Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7L2H7 (EIF3M_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 3 subunit M

Short name=eIF3m
Alternative name(s):
Fetal lung protein B5
Short name=hFL-B5
PCI domain-containing protein 1
Gene names
Name:EIF3M
Synonyms:HFLB5, PCID1
ORF Names:GA17, PNAS-125
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2). Ref.1 Ref.17

Subunit structure

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Ref.11 Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03012.

Tissue specificity

Broadly expressed. Ref.1

Induction

By glucose deprivation in neuroblastoma cells. Ref.9

Sequence similarities

Belongs to the eIF-3 subunit M family.

Contains 1 PCI domain.

Mass spectrometry

Molecular mass is 42413.8 Da from positions 1 - 374. Ref.18

Molecular mass is 42414.7±0.2 Da from positions 1 - 374. Determined by MALDI. Ref.19

Sequence caution

The sequence AAK07542.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAK07542.1 differs from that shown. Reason: Frameshift at position 371.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ORFQ9Q2G42EBI-353901,EBI-6248094From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.18
Chain2 – 374373Eukaryotic translation initiation factor 3 subunit M HAMAP-Rule MF_03012
PRO_0000308195

Regions

Domain235 – 336102PCI
Region344 – 37431Interaction with HSV-1 and HSV-2 HAMAP-Rule MF_03012

Amino acid modifications

Modified residue21N-acetylserine Ref.8 Ref.18 Ref.20 Ref.23 Ref.24
Modified residue21Phosphoserine Ref.23
Modified residue2541N6-acetyllysine Ref.21

Natural variations

Natural variant371G → R.
Corresponds to variant rs11557143 [ dbSNP | Ensembl ].
VAR_036752
Natural variant801E → G in a breast cancer sample; somatic mutation. Ref.25
VAR_036753
Natural variant3461Q → R. Ref.2
Corresponds to variant rs1802363 [ dbSNP | Ensembl ].
VAR_036754

Experimental info

Mutagenesis3501L → P: Reduces HSV binding and entry. Ref.13
Mutagenesis3541L → P: Reduces HSV binding and entry. Ref.13
Mutagenesis3611L → P: Reduces HSV binding and entry. Ref.13
Mutagenesis3641V → P: Reduces HSV binding and entry. Ref.13
Sequence conflict641M → V in AAC17108. Ref.2
Sequence conflict1211Y → C in ABD14422. Ref.9
Sequence conflict129 – 1313KVA → EVV in AAC17108. Ref.2
Sequence conflict1731V → A in AAC17108. Ref.2
Sequence conflict210 – 2112RA → EP in AAC17108. Ref.2
Sequence conflict2871V → I in AAC17108. Ref.2
Sequence conflict2971M → V in BAD96284. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q7L2H7 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 63736CA2B093D794

FASTA37442,503
        10         20         30         40         50         60 
MSVPAFIDIS EEDQAAELRA YLKSKGAEIS EENSEGGLHV DLAQIIEACD VCLKEDDKDV 

        70         80         90        100        110        120 
ESVMNSVVSL LLILEPDKQE ALIESLCEKL VKFREGERPS LRLQLLSNLF HGMDKNTPVR 

       130        140        150        160        170        180 
YTVYCSLIKV AASCGAIQYI PTELDQVRKW ISDWNLTTEK KHTLLRLLYE ALVDCKKSDA 

       190        200        210        220        230        240 
ASKVMVELLG SYTEDNASQA RVDAHRCIVR ALKDPNAFLF DHLLTLKPVK FLEGELIHDL 

       250        260        270        280        290        300 
LTIFVSAKLA SYVKFYQNNK DFIDSLGLLH EQNMAKMRLL TFMGMAVENK EISFDTMQQE 

       310        320        330        340        350        360 
LQIGADDVEA FVIDAVRTKM VYCKIDQTQR KVVVSHSTHR TFGKQQWQQL YDTLNAWKQN 

