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Protein

Signal recognition particle subunit SRP68

Gene

SRP68

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. 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

  • 7S RNA binding Source: InterPro
  • endoplasmic reticulum signal peptide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • signal recognition particle binding Source: UniProtKB
  • signal sequence binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

RNA-binding

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 SRP68
Short name:
SRP68
Alternative name(s):
Signal recognition particle 68 kDa protein
Gene namesi
Name:SRP68
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:11302. SRP68.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: ProtInc
  • focal adhesion Source: HPA
  • nucleolus Source: ProtInc
  • ribosome Source: ProtInc
  • signal recognition particle, endoplasmic reticulum targeting Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Signal recognition particle

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36126.

Polymorphism and mutation databases

BioMutaiSRP68.
DMDMi37154869.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 627627Signal recognition particle subunit SRP68PRO_0000135227Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphoserine1 Publication
Modified residuei452 – 4521N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UHB9.
PaxDbiQ9UHB9.
PeptideAtlasiQ9UHB9.
PRIDEiQ9UHB9.

PTM databases

PhosphoSiteiQ9UHB9.

Expressioni

Gene expression databases

BgeeiQ9UHB9.
CleanExiHS_SRP68.
ExpressionAtlasiQ9UHB9. baseline and differential.
GenevisibleiQ9UHB9. HS.

Organism-specific databases

HPAiHPA023303.
HPA055617.

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

BioGridi112608. 47 interactions.
DIPiDIP-50905N.
IntActiQ9UHB9. 6 interactions.
MINTiMINT-3080223.
STRINGi9606.ENSP00000312066.

Structurei

Secondary structure

1
627
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi62 – 7211Combined sources
Helixi75 – 773Combined sources
Helixi80 – 10324Combined sources
Turni104 – 1063Combined sources
Beta strandi119 – 1213Combined sources
Helixi122 – 14322Combined sources
Turni145 – 1473Combined sources
Helixi151 – 17222Combined sources
Helixi180 – 20021Combined sources
Helixi204 – 22219Combined sources
Helixi227 – 25125Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P3EX-ray3.50C47-254[»]
4P3FX-ray1.70A/B47-254[»]
ProteinModelPortaliQ9UHB9.
SMRiQ9UHB9. Positions 55-252.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 2416Poly-GlyAdd
BLAST

Domaini

The RNA-binding domain is located near the N-terminus.

Sequence similaritiesi

Belongs to the SRP68 family.Curated

Phylogenomic databases

eggNOGiNOG325632.
GeneTreeiENSGT00390000011856.
HOGENOMiHOG000231195.
HOVERGENiHBG059793.
InParanoidiQ9UHB9.
KOiK03107.
OMAiFPITNAK.
OrthoDBiEOG7C5M7W.
PhylomeDBiQ9UHB9.
TreeFamiTF105779.

Family and domain databases

InterProiIPR026258. SRP68.
[Graphical view]
PIRSFiPIRSF038995. SRP68. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UHB9-1) [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
MAAEKQVPGG GGGGGSGGGG GSGGGGSGGG RGAGGEENKE NERPSAGSKA
60 70 80 90 100
NKEFGDSLSL EILQIIKESQ QQHGLRHGDF QRYRGYCSRR QRRLRKTLNF
110 120 130 140 150
KMGNRHKFTG KKVTEELLTD NRYLLLVLMD AERAWSYAMQ LKQEANTEPR
160 170 180 190 200
KRFHLLSRLR KAVKHAEELE RLCESNRVDA KTKLEAQAYT AYLSGMLRFE
210 220 230 240 250
HQEWKAAIEA FNKCKTIYEK LASAFTEEQA VLYNQRVEEI SPNIRYCAYN
260 270 280 290 300
IGDQSAINEL MQMRLRSGGT EGLLAEKLEA LITQTRAKQA ATMSEVEWRG
310 320 330 340 350
RTVPVKIDKV RIFLLGLADN EAAIVQAESE ETKERLFESM LSECRDAIQV
360 370 380 390 400
VREELKPDQK QRDYILEGEP GKVSNLQYLH SYLTYIKLST AIKRNENMAK
410 420 430 440 450
GLQRALLQQQ PEDDSKRSPR PQDLIRLYDI ILQNLVELLQ LPGLEEDKAF
460 470 480 490 500
QKEIGLKTLV FKAYRCFFIA QSYVLVKKWS EALVLYDRVL KYANEVNSDA
510 520 530 540 550
GAFKNSLKDL PDVQELITQV RSEKCSLQAA AILDANDAHQ TETSSSQVKD
560 570 580 590 600
NKPLVERFET FCLDPSLVTK QANLVHFPPG FQPIPCKPLF FDLALNHVAF
610 620
PPLEDKLEQK TKSGLTGYIK GIFGFRS
Length:627
Mass (Da):70,730
Last modified:September 26, 2003 - v2
Checksum:i6EF582892D300B2D
GO
Isoform 2 (identifier: Q9UHB9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     256-286: Missing.

Note: No experimental confirmation available.
Show »
Length:596
Mass (Da):67,304
Checksum:i025BF536B2452299
GO
Isoform 3 (identifier: Q9UHB9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-339: Missing.

Show »
Length:288
Mass (Da):32,851
Checksum:iFF3915ED8952AE0D
GO
Isoform 4 (identifier: Q9UHB9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     84-121: Missing.

