EIF3D

Functionⁱ

mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs (PubMed:27462815). 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 pre-initiation 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 (PubMed:18599441, PubMed:25849773). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs (PubMed:27462815).3 Publications

(Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426).1 Publication

GO - Molecular functionⁱ

mRNA cap binding
Source: UniProtKB
Inferred from direct assayⁱ
- 27462815
RNA binding
Source: UniProtKB
Inferred from direct assayⁱ
translation initiation factor activity Source: UniProtKB-KW

Complete GO annotation...

GO - Biological processⁱ

cap-dependent translational initiation
Source: UniProtKB
Inferred from direct assayⁱ
- 27462815
formation of cytoplasmic translation initiation complex Source: Ensembl
IRES-dependent viral translational initiation
Source: UniProtKB
Inferred from direct assayⁱ
- 9573242
positive regulation of mRNA binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 24092755
positive regulation of translation
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 24092755
translational initiation
Source: UniProtKB
Inferred from direct assayⁱ
- 17581632
viral translational termination-reinitiation
Source: UniProtKB
Inferred from direct assayⁱ
- 21347434

Complete GO annotation...

Keywordsⁱ

Molecular function	Initiation factor, RNA-binding
Biological process	Protein biosynthesis

Enzyme and pathway databases

Reactomeⁱ	R-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression. R-HSA-72649. Translation initiation complex formation. R-HSA-72689. Formation of a pool of free 40S subunits. R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex. R-HSA-72702. Ribosomal scanning and start codon recognition. R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Reactomeⁱ

R-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Eukaryotic translation initiation factor 3 subunit DUniRule annotation Short name: eIF3dUniRule annotation Alternative name(s): Eukaryotic translation initiation factor 3 subunit 7UniRule annotation eIF-3-zetaUniRule annotation eIF3 p66
Gene namesⁱ	Name:EIF3DUniRule annotation Synonyms:EIF3S7UniRule annotation
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 22

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3278. EIF3D.

HGNCⁱ

HGNC:3278. EIF3D.

Subcellular locationⁱ

Cytoplasm
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_03003

GO - Cellular componentⁱ

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Defects in EIF3D are associated with some cancers, such as prostate, breast and colon cancers. Disease susceptibility may be associated with variations affecting the gene represented in this entry. Down-regulation inhibits proliferation of cancers (PubMed:25370813, PubMed:25322666, PubMed:25682860, PubMed:26617750, PubMed:26008152, PubMed:26036682, PubMed:27035563).7 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	249	D → Q: Reduced binding to JUN mRNA; when associated with 262-I-A-263. 1 Publication	1
Mutagenesisⁱ	262 – 263	VY → IA: Reduced binding to JUN mRNA; when associated with Q-249. 1 Publication	2
Mutagenesisⁱ	317 – 321	TYINH → EYENA: Reduced binding to JUN mRNA. 1 Publication	5

Organism-specific databases

DisGeNET More...DisGeNETⁱ	8664.
Open Targets More...OpenTargetsⁱ	ENSG00000100353.
PharmGKBⁱ	PA162384740.

Polymorphism and mutation databases

BioMutaⁱ	EIF3D.

BioMutaⁱ

EIF3D.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000123520	1 – 548	Eukaryotic translation initiation factor 3 subunit DAdd BLAST		548

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	53	N6-acetyllysineBy similarity	1
Modified residueⁱ	161	PhosphoserineCombined sources	1
Modified residueⁱ	528	PhosphoserineCombined sources	1
Modified residueⁱ	529	PhosphoserineCombined sources	1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	O15371.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O15371.
PaxDbⁱ	O15371.
PeptideAtlas More...PeptideAtlasⁱ	O15371.
PRIDEⁱ	O15371.

PTM databases

iPTMnetⁱ	O15371.
PhosphoSitePlusⁱ	O15371.
SwissPalmⁱ	O15371.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000100353.
CleanExⁱ	HS_EIF3D.
ExpressionAtlasⁱ	O15371. baseline and differential.
Genevisibleⁱ	O15371. HS.

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA045882. HPA063330. HPA066216.

HPAⁱ

HPA045882.
HPA063330.
HPA066216.

