Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Rab proteins geranylgeranyltransferase component A 1

Gene

CHM

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

Functioni

Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation.2 Publications

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • Rab geranylgeranyltransferase activity Source: ProtInc
  • Rab GTPase binding Source: UniProtKB

GO - Biological processi

  • blood vessel development Source: Ensembl
  • protein geranylgeranylation Source: UniProtKB
  • protein targeting to membrane Source: UniProtKB
  • response to stimulus Source: UniProtKB-KW
  • visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Rab proteins geranylgeranyltransferase component A 1
Alternative name(s):
Choroideremia protein
Rab escort protein 1
Short name:
REP-1
TCD protein
Gene namesi
Name:CHM
Synonyms:REP1, TCD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:1940. CHM.

Subcellular locationi

  • Cytoplasmcytosol 1 Publication

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • Rab-protein geranylgeranyltransferase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Choroideremia (CHM)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn X-linked recessive disease characterized by a slowly progressive degeneration of the choroid, photoreceptors, and retinal pigment epithelium. Affected males develop night blindness in their teenage years followed by loss of peripheral vision and complete blindness at middle age. Carrier females are generally asymptomatic but funduscopic examination often shows patchy areas of chorioretinal atrophy.

See also OMIM:303100
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti471 – 4711Q → L in CHM; may affect splicing. 1 Publication
VAR_008273
Natural varianti507 – 5071H → R in CHM; impairs the interaction with RABGGTA. 1 Publication
VAR_066847
Natural varianti550 – 5501L → P in CHM. 1 Publication
VAR_066848

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi282 – 2821F → L: Abolishes prenylation of RAB1A and association with RGGT. 1 Publication
Mutagenesisi290 – 2901V → F: Impairs prenylation of RAB1A and abolishes association with RGGT. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi303100. phenotype.
Orphaneti180. Choroideremia.
PharmGKBiPA26471.

Polymorphism and mutation databases

BioMutaiCHM.
DMDMi21431807.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 653653Rab proteins geranylgeranyltransferase component A 1PRO_0000056686Add
BLAST

Proteomic databases

MaxQBiP24386.
PaxDbiP24386.
PRIDEiP24386.

PTM databases

PhosphoSiteiP24386.

Expressioni

Gene expression databases

BgeeiP24386.
CleanExiHS_CHM.
GenevestigatoriP24386.

Organism-specific databases

HPAiCAB016171.
HPA003231.

Interactioni

Subunit structurei

Monomer. Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates Rab protein binding. Can associate with the Rab GGTase dimer (RGGT or component B) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp. Interacts with RAB1A, RAB1B, RAB5A, RAB7A and RAB27A and mediates their prenylation.3 Publications

Protein-protein interaction databases

BioGridi107545. 16 interactions.
IntActiP24386. 48 interactions.
STRINGi9606.ENSP00000350386.

Structurei

3D structure databases

ProteinModelPortaliP24386.
SMRiP24386. Positions 3-107, 178-617.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab GDI family.Curated

Phylogenomic databases

eggNOGiCOG5044.
GeneTreeiENSGT00530000063044.
HOGENOMiHOG000220905.
HOVERGENiHBG004961.
InParanoidiP24386.
OMAiQKNHASV.
OrthoDBiEOG7Q5HCQ.
PhylomeDBiP24386.
TreeFamiTF320813.

Family and domain databases

InterProiIPR018203. GDP_dissociation_inhibitor.
IPR001738. Rab_escort.
[Graphical view]
PfamiPF00996. GDI. 2 hits.
[Graphical view]
PIRSFiPIRSF016550. Rab_ger_ger_transf_A_euk. 1 hit.
PRINTSiPR00893. RABESCORT.
PR00891. RABGDIREP.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P24386-1) [UniParc]FASTAAdd 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
MADTLPSEFD VIVIGTGLPE SIIAAACSRS GRRVLHVDSR SYYGGNWASF
60 70 80 90 100
SFSGLLSWLK EYQENSDIVS DSPVWQDQIL ENEEAIALSR KDKTIQHVEV
110 120 130 140 150
FCYASQDLHE DVEEAGALQK NHALVTSANS TEAADSAFLP TEDESLSTMS
160 170 180 190 200
CEMLTEQTPS SDPENALEVN GAEVTGEKEN HCDDKTCVPS TSAEDMSENV
210 220 230 240 250
PIAEDTTEQP KKNRITYSQI IKEGRRFNID LVSKLLYSRG LLIDLLIKSN
260 270 280 290 300
VSRYAEFKNI TRILAFREGR VEQVPCSRAD VFNSKQLTMV EKRMLMKFLT
310 320 330 340 350
FCMEYEKYPD EYKGYEEITF YEYLKTQKLT PNLQYIVMHS IAMTSETASS
360 370 380 390 400
TIDGLKATKN FLHCLGRYGN TPFLFPLYGQ GELPQCFCRM CAVFGGIYCL
410 420 430 440 450
RHSVQCLVVD KESRKCKAII DQFGQRIISE HFLVEDSYFP ENMCSRVQYR
460 470 480 490 500
QISRAVLITD RSVLKTDSDQ QISILTVPAE EPGTFAVRVI ELCSSTMTCM
510 520 530 540 550
KGTYLVHLTC TSSKTAREDL ESVVQKLFVP YTEMEIENEQ VEKPRILWAL
560 570 580 590 600
YFNMRDSSDI SRSCYNDLPS NVYVCSGPDC GLGNDNAVKQ AETLFQEICP
610 620 630 640 650
NEDFCPPPPN PEDIILDGDS LQPEASESSA IPEANSETFK ESTNLGNLEE

