EFL1

Protein identityUniProt · HPA

UniProt accession

Q7Z2Z2

Gene

EFL1

Ensembl

ENSG00000140598

Chromosome

15

Canonical length

1120 aa

Protein class

Disease related genes, Human disease related genes, Metabolic proteins, Predicted intracellular proteins

Subcellular location

Cytosol

OverviewNCBI Gene

Enables GTPase activity and ribosome binding activity. Involved in GTP metabolic process and cytosolic ribosome assembly. Predicted to be part of ribonucleoprotein complex. Predicted to be active in cytosol. Implicated in Shwachman-Diamond syndrome. [provided by Alliance of Genome Resources, Jul 2025]

Canonical amino-acid sequenceUniProt

1120 residues, UniProt reviewed canonical sequence.

>Q7Z2Z2|EFL1
     1  MVLNSLDKMI QLQKNTANIR NICVLAHVDH GKTTLADCLI SSNGIISSRL AGKLRYMDSR
    61  EDEQIRGITM KSSAISLHYA TGNEEYLINL IDSPGHVDFS SEVSTAVRIC DGCIIVVDAV
   121  EGVCPQTQAV LRQAWLENIR PVLVINKIDR LIVELKFTPQ EAYSHLKNIL EQINALTGTL
   181  FTSKVLEERA ERETESQVNP NSEQGEQVYD WSTGLEDTDD SHLYFSPEQG NVVFTSAIDG
   241  WGFGIEHFAR IYSQKIGIKK EVLMKTLWGD YYINMKAKKI MKGDQAKGKK PLFVQLILEN
   301  IWSLYDAVLK KDKDKIDKIV TSLGLKIGAR EARHSDPKVQ INAICSQWLP ISHAVLAMVC
   361  QKLPSPLDIT AERVERLMCT GSQTFDSFPP ETQALKAAFM KCGSEDTAPV IIFVSKMFAV
   421  DAKALPQNKP RPLTQEEIAQ RRERARQRHA EKLAAAQGQA PLEPTQDGSA IETCPKGEEP
   481  RGDEQQVESM TPKPVLQEEN NQESFIAFAR VFSGVARRGK KIFVLGPKYS PLEFLRRVPL
   541  GFSAPPDGLP QVPHMAYCAL ENLYLLMGRE LEYLEEVPPG NVLGIGGLQD FVLKSATLCS
   601  LPSCPPFIPL NFEATPIVRV AVEPKHPSEM PQLVKGMKLL NQADPCVQIL IQETGEHVLV
   661  TAGEVHLQRC LDDLKERFAK IHISVSEPII PFRETITKPP KVDMVNEEIG KQQKVAVIHQ
   721  MKEDQSKIPE GIQVDSDGLI TITTPNKLAT LSVRAMPLPE EVTQILEENS DLIRSMEQLT
   781  SSLNEGENTH MIHQKTQEKI WEFKGKLEQH LTGRRWRNIV DQIWSFGPRK CGPNILVNKS
   841  EDFQNSVWTG PADKASKEAS RYRDLGNSIV SGFQLATLSG PMCEEPLMGV CFVLEKWDLS
   901  KFEEQGASDL AKEGQEENET CSGGNENQEL QDGCSEAFEK RTSQKGESPL TDCYGPFSGQ
   961  LIATMKEACR YALQVKPQRL MAAMYTCDIM ATGDVLGRVY AVLSKREGRV LQEEMKEGTD
  1021  MFIIKAVLPV AESFGFADEI RKRTSGLASP QLVFSHWEII PSDPFWVPTT EEEYLHFGEK
  1081  ADSENQARKY MNAVRKRKGL YVEEKIVEHA EKQRTLSKNK

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against EFL1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.31

Highest tissue expression

15 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about EFL1.

Disease | AllUniProt

Conditions EFL1 is implicated in, by any mechanism.

• Shwachman-Diamond syndrome 2 (SDS2) MIM:617941

Disease | GeneticClinVar

6 pathogenic / likely-pathogenic of 584 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Shwachman-Diamond syndrome 2
• Shwachman syndrome

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.56

gnomAD pLI

0

DepMap mean gene effect

-0.94

DepMap dependency class

common

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cytosolic ribosome assembly
• GTP metabolic process

Molecular functions

• GTP binding
• GTPase activity
• ribosome binding
• translation elongation factor activity

Cellular components

• cytosol
• ribonucleoprotein complex

Protein domainsUniProt · Pfam · InterPro

• Elongation factor EFG, domain V-like
• Translational (tr)-type GTP-binding domain
• Small GTP-binding domain
• Translation protein, beta-barrel domain superfamily
• Small ribosomal subunit protein uS5 domain 2-type fold, subgroup
• Ribosomal protein uS5 domain 2-type superfamily
• P-loop containing nucleoside triphosphate hydrolase
• EF-G domain III/V-like
• Elongation Factor G, domain II
• Elongation factor Tu GTP binding domain
• Elongation factor G C-terminus
• Elongation Factor G, domain III
• Elongation factor-like GTPase 1 domain
• Elongation factor-like GTPase 1-like domain

KeywordsUniProt

• Acetylation
• Elongation factor
• GTP-binding
• Hydrolase
• Nucleotide-binding
• Protein biosynthesis
• Ribosome biogenesis

InteractionsUniProt · HPA

Protein binding partners of EFL1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• SBDS