Interactionⁱ

Subunit structureⁱ

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.UniRule annotation5 Publications

(Microbial infection) Interacts with Norwalk virus VPg protein (PubMed:12773399).1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
BEND5	Q7L4P6	3	EBI-353818,EBI-724373
HOMER3	B2RA10	3	EBI-353818,EBI-10175777
LZTS2	Q9BRK4	3	EBI-353818,EBI-741037
MORN3	Q6PF18	4	EBI-353818,EBI-9675802
ORF	Q9Q2G4	5	EBI-353818,EBI-6248094	From Human immunodeficiency virus 1.
PHLDA1	Q8WV24	2	EBI-353818,EBI-738731
REL	Q04864	3	EBI-353818,EBI-307352
SAT	Q6ICU9	3	EBI-353818,EBI-10178867
TRIM27	P14373	5	EBI-353818,EBI-719493

Show more details

Protein-protein interaction databases

BioGridⁱ	114213. 70 interactors.
Database of interacting proteins More...DIPⁱ	DIP-32870N.
IntActⁱ	O15371. 57 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-5003799.
STRINGⁱ	9606.ENSP00000216190.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	O15371.
SMRⁱ	O15371.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	285 – 299	RNA gateBy similarityAdd BLAST		15

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	530 – 547	Asp/Glu-rich (highly acidic)Add BLAST		18

Domainⁱ

The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of EIF3D into the full eukaryotic translation initiation factor 3 (eIF-3) complex.1 Publication

Sequence similaritiesⁱ

Belongs to the eIF-3 subunit D family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	KOG2479. Eukaryota. ENOG410XP1E. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000002667.
HOGENOMⁱ	HOG000241593.
HOVERGENⁱ	HBG000849.
InParanoidⁱ	O15371.
KEGG Orthology (KO) More...KOⁱ	K03251.
OMAⁱ	DRIFHTV.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G07IK.
PhylomeDBⁱ	O15371.
TreeFamⁱ	TF101519.

Family and domain databases

Gene3Dⁱ	1.25.10.10. 1 hit.
HAMAPⁱ	MF_03003. eIF3d. 1 hit.
InterProⁱ	View protein in InterPro IPR011989. ARM-like. IPR007783. eIF3d.
PANTHERⁱ	PTHR12399. PTHR12399. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF05091. eIF-3_zeta. 1 hit.
PIRSFⁱ	PIRSF016281. EIF-3_zeta. 1 hit.

Sequences (3)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: O15371-1) [UniParc]FASTA Add 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
MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY 
        60         70         80         90        100
QDKRYTNKYS SQFGGGSQYA YFHEEDESSF QLVDTARTQK TAYQRNRMRF 
       110        120        130        140        150
AQRNLRRDKD RRNMLQFNLQ ILPKSAKQKE RERIRLQKKF QKQFGVRQKW 
       160        170        180        190        200
DQKSQKPRDS SVEVRSDWEV KEEMDFPQLM KMRYLEVSEP QDIECCGALE 
       210        220        230        240        250
YYDKAFDRIT TRSEKPLRSI KRIFHTVTTT DDPVIRKLAK TQGNVFATDA 
       260        270        280        290        300
ILATLMSCTR SVYSWDIVVQ RVGSKLFFDK RDNSDFDLLT VSETANEPPQ 
       310        320        330        340        350
DEGNSFNSPR NLAMEATYIN HNFSQQCLRM GKERYNFPNP NPFVEDDMDK 
       360        370        380        390        400
NEIASVAYRY RRWKLGDDID LIVRCEHDGV MTGANGEVSF INIKTLNEWD 
       410        420        430        440        450
SRHCNGVDWR QKLDSQRGAV IATELKNNSY KLARWTCCAL LAGSEYLKLG 
       460        470        480        490        500
YVSRYHVKDS SRHVILGTQQ FKPNEFASQI NLSVENAWGI LRCVIDICMK 
       510        520        530        540 
LEEGKYLILK DPNKQVIRVY SLPDGTFSSD EDEEEEEEEE EEEEEEET

Length:548

Mass (Da):63,973

Last modified:January 1, 1998 - v1

Checksum:ⁱ7FE0448EC3BE1711

GO

Isoform 2 (identifier: O15371-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
54-102: Missing.

« Hide

        10         20         30         40         50
MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY 
        60         70         80         90        100
QDKRNLRRDK DRRNMLQFNL QILPKSAKQK ERERIRLQKK FQKQFGVRQK 
       110        120        130        140        150
WDQKSQKPRD SSVEVRSDWE VKEEMDFPQL MKMRYLEVSE PQDIECCGAL 
       160        170        180        190        200
EYYDKAFDRI TTRSEKPLRS IKRIFHTVTT TDDPVIRKLA KTQGNVFATD 
       210        220        230        240        250
AILATLMSCT RSVYSWDIVV QRVGSKLFFD KRDNSDFDLL TVSETANEPP 
       260        270        280        290        300
QDEGNSFNSP RNLAMEATYI NHNFSQQCLR MGKERYNFPN PNPFVEDDMD 
       310        320        330        340        350
KNEIASVAYR YRRWKLGDDI DLIVRCEHDG VMTGANGEVS FINIKTLNEW 
       360        370        380        390        400
DSRHCNGVDW RQKLDSQRGA VIATELKNNS YKLARWTCCA LLAGSEYLKL 
       410        420        430        440        450
GYVSRYHVKD SSRHVILGTQ QFKPNEFASQ INLSVENAWG ILRCVIDICM 
       460        470        480        490 
KLEEGKYLIL KDPNKQVIRV YSLPDGTFSS DEDEEEEEEE EEEEEEEET

Note: No experimental confirmation available.

