PID1

Protein identityUniProt · HPA

UniProt accession

Q7Z2X4

Gene

PID1

Ensembl

ENSG00000153823

Chromosome

2

Canonical length

250 aa

Protein class

Predicted intracellular proteins

Subcellular location

Endoplasmic reticulum

OverviewNCBI Gene

Involved in several processes, including negative regulation of ATP biosynthetic process; negative regulation of D-glucose import; and positive regulation of metabolic process. Located in cytoplasm. [provided by Alliance of Genome Resources, Jul 2025]

Canonical amino-acid sequenceUniProt

250 residues, UniProt reviewed canonical sequence.

>Q7Z2X4|PID1
     1  MFSLPLSLPL CEDTAFLPSK CCSSHKTIKQ ARTLIMIFLA SGTHFQTMLK SKLNVLTLKK
    61  EPLPAVIFHE PEAIELCTTT PLMKTRTHSG CKVTYLGKVS TTGMQFLSGC TEKPVIELWK
   121  KHTLAREDVF PANALLEIRP FQVWLHHLDH KGEATVHMDT FQVARIAYCT ADHNVSPNIF
   181  AWVYREINDD LSYQMDCHAV ECESKLEAKK LAHAMMEAFR KTFHSMKSDG RIHSNSSSEE
   241  VSQELESDDG

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PID1 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)

0.44

Highest tissue expression

91 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about PID1.

Disease | GeneticClinVar

1 pathogenic / likely-pathogenic of 41 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Moyamoya angiopathy

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)

1.21

gnomAD pLI

0

gnomAD missense Z

0.27

DepMap mean gene effect

0.11

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cellular response to cytokine stimulus
• cellular response to fatty acid
• cellular response to interleukin-6
• cellular response to leptin stimulus
• cellular response to tumor necrosis factor
• energy reserve metabolic process
• mitochondrion organization
• negative regulation of ATP biosynthetic process
• negative regulation of D-glucose import
• negative regulation of insulin receptor signaling pathway
• negative regulation of protein localization to plasma membrane
• positive regulation of ATP biosynthetic process
• positive regulation of fat cell proliferation
• positive regulation of gene expression
• positive regulation of reactive oxygen species metabolic process
• positive regulation of transcription by RNA polymerase II
• regulation of mitochondrial fusion
• regulation of mitochondrial membrane potential
• regulation of reactive oxygen species metabolic process

Cellular components

• cytoplasm

Protein domainsUniProt · Pfam · InterPro

• PTB/PI domain
• PH-like domain superfamily
• Phosphotyrosine interaction domain (PTB/PID)
• Phosphotyrosine interaction domain containing 1
• PID1, PTB domain

KeywordsUniProt

• Cytoplasm
• Phosphoprotein

InteractionsUniProt · HPA

Protein binding partners of PID1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• CUBN
• LRP1