673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121919. 31 interactions.
IntActiP82673. 6 interactions.
MINTiMINT-6773400.

PTM databases

PhosphoSiteiP82673.

Polymorphism databases

DMDMi74708095.

Proteomic databases

MaxQBiP82673.
PaxDbiP82673.
PRIDEiP82673.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000081029; ENSP00000081029; ENSG00000061794. [P82673-1]
ENST00000538315; ENSP00000445390; ENSG00000061794. [P82673-2]
GeneIDi60488.
KEGGihsa:60488.
UCSCiuc001rih.3. human. [P82673-1]

Organism-specific databases

CTDi60488.
GeneCardsiGC12P027863.
HGNCiHGNC:16635. MRPS35.
HPAiHPA038513.
MIMi611995. gene.
neXtProtiNX_P82673.
PharmGKBiPA31022.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG267668.
GeneTreeiENSGT00390000003443.
HOVERGENiHBG082941.
InParanoidiP82673.
KOiK17413.
OMAiTEWPSAL.
OrthoDBiEOG7QG44D.
PhylomeDBiP82673.
TreeFamiTF318686.

Enzyme and pathway databases

ReactomeiREACT_267634. Mitochondrial translation initiation.
REACT_268133. Mitochondrial translation elongation.
REACT_268261. Mitochondrial translation termination.

Miscellaneous databases

ChiTaRSiMRPS35. human.
GeneWikiiMRPS35.
GenomeRNAii60488.
NextBioi65371.
PROiP82673.
SOURCEiSearch...

Gene expression databases

BgeeiP82673.
CleanExiHS_MRPS28.
HS_MRPS35.
ExpressionAtlasiP82673. baseline and differential.
GenevestigatoriP82673.

Family and domain databases

InterProiIPR019349. Ribosomal_S24/S35_mit.
[Graphical view]
PfamiPF10213. MRP-S28. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
    Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hematopoietic stem cell.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Teratocarcinoma.
  3. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryo.
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: ColonImported, LungImported and PancreasImported.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-323 (ISOFORM 1).
    Tissue: Melanoma.
  6. "A novel gene from human dendritic cells."
    Zhao Z., Huang X., Li N., Zhu X., Cao X.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 180-323 (ISOFORM 1).
    Tissue: Dendritic cellImported.
  7. "Identification of four proteins from the small subunit of the mammalian mitochondrial ribosome using a proteomics approach."
    Koc E.C., Burkhart W., Blackburn K., Koc H., Moseley A., Spremulli L.L.
    Protein Sci. 10:471-481(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRT35_HUMAN
AccessioniPrimary (citable) accession number: P82673
Secondary accession number(s): Q32LZ1
, Q6P4C6, Q7L1M6, Q8NBP4, Q96AI0, Q9H044, Q9HC14, Q9P1R5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2006
Last sequence update: September 30, 2000
Last modified: March 31, 2015
This is version 98 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 12
    Human chromosome 12: 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.