SSE
Length:653
Mass (Da):73,476
Last modified:June 6, 2002 - v3
Checksum:i7CFFAECE7BA1F3AF
GO
Isoform 2 (identifier: P24386-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     105-110: SQDLHE → RSTLLL
     111-653: Missing.

Note: No experimental confirmation available.

Show »
Length:110
Mass (Da):12,301
Checksum:iAD591A7B415DFD18
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti625 – 6262AS → RA in AAA61032 (PubMed:2215697).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti471 – 4711Q → L in CHM; may affect splicing. 1 Publication
VAR_008273
Natural varianti507 – 5071H → R in CHM; impairs the interaction with RABGGTA. 1 Publication
VAR_066847
Natural varianti550 – 5501L → P in CHM. 1 Publication
VAR_066848

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei105 – 1106SQDLHE → RSTLLL in isoform 2. 1 PublicationVSP_042817
Alternative sequencei111 – 653543Missing in isoform 2. 1 PublicationVSP_042818Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78121 mRNA. Translation: CAA55011.1.
AL009175, AL022401, AL035451 Genomic DNA. Translation: CAI42098.1.
AL022401, AL009175, AL035451 Genomic DNA. Translation: CAI43163.1.
AL035451, AL009175 Genomic DNA. Translation: CAI42042.1.
AL035451, AL009175, AL022401 Genomic DNA. Translation: CAI42043.1.
AL009175, AL035451 Genomic DNA. Translation: CAI42097.1.
AL138748 Genomic DNA. No translation available.
BC130494 mRNA. Translation: AAI30495.1.
BC130496 mRNA. Translation: AAI30497.1.
M83773 mRNA. Translation: AAA61032.1.
X57637 mRNA. Translation: CAA40855.1.
S37423
, S37416, S37417, S37422 Genomic DNA. Translation: AAD13814.1.
CCDSiCCDS14454.1. [P24386-1]
CCDS48139.1. [P24386-2]
PIRiI37234.
RefSeqiNP_000381.1. NM_000390.2. [P24386-1]
NP_001138886.1. NM_001145414.2.
UniGeneiHs.496449.

Genome annotation databases

EnsembliENST00000357749; ENSP00000350386; ENSG00000188419. [P24386-1]
ENST00000615443; ENSP00000484306; ENSG00000188419. [P24386-2]
GeneIDi1121.
KEGGihsa:1121.
UCSCiuc004eet.3. human. [P24386-1]
uc004eev.4. human. [P24386-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Mutations of the REP1 gene

Retina International's Scientific Newsletter

Retinal and hearing impairment genetic mutation database choroideremia (Rab escort protein 1) (CHM)

Leiden Open Variation Database (LOVD)

NGRL, Manchester LOVD choroideremia (Rab escort protein 1) (CHM)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78121 mRNA. Translation: CAA55011.1.
AL009175, AL022401, AL035451 Genomic DNA. Translation: CAI42098.1.
AL022401, AL009175, AL035451 Genomic DNA. Translation: CAI43163.1.
AL035451, AL009175 Genomic DNA. Translation: CAI42042.1.
AL035451, AL009175, AL022401 Genomic DNA. Translation: CAI42043.1.
AL009175, AL035451 Genomic DNA. Translation: CAI42097.1.
AL138748 Genomic DNA. No translation available.
BC130494 mRNA. Translation: AAI30495.1.
BC130496 mRNA. Translation: AAI30497.1.
M83773 mRNA. Translation: AAA61032.1.
X57637 mRNA. Translation: CAA40855.1.
S37423
, S37416, S37417, S37422 Genomic DNA. Translation: AAD13814.1.
CCDSiCCDS14454.1. [P24386-1]
CCDS48139.1. [P24386-2]
PIRiI37234.
RefSeqiNP_000381.1. NM_000390.2. [P24386-1]
NP_001138886.1. NM_001145414.2.
UniGeneiHs.496449.

