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P09132 (SRP19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal recognition particle 19 kDa protein

Short name=SRP19
Gene names
Name:SRP19
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length144 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.

Subunit structure

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

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the SRP19 family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P09132-1)

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.
Isoform 2 (identifier: P09132-2)

The sequence of this isoform differs from the canonical sequence as follows:
     101-144: RKSVMLYAAEMIPKLKTRTQKTGGADQSLQQGEGSKKGKGKKKK → HYTLSLTSGS
Note: No experimental confirmation available.
Isoform 3 (identifier: P09132-3)

The sequence of this isoform differs from the canonical sequence as follows:
     15-144: FICIYPAYLN...SKKGKGKKKK → LLKILQLQRF...ALYSSHHVSQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 144144Signal recognition particle 19 kDa protein
PRO_0000135197

Regions

Region136 – 1449Basic region, potentially involved in RNA-binding

Natural variations

Alternative sequence15 – 144130FICIY…GKKKK → LLKILQLQRFKMYVQQLDLT YFLRKIKCTLENGIVMSNTE AESGSSSNRKMGASALYSSH HVSQ in isoform 3.
VSP_044524
Alternative sequence101 – 14444RKSVM…GKKKK → HYTLSLTSGS in isoform 2.
VSP_042540
Natural variant41A → T. Ref.6
Corresponds to variant rs17855423 [ dbSNP | Ensembl ].
VAR_027800

Secondary structure

............................. 144
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 3, 2006. Version 3.
Checksum: E25F661972338CAE

FASTA14416,156
        10         20         30         40         50         60 
MACAAARSPA DQDRFICIYP AYLNNKKTIA EGRRIPISKA VENPTATEIQ DVCSAVGLNV 

        70         80         90        100        110        120 
FLEKNKMYSR EWNRDVQYRG RVRVQLKQED GSLCLVQFPS RKSVMLYAAE MIPKLKTRTQ 

       130        140 
KTGGADQSLQ QGEGSKKGKG KKKK 

« Hide

Isoform 2 [UniParc].

Checksum: F199656A14C743E1
Show »

FASTA11012,400
Isoform 3 [UniParc].

Checksum: 55C1707F8C5C2AE0
Show »

FASTA788,739

References

« Hide 'large scale' references
[1]"Isolation and characterization of a cDNA clone encoding the 19 kDa protein of signal recognition particle (SRP): expression and binding to 7SL RNA."
Lingelbach K., Zwieb C., Webb J.R., Marshallsaz C., Hoben P., Walter P., Dobberstein B.
Nucleic Acids Res. 16:9431-9442(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Gene expression in human erythroid precursor cells."
Gubin A.N., Lee Y.T., Bouffard G.G., Miller J.L.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Erythroblast.
[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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Testis.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2), VARIANT THR-4.
Tissue: Brain and Skin.
[7]"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].
[8]"Crystal structure of an early protein-RNA assembly complex of the signal recognition particle."
Wild K., Sinning I., Cusack S.
Science 294:598-601(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-128.
[9]"Induced structural changes of 7SL RNA during the assembly of human signal recognition particle."
Kuglstatter A., Oubridge C., Nagai K.
Nat. Struct. Biol. 9:740-744(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 14-120 IN COMPLEX WITH SRP54 AND 7SL RNA.
[10]"Structural insights into the assembly of the human and archaeal signal recognition particles."
Wild K., Bange G., Bozkurt G., Segnitz B., Hendricks A., Sinning I.
Acta Crystallogr. D 66:295-303(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 1-120 IN COMPLEX WITH 7SL RNA.
+Additional computationally mapped references.

Web resources

Wikipedia

Signal recognition particle entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12791 mRNA. Translation: CAA31280.1.
BU661702 mRNA. No translation available.
AK311803 mRNA. Translation: BAG34746.1.
AC008536 Genomic DNA. No translation available.
AC008575 Genomic DNA. No translation available.
CH471086 Genomic DNA. Translation: EAW48999.1.
CH471086 Genomic DNA. Translation: EAW49000.1.
BC010947 mRNA. Translation: AAH10947.1.
BC017830 mRNA. Translation: AAH17830.1.
CCDSCCDS4108.1. [P09132-1]
CCDS56375.1. [P09132-2]
CCDS56376.1. [P09132-3]
PIRS01700.
RefSeqNP_001191122.1. NM_001204193.1. [P09132-2]
NP_001191123.1. NM_001204194.1.
NP_001191125.1. NM_001204196.1. [P09132-3]
NP_003126.1. NM_003135.2. [P09132-1]
UniGeneHs.637001.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JIDX-ray1.80A1-120[»]
1MFQX-ray3.10B14-120[»]
1RY1electron microscopy12.00B14-120[»]
2J37electron microscopy8.00B14-120[»]
3KTVX-ray3.80B/D1-120[»]
4P3EX-ray3.50B1-120[»]
DisProtDP00570.
ProteinModelPortalP09132.
SMRP09132. Positions 5-118.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112606. 13 interactions.
IntActP09132. 6 interactions.
MINTMINT-247583.
STRING9606.ENSP00000282999.

Protein family/group databases

TCDB3.A.5.9.1. the general secretory pathway (sec) family.

PTM databases

PhosphoSiteP09132.

Polymorphism databases

DMDM115502457.

Proteomic databases

MaxQBP09132.
PaxDbP09132.
PRIDEP09132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282999; ENSP00000282999; ENSG00000153037. [P09132-2]
ENST00000505459; ENSP00000424870; ENSG00000153037. [P09132-1]
ENST00000515463; ENSP00000425562; ENSG00000153037. [P09132-3]
GeneID6728.
KEGGhsa:6728.
UCSCuc003kqb.2. human. [P09132-2]
uc003kqc.3. human. [P09132-1]
uc021yck.1. human. [P09132-3]

Organism-specific databases

CTD6728.
GeneCardsGC05P112196.
HGNCHGNC:11300. SRP19.
HPAHPA029272.
MIM182175. gene.
neXtProtNX_P09132.
PharmGKBPA36124.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265516.
HOGENOMHOG000237221.
HOVERGENHBG059463.
InParanoidP09132.
KOK03105.
OMARWICIYP.
OrthoDBEOG72G199.
PhylomeDBP09132.
TreeFamTF106248.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

BgeeP09132.
CleanExHS_SRP19.
GenevestigatorP09132.

Family and domain databases

Gene3D3.30.56.30. 1 hit.
InterProIPR002778. Signal_recog_particle_SRP19.
[Graphical view]
PANTHERPTHR17453. PTHR17453. 1 hit.
PfamPF01922. SRP19. 1 hit.
[Graphical view]
SUPFAMSSF69695. SSF69695. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSRP19. human.
EvolutionaryTraceP09132.
GenomeRNAi6728.
NextBio26244.
PROP09132.
SOURCESearch...

Entry information

Entry nameSRP19_HUMAN
AccessionPrimary (citable) accession number: P09132
Secondary accession number(s): B2R4E9 expand/collapse secondary AC list , D6RCQ5, Q05D77, Q96FG6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM