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Protein

mRNA export factor

Gene

RAE1

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

Functioni

Binds mRNA. May function in nucleocytoplasmic transport and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton.

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • RNA binding Source: GO_Central
  • ubiquitin binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.
SignaLinkiP78406.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA export factor
Alternative name(s):
Rae1 protein homolog
mRNA-associated protein mrnp 41
Gene namesi
Name:RAE1
Synonyms:MRNP41
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:9828. RAE1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • nuclear envelope Source: GO_Central
  • nuclear pore Source: GO_Central
  • nucleolus Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34182.

Polymorphism and mutation databases

BioMutaiRAE1.
DMDMi3122666.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368mRNA export factorPRO_0000051181Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei229 – 2291PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP78406.
MaxQBiP78406.
PaxDbiP78406.
PeptideAtlasiP78406.
PRIDEiP78406.
TopDownProteomicsiP78406.

PTM databases

iPTMnetiP78406.
PhosphoSiteiP78406.
SwissPalmiP78406.

Expressioni

Gene expression databases

BgeeiP78406.
CleanExiHS_RAE1.
ExpressionAtlasiP78406. baseline and differential.
GenevisibleiP78406. HS.

Organism-specific databases

HPAiHPA018242.
HPA048795.

Interactioni

Subunit structurei

Interacts with NUP98 (PubMed:20498086). Interacts with MYCBP2 (PubMed:22357847).2 Publications

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • ubiquitin binding Source: GO_Central

Protein-protein interaction databases

BioGridi114054. 133 interactions.
DIPiDIP-41063N.
IntActiP78406. 37 interactions.
MINTiMINT-121447.
STRINGi9606.ENSP00000360286.

Structurei

Secondary structure

1
368
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 476Combined sources
Beta strandi52 – 6110Combined sources
Beta strandi64 – 718Combined sources
Beta strandi77 – 848Combined sources
Beta strandi89 – 946Combined sources
Beta strandi98 – 1058Combined sources
Beta strandi108 – 1147Combined sources
Turni115 – 1184Combined sources
Beta strandi119 – 1257Combined sources
Beta strandi130 – 1378Combined sources
Beta strandi142 – 1487Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi164 – 1685Combined sources
Beta strandi173 – 1797Combined sources
Beta strandi182 – 1876Combined sources
Helixi188 – 1903Combined sources
Beta strandi192 – 1965Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi202 – 2065Combined sources
Beta strandi215 – 2228Combined sources
Beta strandi228 – 2358Combined sources
Beta strandi238 – 2469Combined sources
Helixi250 – 2534Combined sources
Beta strandi254 – 2585Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi264 – 2663Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi276 – 2816Combined sources
Turni283 – 2853Combined sources
Beta strandi288 – 2925Combined sources
Beta strandi297 – 3015Combined sources
Turni302 – 3054Combined sources
Beta strandi306 – 3105Combined sources
Beta strandi318 – 3236Combined sources
Beta strandi330 – 3345Combined sources
Helixi342 – 3443Combined sources
Beta strandi352 – 3565Combined sources
Turni359 – 3624Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MMYX-ray1.65A/C/E/G1-368[»]
4OWRX-ray3.15A31-368[»]
ProteinModelPortaliP78406.
SMRiP78406. Positions 8-365.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78406.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati37 – 7943WD 1PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati84 – 11431WD 2PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati125 – 15733WD 3PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati168 – 20639WD 4PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati215 – 25541WD 5PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati271 – 30131WD 6PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati310 – 34637WD 7PROSITE-ProRule annotation1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat rae1 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0647. Eukaryota.
ENOG410XQ1M. LUCA.
GeneTreeiENSGT00530000063440.
HOVERGENiHBG002942.
InParanoidiP78406.
KOiK14298.
OrthoDBiEOG7H792F.
PhylomeDBiP78406.
TreeFamiTF105481.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 2 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P78406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLFGTTSGF GTSGTSMFGS ATTDNHNPMK DIEVTSSPDD SIGCLSFSPP
60 70 80 90 100
TLPGNFLIAG SWANDVRCWE VQDSGQTIPK AQQMHTGPVL DVCWSDDGSK
110 120 130 140 150
VFTASCDKTA KMWDLSSNQA IQIAQHDAPV KTIHWIKAPN YSCVMTGSWD
160 170 180 190 200
KTLKFWDTRS SNPMMVLQLP ERCYCADVIY PMAVVATAER GLIVYQLENQ
210 220 230 240 250
PSEFRRIESP LKHQHRCVAI FKDKQNKPTG FALGSIEGRV AIHYINPPNP
260 270 280 290 300
AKDNFTFKCH RSNGTNTSAP QDIYAVNGIA FHPVHGTLAT VGSDGRFSFW
310 320 330 340 350
DKDARTKLKT SEQLDQPISA CCFNHNGNIF AYASSYDWSK GHEFYNPQKK
360
NYIFLRNAAE ELKPRNKK
Length:368
Mass (Da):40,968
Last modified:May 1, 1997 - v1
Checksum:i89A99C34BA668A97
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101F → L in AAC28127 (PubMed:9256445).Curated
Sequence conflicti31 – 311D → G in AAC28127 (PubMed:9256445).Curated
Sequence conflicti56 – 561F → S in AAC28127 (PubMed:9256445).Curated
Sequence conflicti120 – 1201A → V in AAR04856 (Ref. 3) Curated
Sequence conflicti158 – 1581T → N in AAC28127 (PubMed:9256445).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84720 mRNA. Translation: AAC28126.1.
U85943 mRNA. Translation: AAC28127.1.
AY349350 mRNA. Translation: AAR04856.1.
AK292247 mRNA. Translation: BAF84936.1.
AL135939 Genomic DNA. Translation: CAI21524.1.
AL109955, AL135939 Genomic DNA. Translation: CAX15041.1.
CH471077 Genomic DNA. Translation: EAW75523.1.
CH471077 Genomic DNA. Translation: EAW75524.1.
CH471077 Genomic DNA. Translation: EAW75525.1.
BC103754 mRNA. Translation: AAI03755.1.
BC106924 mRNA. Translation: AAI06925.1.
BC106923 mRNA. Translation: AAI06924.1.
CCDSiCCDS13458.1.
RefSeqiNP_001015885.1. NM_001015885.1.
NP_003601.1. NM_003610.3.
XP_005260639.2. XM_005260582.2.
XP_011527390.1. XM_011529088.1.
XP_011527391.1. XM_011529089.1.
UniGeneiHs.371698.

