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Protein

Probable RNA-binding protein EIF1AD

Gene

EIF1AD

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

Functioni

Plays a role into cellular response to oxidative stress. Decreases cell proliferation.2 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable RNA-binding protein EIF1AD
Alternative name(s):
Eukaryotic translation initiation factor 1A domain-containing protein
Haponin
Gene namesi
Name:EIF1AD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:28147. EIF1AD.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384553.

Polymorphism and mutation databases

BioMutaiEIF1AD.
DMDMi74729733.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 165165Probable RNA-binding protein EIF1ADPRO_0000314151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331PhosphothreonineCombined sources
Modified residuei131 – 1311PhosphoserineBy similarity
Modified residuei135 – 1351PhosphoserineBy similarity
Modified residuei136 – 1361PhosphoserineBy similarity
Modified residuei137 – 1371PhosphoserineBy similarity
Modified residuei155 – 1551PhosphoserineCombined sources
Modified residuei159 – 1591PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N9N8.
MaxQBiQ8N9N8.
PaxDbiQ8N9N8.
PeptideAtlasiQ8N9N8.
PRIDEiQ8N9N8.

PTM databases

iPTMnetiQ8N9N8.
PhosphoSiteiQ8N9N8.

Expressioni

Tissue specificityi

Expressed in the glioblastoma cell line U-87MG, the embryonic kidney cell line HEK293, the pancreatic carcinoma cell line PANC-1, the breast carcinoma cell line MCF-7, the lung cancer cell line NCI-H460, and the chronic myelogenous leukemia cell line K-562.1 Publication

Gene expression databases

BgeeiQ8N9N8.
CleanExiHS_EIF1AD.
ExpressionAtlasiQ8N9N8. baseline and differential.
GenevisibleiQ8N9N8. HS.

Organism-specific databases

HPAiHPA054991.
HPA058735.

Interactioni

Subunit structurei

Interacts with GAPDH and STAT1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BEND7Q8N7W2-23EBI-750700,EBI-10181188
CEP55D3DR373EBI-750700,EBI-10173536
GLYR1Q49A263EBI-750700,EBI-2804292
MEOX2A4D1273EBI-750700,EBI-10172134
SDCBPO005603EBI-750700,EBI-727004
SDCBP2Q9H1904EBI-750700,EBI-742426
STAT1P422244EBI-750700,EBI-1057697
STX11O755583EBI-750700,EBI-714135
TBC1D5B9A6K13EBI-750700,EBI-10217641
ZBTB14O438293EBI-750700,EBI-10176632
ZBTB8AQ96BR93EBI-750700,EBI-742740

Protein-protein interaction databases

BioGridi124012. 16 interactions.
IntActiQ8N9N8. 12 interactions.
MINTiMINT-1479911.
STRINGi9606.ENSP00000309175.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 327Combined sources
Beta strandi35 – 428Combined sources
Beta strandi48 – 525Combined sources
Beta strandi68 – 736Combined sources
Beta strandi82 – 876Combined sources
Helixi90 – 9910Combined sources
Helixi104 – 1107Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DGYNMR-A17-114[»]
ProteinModelPortaliQ8N9N8.
SMRiQ8N9N8. Positions 16-115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N9N8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 8985S1-likePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi6 – 127Nuclear localization signalSequence analysis
Motifi56 – 6510Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi154 – 16310Poly-Glu

Sequence similaritiesi

Belongs to the EIF1AD family.Curated
Contains 1 S1-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2925. Eukaryota.
ENOG4111N6Z. LUCA.
GeneTreeiENSGT00390000011180.
HOGENOMiHOG000007486.
HOVERGENiHBG097893.
InParanoidiQ8N9N8.
KOiK15025.
OMAiVNTNRCN.
OrthoDBiEOG75J0Q8.
PhylomeDBiQ8N9N8.
TreeFamiTF314439.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR001253. TIF_eIF-1A.
[Graphical view]
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
SMARTiSM00652. eIF1a. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8N9N8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQATKRKHV VKEVLGEHIV PSDQQQIVRV LRTPGNNLHE VETAQGQRFL
60 70 80 90 100
VSMPSKYRKN IWIKRGDFLI VDPIEEGEKV KAEISFVLCK DHVRSLQKEG
110 120 130 140 150
FWPEAFSEVA EKHNNRNRQT QPELPAEPQL SGEESSSEDD SDLFVNTNRR
160
QYHESEEESE EEEAA
Length:165
Mass (Da):19,053
Last modified:October 1, 2002 - v1
Checksum:i33FB5ACB777084B2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231D → N.1 Publication
Corresponds to variant rs17849919 [ dbSNP | Ensembl ].
VAR_037851
Natural varianti159 – 1591S → N.
Corresponds to variant rs2276017 [ dbSNP | Ensembl ].
VAR_037852

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK094129 mRNA. Translation: BAC04293.1.
AK311891 mRNA. Translation: BAG34832.1.
CH471076 Genomic DNA. Translation: EAW74478.1.
BC005131 mRNA. Translation: AAH05131.1.
CCDSiCCDS8124.1.
RefSeqiNP_001229410.1. NM_001242481.1.
NP_001229411.1. NM_001242482.1.
NP_001229412.1. NM_001242483.1.
NP_001229413.1. NM_001242484.1.
NP_001229414.1. NM_001242485.1.
NP_001229415.1. NM_001242486.1.
NP_115701.2. NM_032325.3.
UniGeneiHs.425178.

