P62979 (RS27A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-40S ribosomal protein S27a

Alternative name(s):
Ubiquitin carboxyl extension protein 80

Cleaved into the following 2 chains:

1. Ubiquitin
2. 40S ribosomal protein S27a

Gene names

Name:	RPS27A
Synonyms:	UBA80, UBCEP1

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	156 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	Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. Ref.12 Ref.16 Ribosomal protein S27a is a component of the 40S subunit of the ribosome. Ref.12 Ref.16
Subunit structure	Ribosomal protein S27a is part of the 40S ribosomal subunit By similarity.
Subcellular location	Ubiquitin: Cytoplasm By similarity. Nucleus By similarity.
Miscellaneous	Ubiquitin is encoded by 4 different genes. UBA52 and RPS27A genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively. UBB and UBC genes code for a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains. For a better understanding, features related to ubiquitin are only indicated for the first chain.
Sequence similarities	In the N-terminal section; belongs to the ubiquitin family. In the C-terminal section; belongs to the ribosomal protein S27Ae family. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Traceable author statement. Source: Reactome DNA repair Traceable author statement. Source: Reactome G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome I-kappaB kinase/NF-kappaB cascade Traceable author statement. Source: Reactome JNK cascade Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Notch receptor processing Traceable author statement. Source: Reactome Notch signaling pathway Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome SRP-dependent cotranslational protein targeting to membrane Traceable author statement. Source: Reactome T cell receptor signaling pathway Traceable author statement. Source: Reactome TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome activation of MAPK activity Traceable author statement. Source: Reactome anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome cellular membrane organization Traceable author statement. Source: Reactome cytokine-mediated signaling pathway Traceable author statement. Source: Reactome egress of virus within host cell Traceable author statement. Source: Reactome endosomal transport Traceable author statement. Source: Reactome epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome negative regulation of epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome negative regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome negative regulation of transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome negative regulation of type I interferon production Traceable author statement. Source: Reactome negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Traceable author statement. Source: Reactome nucleotide-binding oligomerization domain containing signaling pathway Traceable author statement. Source: Reactome positive regulation of I-kappaB kinase/NF-kappaB cascade Traceable author statement. Source: Reactome positive regulation of NF-kappaB transcription factor activity Traceable author statement. Source: Reactome positive regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein polyubiquitination Traceable author statement. Source: Reactome regulation of apoptotic process Traceable author statement. Source: Reactome regulation of transcription from RNA polymerase II promoter in response to hypoxia Traceable author statement. Source: Reactome toll-like receptor 1 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome translational elongation Traceable author statement. Source: Reactome translational initiation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular_component	cytosolic small ribosomal subunit Inferred from direct assay PubMed 15883184Ref.5. Source: UniProtKB endocytic vesicle membrane Traceable author statement. Source: Reactome endosome membrane Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from direct assay PubMed 15883184. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 76

76

Ubiquitin

PRO_0000396477

Chain

77 – 156

80

40S ribosomal protein S27a

PRO_0000396478

Regions

Domain

1 – 76

76

Ubiquitin-like

Zinc finger

121 – 144

24

C4-type

Compositional bias

77 – 99

23

Lys-rich (highly basic)

Sites

Binding site

54

1

Activating enzyme

Binding site

72

1

Activating enzyme

Site

68

1

Essential for function

Amino acid modifications

Modified residue

57

1

Phosphoserine By similarity

Modified residue

104

1

N6-acetyllysine Ref.17

Modified residue

113

1

N6-acetyllysine Ref.17

Cross-link

6

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Cross-link

11

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8 Ref.12

Cross-link

27

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Cross-link

29

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12

Cross-link

33

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

48

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8 Ref.12 Ref.14

Cross-link

63

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12 Ref.15

Cross-link

76

Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Experimental info

Mutagenesis

48

1

K → R: No effect on HLTF-mediated polyubiquitination of PCNA. Ref.15

Mutagenesis

63

1

K → R: Abolishes HLTF-mediated polyubiquitination of PCNA. Ref.15

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

156

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Beta strand

8 – 10

3

Beta strand

12 – 16

5

Helix

23 – 34

12

Helix

38 – 40

3

Beta strand

42 – 45

4

Helix

57 – 59

3

Beta strand

66 – 70

5

Sequences

	Sequence		Length	Mass (Da)
	P62979 [UniParc]. Last modified August 10, 2010. Version 2. Checksum: 617BC63DF3A904F7	FASTA	156	17,965
	10 20 30 40 50 60 MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 70 80 90 100 110 120 IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL AVLKYYKVDE NGKISRLRRE 130 140 150 CPSDECGAGV FMASHFDRHY CGKCCLTYCF NKPEDK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL)." Pancre V., Pierce R.J., Fournier F., Mehtali M., Delanoye A., Capron A., Auriault C. Eur. J. Immunol. 21:2735-2741(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Differential expression of translation-associated genes in benign and malignant human breast tumours." Adams S.M., Sharp M.G., Walker R.A., Brammar W.J., Varley J.M. Br. J. Cancer 65:65-71(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta and Skin.
[5]	"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry." Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A. Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-98. Tissue: Placenta.
[6]	"Hybrid troponin reconstituted from vertebrate and arthropod subunits." Schlesinger D.H., Goldstein G. Nature 255:423-424(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-74.
[7]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[8]	"Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation." Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J. J. Biol. Chem. 281:10825-10838(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 AND LYS-48, MASS SPECTROMETRY.
[9]	"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes." Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N. Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[10]	"Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor." Lund P.K., Moats-Staats B.M., Simmons J.G., Hoyt E., D'Ercole A.J., Martin F., van Wyk J.J. J. Biol. Chem. 260:7609-7613(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-156.
[11]	"A map of 75 human ribosomal protein genes." Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C. Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-148.
[12]	"Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain." Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A. Mol. Cell 21:737-748(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, MASS SPECTROMETRY.
[13]	"Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis." Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K. J. Biol. Chem. 279:53533-53543(2004) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-27.
[14]	"The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells." Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D. J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, MASS SPECTROMETRY. Tissue: Lung adenocarcinoma.
[15]	"Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks." Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K. Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-63, MUTAGENESIS OF LYS-48 AND LYS-63.
[16]	"The emerging complexity of protein ubiquitination." Komander D. Biochem. Soc. Trans. 37:937-953(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW, FUNCTION.
[17]	"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-104 AND LYS-113, MASS SPECTROMETRY.
[18]	"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