3D structure databases

ProteinModelPortaliP24386.
SMRiP24386. Positions 3-107, 178-617.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107545. 16 interactions.
IntActiP24386. 48 interactions.
STRINGi9606.ENSP00000350386.

PTM databases

PhosphoSiteiP24386.

Polymorphism and mutation databases

BioMutaiCHM.
DMDMi21431807.

Proteomic databases

MaxQBiP24386.
PaxDbiP24386.
PRIDEiP24386.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357749; ENSP00000350386; ENSG00000188419. [P24386-1]
ENST00000615443; ENSP00000484306; ENSG00000188419. [P24386-2]
GeneIDi1121.
KEGGihsa:1121.
UCSCiuc004eet.3. human. [P24386-1]
uc004eev.4. human. [P24386-2]

Organism-specific databases

CTDi1121.
GeneCardsiGC0XM085116.
GeneReviewsiCHM.
HGNCiHGNC:1940. CHM.
HPAiCAB016171.
HPA003231.
MIMi300390. gene.
303100. phenotype.
neXtProtiNX_P24386.
Orphaneti180. Choroideremia.
PharmGKBiPA26471.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5044.
GeneTreeiENSGT00530000063044.
HOGENOMiHOG000220905.
HOVERGENiHBG004961.
InParanoidiP24386.
OMAiQKNHASV.
OrthoDBiEOG7Q5HCQ.
PhylomeDBiP24386.
TreeFamiTF320813.

Miscellaneous databases

ChiTaRSiCHM. human.
GeneWikiiRab_escort_protein.
GenomeRNAii1121.
NextBioi4654.
PROiP24386.
SOURCEiSearch...

Gene expression databases

BgeeiP24386.
CleanExiHS_CHM.
GenevestigatoriP24386.

Family and domain databases

InterProiIPR018203. GDP_dissociation_inhibitor.
IPR001738. Rab_escort.
[Graphical view]
PfamiPF00996. GDI. 2 hits.
[Graphical view]
PIRSFiPIRSF016550. Rab_ger_ger_transf_A_euk. 1 hit.
PRINTSiPR00893. RABESCORT.
PR00891. RABGDIREP.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 2).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 289-653 (ISOFORM 1).
    Tissue: Retina.
  5. "Cloning of a gene that is rearranged in patients with choroideraemia."
    Cremers F.P.M., van de Pol D.J.R., van Kerkhoff L.P.M., Wieringa B., Ropers H.-H.
    Nature 347:674-677(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 338-653 (ISOFORM 1).
  6. "Detection and characterization of point mutations in the choroideremia candidate gene by PCR-SSCP analysis and direct DNA sequencing."
    van den Hurk J.A.J.M., van de Pol T.J.R., Molloy C.M., Brunsmann F., Ruther K., Zrenner E., Pinckers A.J.L.G., Pawlowitzki I.H., Bleeker-Wagemakers E.M., Wieringa B., Ropers H.-H., Cremers F.P.M.
    Am. J. Hum. Genet. 50:1195-1202(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 451-590.
  7. Cited for: SIMILARITY TO SMG P25A GDI.
  8. "Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes."
    Alexandrov K., Horiuchi H., Steele-Mortimer O., Seabra M.C., Zerial M.
    EMBO J. 13:5262-5273(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A AND RAB7A.
  9. "Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT complex and is regulated by geranylgeranyl pyrophosphate."
    Baron R.A., Seabra M.C.
    Biochem. J. 415:67-75(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-282 AND VAL-290.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Comprehensive mutation analysis (20 families) of the choroideremia gene reveals a missense variant that prevents the binding of REP1 with rab geranylgeranyl transferase."
    Esposito G., De Falco F., Tinto N., Testa F., Vitagliano L., Tandurella I.C., Iannone L., Rossi S., Rinaldi E., Simonelli F., Zagari A., Salvatore F.
    Hum. Mutat. 32:1460-1469(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABGGTA, VARIANT CHM ARG-507, CHARACTERIZATION OF VARIANT CHM ARG-507.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: VARIANT CHM LEU-471.
  14. "The functional effect of pathogenic mutations in Rab escort protein 1."
    Sergeev Y.V., Smaoui N., Sui R., Stiles D., Gordiyenko N., Strunnikova N., Macdonald I.M.
    Mutat. Res. 665:44-50(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CHM PRO-550.

Entry informationi

Entry nameiRAE1_HUMAN
AccessioniPrimary (citable) accession number: P24386
Secondary accession number(s): A1L4D2, O43732
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: June 6, 2002
Last modified: May 27, 2015
This is version 141 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.