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Protein
Submitted name:

40S ribosomal protein SA

Gene

RPSA

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.SAAS annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal proteinUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Submitted name:
40S ribosomal protein SAImported
Gene namesi
Name:RPSAImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6502. RPSA.

Subcellular locationi

  • Cytoplasm SAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmSAAS annotation

PTM / Processingi

Proteomic databases

EPDiC9J9K3.
PaxDbiC9J9K3.
PRIDEiC9J9K3.

Expressioni

Gene expression databases

BgeeiC9J9K3.
ExpressionAtlasiC9J9K3. baseline and differential.

Interactioni

Protein-protein interaction databases

IntActiC9J9K3. 12 interactions.
MINTiMINT-8395011.
STRINGi9606.ENSP00000346067.

Structurei

3D structure databases

ProteinModelPortaliC9J9K3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini202 – 2646340S_SA_CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S2P family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG0830. Eukaryota.
COG0052. LUCA.
GeneTreeiENSGT00390000015036.
HOGENOMiHOG000232073.

Family and domain databases

HAMAPiMF_03015. Ribosomal_S2_euk.
InterProiIPR032281. 40S_SA_C.
IPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF16122. 40S_SA_C. 1 hit.
PF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. uS2_euk_arch. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

C9J9K3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN
60 70 80 90 100
LKRTWEKLLL AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA
110 120 130 140 150
GRFTPGTFTN QIQAAFREPR LLVVTDPRAD HQPLTEASYV NLPTIALCNT
160 170 180 190 200
DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR EVLRMRGTIS REHPWEVMPD
210 220 230 240 250
LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA TQPEVADWSE
260
GVQVPSVPIQ QFPT
Length:264
Mass (Da):29,506
Last modified:February 17, 2016 - v7
Checksum:i5DE1A98D0935F3C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei264 – 2641Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC099332 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000458478; ENSP00000410848; ENSG00000168028.
UCSCiuc062ijz.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC099332 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliC9J9K3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiC9J9K3. 12 interactions.
MINTiMINT-8395011.
STRINGi9606.ENSP00000346067.

Proteomic databases

EPDiC9J9K3.
PaxDbiC9J9K3.
PRIDEiC9J9K3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000458478; ENSP00000410848; ENSG00000168028.
UCSCiuc062ijz.1. human.

Organism-specific databases

HGNCiHGNC:6502. RPSA.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0830. Eukaryota.
COG0052. LUCA.
GeneTreeiENSGT00390000015036.
HOGENOMiHOG000232073.

Miscellaneous databases

ChiTaRSiRPSA. human.
NextBioi35485606.

Gene expression databases

BgeeiC9J9K3.
ExpressionAtlasiC9J9K3. baseline and differential.

Family and domain databases

HAMAPiMF_03015. Ribosomal_S2_euk.
InterProiIPR032281. 40S_SA_C.
IPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF16122. 40S_SA_C. 1 hit.
PF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. uS2_euk_arch. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "N-terminome analysis of the human mitochondrial proteome."
    Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.
    Proteomics 15:2519-2524(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiC9J9K3_HUMAN
AccessioniPrimary (citable) accession number: C9J9K3
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: February 17, 2016
Last modified: May 11, 2016
This is version 50 of the entry and version 7 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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 one 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.