       370 
LNKVKNSLLS LSDT 

« Hide

References

« Hide 'large scale' references
[1]"A new class of receptor for herpes simplex virus has heptad repeat motifs that are common to membrane fusion proteins."
Perez A., Li Q.-X., Perez-Romero P., DeLassus G., Lopez S.R., Sutter S., McLaren N., Fuller A.O.
J. Virol. 79:7419-7430(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Fetal lung.
[2]"A novel gene from human dendritic cell."
Zhao Z., Huang X., Li N., Zhu X., Cao X.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-346.
Tissue: Dendritic cell.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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. 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].
Tissue: Synovium and Thalamus.
[5]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Coronary arterial endothelium.
[6]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].
[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: Muscle and Uterus.
[8]Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W., Vousden K.H., Lukashchuk N.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-19; 103-115; 184-201; 261-276 AND 279-290, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma and Lung carcinoma.
[9]"Subtractive hybridisation screen identifies genes regulated by glucose deprivation in human neuroblastoma cells."
Kobayashi K., Xin Y., Ymer S.I., Werther G.A., Russo V.C.
Brain Res. 1170:129-139(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-139, INDUCTION.
[10]"Human acute promyelocytic leukemia cell line NB4's apoptosis/differentiation related genes."
Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-374.
[11]"Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP."
Unbehaun A., Borukhov S.I., Hellen C.U.T., Pestova T.V.
Genes Dev. 18:3078-3093(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes."
Zhou C., Arslan F., Wee S., Krishnan S., Ivanov A.R., Oliva A., Leatherwood J., Wolf D.A.
BMC Biol. 3:14-14(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[13]"The C-terminus of the B5 receptor for herpes simplex virus contains a functional region important for infection."
Perez-Romero P., Fuller A.O.
J. Virol. 79:7431-7437(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-350; LEU-354; LEU-361 AND VAL-364.
[14]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association."
Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.
RNA 11:470-486(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[16]"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit."
LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E.
J. Biol. Chem. 281:22917-22932(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"CIF-1, a shared subunit of the COP9/signalosome and eukaryotic initiation factor 3 complexes, regulates MEL-26 levels in the Caenorhabditis elegans embryo."
Luke-Glaser S., Roy M., Larsen B., Le Bihan T., Metalnikov P., Tyers M., Peter M., Pintard L.
Mol. Cell. Biol. 27:4526-4540(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE EIF-3 COMPLEX.
[18]"Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry."
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.
Mol. Cell. Proteomics 6:1135-1146(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY.
[19]"Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3."
Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., Doudna J.A., Robinson C.V.
Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY, INTERACTION WITH EIF3B; EIF3F AND EIF3H.
[20]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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].
[23]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-80.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY769947 mRNA. Translation: AAX12524.1.
AF064603 mRNA. Translation: AAC17108.1.
CR450300 mRNA. Translation: CAG29296.1.
AK222564 mRNA. Translation: BAD96284.1.
AK292139 mRNA. Translation: BAF84828.1.
AK312512 mRNA. Translation: BAG35413.1.
CH471064 Genomic DNA. Translation: EAW68217.1.
BC019103 mRNA. Translation: AAH19103.1.
BC051292 mRNA. Translation: AAH51292.1.
DQ185042 mRNA. Translation: ABD14422.1.
AF277183 mRNA. Translation: AAK07542.1. Sequence problems.
RefSeqNP_006351.2. NM_006360.4.
UniGeneHs.502244.

3D structure databases

ProteinModelPortalQ7L2H7.
SMRQ7L2H7. Positions 187-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115743. 25 interactions.
DIPDIP-31256N.
IntActQ7L2H7. 12 interactions.
MINTMINT-4915331.
STRING9606.ENSP00000319910.

PTM databases

PhosphoSiteQ7L2H7.

Polymorphism databases

DMDM74754296.

Proteomic databases

PaxDbQ7L2H7.
PeptideAtlasQ7L2H7.
PRIDEQ7L2H7.

Protocols and materials databases

DNASU10480.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000531120; ENSP00000436049; ENSG00000149100.
GeneID10480.
KEGGhsa:10480.
UCSCuc001mtu.4. human.

Organism-specific databases

CTD10480.
GeneCardsGC11P032564.
HGNCHGNC:24460. EIF3M.
HPAHPA031063.
MIM609641. gene.
neXtProtNX_Q7L2H7.
PharmGKBPA162384944.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253821.
HOGENOMHOG000112351.
HOVERGENHBG107844.
InParanoidQ7L2H7.
KOK15030.
OMASSCGAIQ.
PhylomeDBQ7L2H7.
TreeFamTF106148.

Gene expression databases

ArrayExpressQ7L2H7.
BgeeQ7L2H7.
CleanExHS_EIF3M.
GenevestigatorQ7L2H7.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
HAMAPMF_03012. eIF3m.
InterProIPR016024. ARM-type_fold.
IPR027528. eIF3m.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF01399. PCI. 1 hit.
[Graphical view]
SMARTSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

ChiTaRSEIF3M. human.
GeneWikiEIF3M.
GenomeRNAi10480.
NextBio39758.
PROQ7L2H7.
SOURCESearch...

Entry information

Entry nameEIF3M_HUMAN
AccessionPrimary (citable) accession number: Q7L2H7
Secondary accession number(s): A8K7X4 expand/collapse secondary AC list , O60735, Q2F836, Q53HL6, Q9BXW1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 5, 2005
Last modified: April 16, 2014
This is version 88 of the entry and version 1 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

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 11

Human chromosome 11: entries, gene names and cross-references to MIM