Genome annotation databases

EnsembliENST00000312234; ENSP00000309175; ENSG00000175376.
ENST00000526451; ENSP00000436644; ENSG00000175376.
ENST00000527249; ENSP00000435439; ENSG00000175376.
ENST00000529964; ENSP00000435942; ENSG00000175376.
ENST00000533544; ENSP00000434056; ENSG00000175376.
GeneIDi84285.
KEGGihsa:84285.
UCSCiuc001ogm.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK094129 mRNA. Translation: BAC04293.1.
AK311891 mRNA. Translation: BAG34832.1.
CH471076 Genomic DNA. Translation: EAW74478.1.
BC005131 mRNA. Translation: AAH05131.1.
CCDSiCCDS8124.1.
RefSeqiNP_001229410.1. NM_001242481.1.
NP_001229411.1. NM_001242482.1.
NP_001229412.1. NM_001242483.1.
NP_001229413.1. NM_001242484.1.
NP_001229414.1. NM_001242485.1.
NP_001229415.1. NM_001242486.1.
NP_115701.2. NM_032325.3.
UniGeneiHs.425178.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DGYNMR-A17-114[»]
ProteinModelPortaliQ8N9N8.
SMRiQ8N9N8. Positions 16-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124012. 16 interactions.
IntActiQ8N9N8. 12 interactions.
MINTiMINT-1479911.
STRINGi9606.ENSP00000309175.

PTM databases

iPTMnetiQ8N9N8.
PhosphoSiteiQ8N9N8.

Polymorphism and mutation databases

BioMutaiEIF1AD.
DMDMi74729733.

Proteomic databases

EPDiQ8N9N8.
MaxQBiQ8N9N8.
PaxDbiQ8N9N8.
PeptideAtlasiQ8N9N8.
PRIDEiQ8N9N8.

Protocols and materials databases

DNASUi84285.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312234; ENSP00000309175; ENSG00000175376.
ENST00000526451; ENSP00000436644; ENSG00000175376.
ENST00000527249; ENSP00000435439; ENSG00000175376.
ENST00000529964; ENSP00000435942; ENSG00000175376.
ENST00000533544; ENSP00000434056; ENSG00000175376.
GeneIDi84285.
KEGGihsa:84285.
UCSCiuc001ogm.3. human.

Organism-specific databases

CTDi84285.
GeneCardsiEIF1AD.
HGNCiHGNC:28147. EIF1AD.
HPAiHPA054991.
HPA058735.
neXtProtiNX_Q8N9N8.
PharmGKBiPA162384553.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2925. Eukaryota.
ENOG4111N6Z. LUCA.
GeneTreeiENSGT00390000011180.
HOGENOMiHOG000007486.
HOVERGENiHBG097893.
InParanoidiQ8N9N8.
KOiK15025.
OMAiVNTNRCN.
OrthoDBiEOG75J0Q8.
PhylomeDBiQ8N9N8.
TreeFamiTF314439.

Miscellaneous databases

ChiTaRSiEIF1AD. human.
EvolutionaryTraceiQ8N9N8.
GenomeRNAii84285.
PROiQ8N9N8.

Gene expression databases

BgeeiQ8N9N8.
CleanExiHS_EIF1AD.
ExpressionAtlasiQ8N9N8. baseline and differential.
GenevisibleiQ8N9N8. HS.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR001253. TIF_eIF-1A.
[Graphical view]
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
SMARTiSM00652. eIF1a. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Haponin (eIF1AD) interacts with glyceraldehyde 3-phosphate dehydrogenase in the CHO-K1 cell line."
    Rakitina T.V., Bogatova O.V., Smirnova E.V., Pozdeev V.I., Kostanian I.A., Lipkin V.M.
    Bioorg. Khim. 36:312-318(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH GAPDH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  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].
    Tissue: Skeletal muscle.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANT ASN-23.
    Tissue: Skin.
  5. Cited for: INTERACTION WITH STAT1.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  11. "Solution structure of the eukaryotic initiation factor 1A in MGC11102 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 16-114.

Entry informationi

Entry nameiEIF1A_HUMAN
AccessioniPrimary (citable) accession number: Q8N9N8
Secondary accession number(s): B2R4N5, Q9BSC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 117 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.