Show »

Length:499

Mass (Da):58,140

Checksum:ⁱE6E9019C723159C2

GO

Isoform 3 (identifier: O15371-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
137-151: Missing.

« Hide

        10         20         30         40         50
MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY 
        60         70         80         90        100
QDKRYTNKYS SQFGGGSQYA YFHEEDESSF QLVDTARTQK TAYQRNRMRF 
       110        120        130        140        150
AQRNLRRDKD RRNMLQFNLQ ILPKSAKQKE RERIRLQKSQ KPRDSSVEVR 
       160        170        180        190        200
SDWEVKEEMD FPQLMKMRYL EVSEPQDIEC CGALEYYDKA FDRITTRSEK 
       210        220        230        240        250
PLRSIKRIFH TVTTTDDPVI RKLAKTQGNV FATDAILATL MSCTRSVYSW 
       260        270        280        290        300
DIVVQRVGSK LFFDKRDNSD FDLLTVSETA NEPPQDEGNS FNSPRNLAME 
       310        320        330        340        350
ATYINHNFSQ QCLRMGKERY NFPNPNPFVE DDMDKNEIAS VAYRYRRWKL 
       360        370        380        390        400
GDDIDLIVRC EHDGVMTGAN GEVSFINIKT LNEWDSRHCN GVDWRQKLDS 
       410        420        430        440        450
QRGAVIATEL KNNSYKLARW TCCALLAGSE YLKLGYVSRY HVKDSSRHVI 
       460        470        480        490        500
LGTQQFKPNE FASQINLSVE NAWGILRCVI DICMKLEEGK YLILKDPNKQ 
       510        520        530 
VIRVYSLPDG TFSSDEDEEE EEEEEEEEEE EET

Note: No experimental confirmation available.

Show »

Length:533

Mass (Da):62,040

Checksum:ⁱ32AA0A0A31EEF2CD

GO

Mass spectrometryⁱ

Molecular mass is 63972.9 Da from positions 1 - 548. 1 Publication

Molecular mass is 64046.7±1.4 Da from positions 1 - 548. Determined by MALDI. 1 Publication

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_074184	310	R → C1 PublicationCorresponds to variant dbSNP:rs745920273Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_055473	54 – 102	Missing in isoform 2. 1 PublicationAdd BLAST		49
Alternative sequenceⁱVSP_055474	137 – 151	Missing in isoform 3. 1 PublicationAdd BLAST		15

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U54558 mRNA. Translation: AAD03466.1. BT007381 mRNA. Translation: AAP36045.1. CR456489 mRNA. Translation: CAG30375.1. AK300199 mRNA. Translation: BAG61970.1. AK301284 mRNA. Translation: BAG62843.1. AK312939 mRNA. Translation: BAG35781.1. AL022313 Genomic DNA. Translation: CAA18440.1. CH471095 Genomic DNA. Translation: EAW60109.1. BC000328 mRNA. Translation: AAH00328.1. BC000469 mRNA. Translation: AAH00469.1. BC014912 mRNA. Translation: AAH14912.1. BC080515 mRNA. Translation: AAH80515.1. BC093100 mRNA. Translation: AAH93100.1. BC093686 mRNA. Translation: AAH93686.1. BC101477 mRNA. Translation: AAI01478.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS13930.1. [O15371-1]
NCBI Reference Sequences More...RefSeqⁱ	NP_003744.1. NM_003753.3. [O15371-1]
UniGeneⁱ	Hs.55682.