Genome annotation databases

EnsembliENST00000371242; ENSP00000360286; ENSG00000101146.
ENST00000395840; ENSP00000379181; ENSG00000101146.
ENST00000395841; ENSP00000379182; ENSG00000101146.
GeneIDi8480.
KEGGihsa:8480.
UCSCiuc002xyg.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84720 mRNA. Translation: AAC28126.1.
U85943 mRNA. Translation: AAC28127.1.
AY349350 mRNA. Translation: AAR04856.1.
AK292247 mRNA. Translation: BAF84936.1.
AL135939 Genomic DNA. Translation: CAI21524.1.
AL109955, AL135939 Genomic DNA. Translation: CAX15041.1.
CH471077 Genomic DNA. Translation: EAW75523.1.
CH471077 Genomic DNA. Translation: EAW75524.1.
CH471077 Genomic DNA. Translation: EAW75525.1.
BC103754 mRNA. Translation: AAI03755.1.
BC106924 mRNA. Translation: AAI06925.1.
BC106923 mRNA. Translation: AAI06924.1.
CCDSiCCDS13458.1.
RefSeqiNP_001015885.1. NM_001015885.1.
NP_003601.1. NM_003610.3.
XP_005260639.2. XM_005260582.2.
XP_011527390.1. XM_011529088.1.
XP_011527391.1. XM_011529089.1.
UniGeneiHs.371698.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MMYX-ray1.65A/C/E/G1-368[»]
4OWRX-ray3.15A31-368[»]
ProteinModelPortaliP78406.
SMRiP78406. Positions 8-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114054. 133 interactions.
DIPiDIP-41063N.
IntActiP78406. 37 interactions.
MINTiMINT-121447.
STRINGi9606.ENSP00000360286.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiP78406.
PhosphoSiteiP78406.
SwissPalmiP78406.

Polymorphism and mutation databases

BioMutaiRAE1.
DMDMi3122666.

Proteomic databases

EPDiP78406.
MaxQBiP78406.
PaxDbiP78406.
PeptideAtlasiP78406.
PRIDEiP78406.
TopDownProteomicsiP78406.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371242; ENSP00000360286; ENSG00000101146.
ENST00000395840; ENSP00000379181; ENSG00000101146.
ENST00000395841; ENSP00000379182; ENSG00000101146.
GeneIDi8480.
KEGGihsa:8480.
UCSCiuc002xyg.4. human.

Organism-specific databases

CTDi8480.
GeneCardsiRAE1.
HGNCiHGNC:9828. RAE1.
HPAiHPA018242.
HPA048795.
MIMi603343. gene.
neXtProtiNX_P78406.
PharmGKBiPA34182.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0647. Eukaryota.
ENOG410XQ1M. LUCA.
GeneTreeiENSGT00530000063440.
HOVERGENiHBG002942.
InParanoidiP78406.
KOiK14298.
OrthoDBiEOG7H792F.
PhylomeDBiP78406.
TreeFamiTF105481.

Enzyme and pathway databases

ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.
SignaLinkiP78406.

Miscellaneous databases

EvolutionaryTraceiP78406.
GeneWikiiRAE1.
GenomeRNAii8480.
PROiP78406.
SOURCEiSearch...

Gene expression databases

BgeeiP78406.
CleanExiHS_RAE1.
ExpressionAtlasiP78406. baseline and differential.
GenevisibleiP78406. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 2 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of poly(A)+ RNA."
    Bharathi A., Ghosh A., Whalen W.A., Yoon J.H., Pu R., Dasso M., Dhar R.
    Gene 198:251-258(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary carcinoma.
  2. "mRNA binding protein mrnp 41 localizes to both nucleus and cytoplasm."
    Kraemer D.M., Blobel G.
    Proc. Natl. Acad. Sci. U.S.A. 94:9119-9124(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  3. Lu L., Huang X.Y., Xu M., Yin L.L., Li J.M., Zhou Z.M., Sha J.H.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  4. "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].
    Tissue: Testis.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Uterus.
  8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1."
    Ren Y., Seo H.S., Blobel G., Hoelz A.
    Proc. Natl. Acad. Sci. U.S.A. 107:10406-10411(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NUP98, WD REPEATS.
  12. "RAE-1, a novel PHR binding protein, is required for axon termination and synapse formation in Caenorhabditis elegans."
    Grill B., Chen L., Tulgren E.D., Baker S.T., Bienvenut W., Anderson M., Quadroni M., Jin Y., Garner C.C.
    J. Neurosci. 32:2628-2636(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYCBP2.

Entry informationi

Entry nameiRAE1L_HUMAN
AccessioniPrimary (citable) accession number: P78406
Secondary accession number(s): A8K882
, O15306, Q3SYL7, Q5TCH8, Q6V708, Q9H100, Q9NQM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: July 6, 2016
This is version 159 of the entry and version 1 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 20
    Human chromosome 20: 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

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.