Note: No experimental confirmation available.
Show »
Length:589
Mass (Da):66,108
Checksum:iC8F8D0CB68D9C34D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 195Missing in AAF24308 (PubMed:10618370).Curated
Sequence conflicti27 – 293Missing in AAF24308 (PubMed:10618370).Curated
Sequence conflicti174 – 1741E → K in AAF24308 (PubMed:10618370).Curated
Sequence conflicti534 – 5352DA → ES in AAF24308 (PubMed:10618370).Curated
Sequence conflicti606 – 6061K → E in BAG54299 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 339339Missing in isoform 3. 1 PublicationVSP_045132Add
BLAST
Alternative sequencei84 – 12138Missing in isoform 4. 1 PublicationVSP_046944Add
BLAST
Alternative sequencei256 – 28631Missing in isoform 2. 1 PublicationVSP_008347Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195951 mRNA. Translation: AAF24308.1.
AK074698 mRNA. Translation: BAC11145.1.
AK097962 mRNA. Translation: BAG53557.1.
AK126258 mRNA. Translation: BAG54299.1.
AC040980 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89360.1.
CH471099 Genomic DNA. Translation: EAW89362.1.
BC020238 mRNA. Translation: AAH20238.1.
CCDSiCCDS11738.1. [Q9UHB9-1]
CCDS58600.1. [Q9UHB9-3]
CCDS58601.1. [Q9UHB9-4]
RefSeqiNP_001247431.1. NM_001260502.1. [Q9UHB9-4]
NP_001247432.1. NM_001260503.1. [Q9UHB9-3]
NP_055045.2. NM_014230.3. [Q9UHB9-1]
UniGeneiHs.514495.

Genome annotation databases

EnsembliENST00000307877; ENSP00000312066; ENSG00000167881.
ENST00000539137; ENSP00000446136; ENSG00000167881. [Q9UHB9-4]
ENST00000602720; ENSP00000473613; ENSG00000167881. [Q9UHB9-3]
GeneIDi6730.
KEGGihsa:6730.
UCSCiuc002jqj.2. human.
uc002jqk.2. human. [Q9UHB9-1]
uc002jql.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Signal recognition particle entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195951 mRNA. Translation: AAF24308.1.
AK074698 mRNA. Translation: BAC11145.1.
AK097962 mRNA. Translation: BAG53557.1.
AK126258 mRNA. Translation: BAG54299.1.
AC040980 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89360.1.
CH471099 Genomic DNA. Translation: EAW89362.1.
BC020238 mRNA. Translation: AAH20238.1.
CCDSiCCDS11738.1. [Q9UHB9-1]
CCDS58600.1. [Q9UHB9-3]
CCDS58601.1. [Q9UHB9-4]
RefSeqiNP_001247431.1. NM_001260502.1. [Q9UHB9-4]
NP_001247432.1. NM_001260503.1. [Q9UHB9-3]
NP_055045.2. NM_014230.3. [Q9UHB9-1]
UniGeneiHs.514495.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P3EX-ray3.50C47-254[»]
4P3FX-ray1.70A/B47-254[»]
ProteinModelPortaliQ9UHB9.
SMRiQ9UHB9. Positions 55-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112608. 47 interactions.
DIPiDIP-50905N.
IntActiQ9UHB9. 6 interactions.
MINTiMINT-3080223.
STRINGi9606.ENSP00000312066.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ9UHB9.

Polymorphism and mutation databases

BioMutaiSRP68.
DMDMi37154869.

Proteomic databases

MaxQBiQ9UHB9.
PaxDbiQ9UHB9.
PeptideAtlasiQ9UHB9.
PRIDEiQ9UHB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307877; ENSP00000312066; ENSG00000167881.
ENST00000539137; ENSP00000446136; ENSG00000167881. [Q9UHB9-4]
ENST00000602720; ENSP00000473613; ENSG00000167881. [Q9UHB9-3]
GeneIDi6730.
KEGGihsa:6730.
UCSCiuc002jqj.2. human.
uc002jqk.2. human. [Q9UHB9-1]
uc002jql.2. human.

Organism-specific databases

CTDi6730.
GeneCardsiGC17M074035.
HGNCiHGNC:11302. SRP68.
HPAiHPA023303.
HPA055617.
MIMi604858. gene.
neXtProtiNX_Q9UHB9.
PharmGKBiPA36126.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG325632.
GeneTreeiENSGT00390000011856.
HOGENOMiHOG000231195.
HOVERGENiHBG059793.
InParanoidiQ9UHB9.
KOiK03107.
OMAiFPITNAK.
OrthoDBiEOG7C5M7W.
PhylomeDBiQ9UHB9.
TreeFamiTF105779.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.

Miscellaneous databases

ChiTaRSiSRP68. human.
GenomeRNAii6730.
NextBioi26254.
PROiQ9UHB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UHB9.
CleanExiHS_SRP68.
ExpressionAtlasiQ9UHB9. baseline and differential.
GenevisibleiQ9UHB9. HS.

Family and domain databases

InterProiIPR026258. SRP68.
[Graphical view]
PIRSFiPIRSF038995. SRP68. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Tissue: Liver, Mammary gland and Thymus.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Skin.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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].
    Tissue: Liver.

Entry informationi

Entry nameiSRP68_HUMAN
AccessioniPrimary (citable) accession number: Q9UHB9
Secondary accession number(s): B3KUU5
, B3KWY7, G3V1U4, Q8NCJ4, Q8WUK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: September 26, 2003
Last modified: July 22, 2015
This is version 129 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.