Genome annotation databases

Ensemblⁱ	ENST00000216190; ENSP00000216190; ENSG00000100353. [O15371-1] ENST00000405442; ENSP00000385812; ENSG00000100353. [O15371-1]
GeneIDⁱ	8664.
KEGGⁱ	hsa:8664.
UCSC genome browser More...UCSCⁱ	uc003apr.4. human. [O15371-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

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.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U54558 mRNA. Translation: AAD03466.1. BT007381 mRNA. Translation: AAP36045.1. CR456489 mRNA. Translation: CAG30375.1. AK300199 mRNA. Translation: BAG61970.1. AK301284 mRNA. Translation: BAG62843.1. AK312939 mRNA. Translation: BAG35781.1. AL022313 Genomic DNA. Translation: CAA18440.1. CH471095 Genomic DNA. Translation: EAW60109.1. BC000328 mRNA. Translation: AAH00328.1. BC000469 mRNA. Translation: AAH00469.1. BC014912 mRNA. Translation: AAH14912.1. BC080515 mRNA. Translation: AAH80515.1. BC093100 mRNA. Translation: AAH93100.1. BC093686 mRNA. Translation: AAH93686.1. BC101477 mRNA. Translation: AAI01478.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS13930.1. [O15371-1]
NCBI Reference Sequences More...RefSeqⁱ	NP_003744.1. NM_003753.3. [O15371-1]
UniGeneⁱ	Hs.55682.

3D structure databases

ProteinModelPortalⁱ	O15371.
SMRⁱ	O15371.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	114213. 70 interactors.
Database of interacting proteins More...DIPⁱ	DIP-32870N.
IntActⁱ	O15371. 57 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-5003799.
STRINGⁱ	9606.ENSP00000216190.

PTM databases

iPTMnetⁱ	O15371.
PhosphoSitePlusⁱ	O15371.
SwissPalmⁱ	O15371.

Polymorphism and mutation databases

BioMutaⁱ	EIF3D.

BioMutaⁱ

EIF3D.

Proteomic databases

EPDⁱ	O15371.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O15371.
PaxDbⁱ	O15371.
PeptideAtlas More...PeptideAtlasⁱ	O15371.
PRIDEⁱ	O15371.

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	8664.
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000216190; ENSP00000216190; ENSG00000100353. [O15371-1] ENST00000405442; ENSP00000385812; ENSG00000100353. [O15371-1]
GeneIDⁱ	8664.
KEGGⁱ	hsa:8664.
UCSC genome browser More...UCSCⁱ	uc003apr.4. human. [O15371-1]

Organism-specific databases

CTDⁱ	8664.
DisGeNET More...DisGeNETⁱ	8664.
GeneCardsⁱ	EIF3D.
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3278. EIF3D.
Human Protein Atlas More...HPAⁱ	HPA045882. HPA063330. HPA066216.
MIMⁱ	603915. gene.
neXtProtⁱ	NX_O15371.
Open Targets More...OpenTargetsⁱ	ENSG00000100353.
PharmGKBⁱ	PA162384740.
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2479. Eukaryota. ENOG410XP1E. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000002667.
HOGENOMⁱ	HOG000241593.
HOVERGENⁱ	HBG000849.
InParanoidⁱ	O15371.
KEGG Orthology (KO) More...KOⁱ	K03251.
OMAⁱ	DRIFHTV.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G07IK.
PhylomeDBⁱ	O15371.
TreeFamⁱ	TF101519.

Enzyme and pathway databases

Reactomeⁱ	R-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression. R-HSA-72649. Translation initiation complex formation. R-HSA-72689. Formation of a pool of free 40S subunits. R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex. R-HSA-72702. Ribosomal scanning and start codon recognition. R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Reactomeⁱ

R-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSⁱ	EIF3D. human.
GeneWikiⁱ	EIF3D.
GenomeRNAiⁱ	8664.
Protein Ontology More...PROⁱ	PR:O15371.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000100353.
CleanExⁱ	HS_EIF3D.
ExpressionAtlasⁱ	O15371. baseline and differential.
Genevisibleⁱ	O15371. HS.

Family and domain databases

Gene3Dⁱ	1.25.10.10. 1 hit.
HAMAPⁱ	MF_03003. eIF3d. 1 hit.
InterProⁱ	View protein in InterPro IPR011989. ARM-like. IPR007783. eIF3d.
PANTHERⁱ	PTHR12399. PTHR12399. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF05091. eIF-3_zeta. 1 hit.
PIRSFⁱ	PIRSF016281. EIF-3_zeta. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	EIF3D_HUMAN
Accessionⁱ	O15371Primary (citable) accession number: O15371 Secondary accession number(s): A8MWD3 , B2R7D4, B4DTF8, B4DVY1, Q3MJD9, Q5M9Q6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
	Last sequence update:	January 1, 1998
	Last modified:	July 5, 2017
	This is version 165 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Complete proteome, Reference proteome

Documents

Human chromosome 22
Human chromosome 22: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
Translation initiation factors
List of translation initiation factor entries
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
SIMILARITY comments
Index of protein domains and families

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UniProtKB - O15371 (EIF3D_HUMAN)

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Eukaryotic translation initiation factor 3 subunit D

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (3)ⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