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O76094

- SRP72_HUMAN

UniProt

O76094 - SRP72_HUMAN

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Protein

Signal recognition particle subunit SRP72

Gene
SRP72
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function.

GO - Molecular functioni

  1. 7S RNA binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. signal recognition particle binding Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. response to drug Source: UniProtKB
  4. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  5. translation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.

Protein family/group databases

TCDBi3.A.5.9.1. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle subunit SRP72
Short name:
SRP72
Alternative name(s):
Signal recognition particle 72 kDa protein
Gene namesi
Name:SRP72
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:11303. SRP72.

Subcellular locationi

Cytoplasm. Endoplasmic reticulum 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endoplasmic reticulum Source: UniProtKB
  3. signal recognition particle, endoplasmic reticulum targeting Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Signal recognition particle

Pathology & Biotechi

Involvement in diseasei

Bone marrow failure syndrome 1 (BMFS1) [MIM:614675]: An autosomal dominant disease characterized by aplastic anemia and myelodysplasia resulting from bone marrow failure. Aplastic anemia is a form of anemia in which the bone marrow fails to produce adequate numbers of peripheral blood elements. Myelodysplasia is a clonal hematopoietic stem cell disorder in which immature cells in the bone marrow become malformed and dysfunctional.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071R → H in BMFS1; affects protein localization to ER. 1 Publication
VAR_068522

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614675. phenotype.
Orphaneti314399. Autosomal dominant aplasia and myelodysplasia.
PharmGKBiPA36127.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 671670Signal recognition particle subunit SRP72PRO_0000135234Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei571 – 5711Phosphothreonine1 Publication
Modified residuei618 – 6181Phosphothreonine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO76094.
PaxDbiO76094.
PeptideAtlasiO76094.
PRIDEiO76094.

PTM databases

PhosphoSiteiO76094.

Expressioni

Gene expression databases

ArrayExpressiO76094.
BgeeiO76094.
CleanExiHS_SRP72.
GenevestigatoriO76094.

Organism-specific databases

HPAiHPA034621.

Interactioni

Subunit structurei

Signal recognition particle consists of a 7S RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9.

Protein-protein interaction databases

BioGridi112609. 18 interactions.
IntActiO76094. 8 interactions.
MINTiMINT-1197309.
STRINGi9606.ENSP00000342181.

Structurei

3D structure databases

ProteinModelPortaliO76094.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati11 – 4434TPR 1Add
BLAST
Repeati109 – 14234TPR 2Add
BLAST
Repeati226 – 25934TPR 3Add
BLAST
Repeati406 – 43934TPR 4Add
BLAST
Repeati447 – 48034TPR 5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi552 – 56110Poly-Lys
Compositional biasi662 – 6654Poly-Lys

Domaini

The C-terminus is essential for the interaction with the SRP68/7S RNA complex By similarity.

Sequence similaritiesi

Belongs to the SRP72 family.
Contains 5 TPR repeats.

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiNOG263236.
HOGENOMiHOG000006745.
HOVERGENiHBG059920.
InParanoidiO76094.
KOiK03108.
OMAiIGQGQLS.
OrthoDBiEOG7RFTH7.
PhylomeDBiO76094.
TreeFamiTF106250.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR013699. Signal_recog_part_SRP72_RNA-bd.
IPR026270. SRP72.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR14094. PTHR14094. 1 hit.
PfamiPF08492. SRP72. 1 hit.
PF00515. TPR_1. 1 hit.
PF13174. TPR_6. 1 hit.
[Graphical view]
PIRSFiPIRSF038922. SRP72. 1 hit.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 3 hits.
[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. Align

Isoform 1 (identifier: O76094-1) [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

MASGGSGGVS VPALWSEVNR YGQNGDFTRA LKTVNKILQI NKDDVTALHC    50
KVVCLIQNGS FKEALNVINT HTKVLANNSL SFEKAYCEYR LNRIENALKT 100
IESANQQTDK LKELYGQVLY RLERYDECLA VYRDLVRNSQ DDYDEERKTN 150
LSAVVAAQSN WEKVVPENLG LQEGTHELCY NTACALIGQG QLNQAMKILQ 200
KAEDLCRRSL SEDTDGTEED PQAELAIIHG QMAYILQLQG RTEEALQLYN 250
QIIKLKPTDV GLLAVIANNI ITINKDQNVF DSKKKVKLTN AEGVEFKLSK 300
KQLQAIEFNK ALLAMYTNQA EQCRKISASL QSQSPEHLLP VLIQAAQLCR 350
EKQHTKAIEL LQEFSDQHPE NAAEIKLTMA QLKISQGNIS KACLILRSIE 400
ELKHKPGMVS ALVTMYSHEE DIDSAIEVFT QAIQWYQNHQ PKSPAHLSLI 450
REAANFKLKY GRKKEAISDL QQLWKQNPKD IHTLAQLISA YSLVDPEKAK 500
ALSKHLPSSD SMSLKVDVEA LENSAGATYI RKKGGKVTGD SQPKEQGQGD 550
LKKKKKKKKG KLPKNYDPKV TPDPERWLPM RERSYYRGRK KGKKKDQIGK 600
GTQGATAGAS SELDASKTVS SPPTSPRPGS AATVSASTSN IIPPRHQKPA 650
GAPATKKKQQ QKKKKGGKGG W 671
Length:671
Mass (Da):74,606
Last modified:January 23, 2007 - v3
Checksum:iCC0BA17AC52E3613
GO
Isoform 2 (identifier: O76094-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     215-275: Missing.