X63237 mRNA. Translation: CAA44911.1.
S79522 mRNA. Translation: AAB21188.1.
AC012358 Genomic DNA. No translation available.
BC001392 mRNA. Translation: AAH01392.1.
BC066293 mRNA. Translation: AAH66293.1.
AB062071 Genomic DNA. Translation: BAB79490.1.
M10939 mRNA. Translation: AAA36788.1.
AB007163 Genomic DNA. Translation: BAA25826.1.

IPI

IPI00179330.

RefSeq

NP_001129064.1. NM_001135592.2.
NP_001170884.1. NM_001177413.1.
NP_002945.1. NM_002954.5.

UniGene

Hs.311640.
Hs.546292.
Hs.708727.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KHW	NMR	-	B	1-76	[»]
2KOX	NMR	-	A	1-76	[»]
2KTF	NMR	-	A	1-76	[»]
2KWU	NMR	-	B	1-76	[»]
2KWV	NMR	-	B	1-76	[»]
2L0F	NMR	-	A	1-76	[»]
2L0T	NMR	-	A	1-76	[»]
2XK5	X-ray	3.00	A/B	1-76	[»]
3AXC	X-ray	2.19	A	1-76	[»]
3K9P	X-ray	2.80	B	1-76	[»]
3N30	X-ray	3.00	A/B	1-76	[»]
3N32	X-ray	1.80	A	1-76	[»]
3NHE	X-ray	1.26	B	1-76	[»]
3NOB	X-ray	2.19	A/B/C/D/E/F/G/H	1-76	[»]
3NS8	X-ray	1.71	A/B	1-76	[»]
3PHD	X-ray	3.00	E/F/G/H	1-76	[»]
3PHW	X-ray	2.00	B/D/F/H	1-75	[»]
3TBL	X-ray	2.90	D/E	1-76	[»]

ProteinModelPortal

P62979.

SMR

P62979. Positions 1-76, 102-150.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62979. 12 interactions.

MINT

MINT-1138719.

STRING

9606.ENSP00000272317.

PTM databases

PhosphoSite

P62979.

Polymorphism databases

DMDM

302393745.

2D gel databases

UCD-2DPAGE

P02248.

Proteomic databases

PaxDb

P62979.

PRIDE

P62979.

Protocols and materials databases

DNASU

6233.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000272317; ENSP00000272317; ENSG00000143947.
ENST00000402285; ENSP00000383981; ENSG00000143947.
ENST00000404735; ENSP00000385659; ENSG00000143947.

GeneID

6233.

KEGG

hsa:6233.

UCSC

uc002ryk.3. human.

Organism-specific databases

CTD

6233.

GeneCards

GC02P055459.

H-InvDB

HIX0161861.

HGNC

HGNC:10417. RPS27A.

HPA

CAB033319.
HPA041344.

MIM

191343. gene.

neXtProt

NX_P62979.

PharmGKB

PA34821.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5272.

HOVERGEN

HBG079148.

InParanoid

P62979.

KO

K02977.

OMA

KKVYTTP.

OrthoDB

EOG4PZJ82.

PhylomeDB

P62979.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.
REACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_115202. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_2001. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
REACT_24941. Circadian Clock.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_71. Gene Expression.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
REACT_81380. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
REACT_97910. Signal Transduction.

Gene expression databases

ArrayExpress

P62979.

Bgee

P62979.

CleanEx

HS_RPS27A.

Genevestigator

P62979.

GermOnline

ENSG00000143947. Homo sapiens.

Family and domain databases

InterPro

IPR002906. Ribosomal_S27a.
IPR000626. Ubiquitin.
IPR019954. Ubiquitin_CS.
IPR019956. Ubiquitin_subgr.
IPR019955. Ubiquitin_supergroup.
[Graphical view]

Pfam

PF01599. Ribosomal_S27. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]

PRINTS

PR00348. UBIQUITIN.

SMART

SM00213. UBQ. 1 hit.
[Graphical view]

PROSITE

PS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RPS27A. human.

EvolutionaryTrace

P62979.

GenomeRNAi

6233.

NextBio

24197.

SOURCE

Search...

Entry information

Entry name

RS27A_HUMAN

Accession

Primary (citable) accession number: P62979
Secondary accession number(s): P02248 , P02249, P02250, P14798, P62988, Q29120, Q6LBL4, Q6LDU5, Q8WYN8, Q91887, Q91888, Q9BQ77, Q9BWD6, Q9BX98, Q9UEF2, Q9UEG1, Q9UEK8, Q9UPK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	August 10, 2010
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 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.