Note: No experimental confirmation available.

Show »
Length:610
Mass (Da):67,879
Checksum:i6351C7451A38ECEC
GO

Sequence cautioni

The sequence CAD97950.1 differs from that shown. Reason: Frameshift at position 565.
The sequence CAD97950.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071R → H in BMFS1; affects protein localization to ER. 1 Publication
VAR_068522

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei215 – 27561Missing in isoform 2. VSP_045576Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231Q → R in CAD97950. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077019 mRNA. Translation: AAC27324.1.
AF069765 mRNA. Translation: AAC97490.1.
BX537991 mRNA. Translation: CAD97950.1. Sequence problems.
AC114766 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05498.1.
CCDSiCCDS3506.1. [O76094-1]
CCDS58898.1. [O76094-2]
RefSeqiNP_001254651.1. NM_001267722.1. [O76094-2]
NP_008878.3. NM_006947.3. [O76094-1]
UniGeneiHs.237825.

Genome annotation databases

EnsembliENST00000342756; ENSP00000342181; ENSG00000174780. [O76094-1]
ENST00000510663; ENSP00000424576; ENSG00000174780. [O76094-2]
GeneIDi6731.
KEGGihsa:6731.
UCSCiuc003hbv.3. human. [O76094-1]
uc010ihe.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Signal recognition particle entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077019 mRNA. Translation: AAC27324.1 .
AF069765 mRNA. Translation: AAC97490.1 .
BX537991 mRNA. Translation: CAD97950.1 . Sequence problems.
AC114766 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05498.1 .
CCDSi CCDS3506.1. [O76094-1 ]
CCDS58898.1. [O76094-2 ]
RefSeqi NP_001254651.1. NM_001267722.1. [O76094-2 ]
NP_008878.3. NM_006947.3. [O76094-1 ]
UniGenei Hs.237825.

3D structure databases

ProteinModelPortali O76094.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112609. 18 interactions.
IntActi O76094. 8 interactions.
MINTi MINT-1197309.
STRINGi 9606.ENSP00000342181.

Protein family/group databases

TCDBi 3.A.5.9.1. the general secretory pathway (sec) family.

PTM databases

PhosphoSitei O76094.

Proteomic databases

MaxQBi O76094.
PaxDbi O76094.
PeptideAtlasi O76094.
PRIDEi O76094.

Protocols and materials databases

DNASUi 6731.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000342756 ; ENSP00000342181 ; ENSG00000174780 . [O76094-1 ]
ENST00000510663 ; ENSP00000424576 ; ENSG00000174780 . [O76094-2 ]
GeneIDi 6731.
KEGGi hsa:6731.
UCSCi uc003hbv.3. human. [O76094-1 ]
uc010ihe.3. human.

Organism-specific databases

CTDi 6731.
GeneCardsi GC04P057334.
HGNCi HGNC:11303. SRP72.
HPAi HPA034621.
MIMi 602122. gene.
614675. phenotype.
neXtProti NX_O76094.
Orphaneti 314399. Autosomal dominant aplasia and myelodysplasia.
PharmGKBi PA36127.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG263236.
HOGENOMi HOG000006745.
HOVERGENi HBG059920.
InParanoidi O76094.
KOi K03108.
OMAi IGQGQLS.
OrthoDBi EOG7RFTH7.
PhylomeDBi O76094.
TreeFami TF106250.

Enzyme and pathway databases

Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.

Miscellaneous databases

ChiTaRSi SRP72. human.
GenomeRNAii 6731.
NextBioi 26258.
PROi O76094.
SOURCEi Search...

Gene expression databases

ArrayExpressi O76094.
Bgeei O76094.
CleanExi HS_SRP72.
Genevestigatori O76094.

Family and domain databases

Gene3Di 1.25.40.10. 4 hits.
InterProi IPR013699. Signal_recog_part_SRP72_RNA-bd.
IPR026270. SRP72.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view ]
PANTHERi PTHR14094. PTHR14094. 1 hit.
Pfami PF08492. SRP72. 1 hit.
PF00515. TPR_1. 1 hit.
PF13174. TPR_6. 1 hit.
[Graphical view ]
PIRSFi PIRSF038922. SRP72. 1 hit.
PROSITEi PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Protein SRP72 sequence of human signal recognition particle."
    Gowda K., Zwieb C.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Sequence of human signal recognition particle (SRP) 72."
    Utz P.J., Hottelet M., Miller I.J., Anderson P.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Esophageal carcinoma.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-20; 63-84; 113-121; 148-163; 242-275; 288-297; 302-324; 326-350; 357-376; 465-475; 480-498; 516-531 AND 601-617, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Exome sequencing identifies autosomal-dominant SRP72 mutations associated with familial aplasia and myelodysplasia."
    Kirwan M., Walne A.J., Plagnol V., Velangi M., Ho A., Hossain U., Vulliamy T., Dokal I.
    Am. J. Hum. Genet. 90:888-892(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BMFS1 HIS-207, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT BMFS1 HIS-207.

Entry informationi

Entry nameiSRP72_HUMAN
AccessioniPrimary (citable) accession number: O76094
Secondary accession number(s): G5E9Z8, Q7Z3C0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 124 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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