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Protein

Rab proteins geranylgeranyltransferase component A 2

Gene

CHML

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Substrate-binding subunit (component A) of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Less effective than CHM in supporting prenylation of Rab3 family.3 Publications

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • oxidoreductase activity Source: InterPro
  • Rab GTPase binding Source: UniProtKB

GO - Biological processi

  • intracellular protein transport Source: InterPro
  • protein geranylgeranylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Rab proteins geranylgeranyltransferase component A 2
Alternative name(s):
Choroideremia-like protein
Rab escort protein 2
Short name:
REP-2
Gene namesi
Name:CHML
Synonyms:REP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1941. CHML.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • Rab-protein geranylgeranyltransferase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26472.

Polymorphism and mutation databases

BioMutaiCHML.
DMDMi47117837.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 656656Rab proteins geranylgeranyltransferase component A 2PRO_0000056689Add
BLAST

Proteomic databases

EPDiP26374.
MaxQBiP26374.
PaxDbiP26374.
PRIDEiP26374.

PTM databases

iPTMnetiP26374.
PhosphoSiteiP26374.

Expressioni

Gene expression databases

BgeeiP26374.
CleanExiHS_CHML.
GenevisibleiP26374. HS.

Organism-specific databases

HPAiHPA029628.

Interactioni

Subunit structurei

Monomer. Heterotrimer composed of RABGGTA, RABGGTB and CHML; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHML (component A) mediates Rab protein binding. Interacts with RAB1A, RAB7A and RAB27A, but has much lower affinity for RAB1A, RAB7A and RAB27A than CHM.3 Publications

GO - Molecular functioni

  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107546. 21 interactions.
IntActiP26374. 1 interaction.
STRINGi9606.ENSP00000355511.

Structurei

3D structure databases

ProteinModelPortaliP26374.
SMRiP26374. Positions 3-108, 214-620.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab GDI family.Curated

Phylogenomic databases

eggNOGiKOG4405. Eukaryota.
COG5044. LUCA.
GeneTreeiENSGT00530000063044.
HOGENOMiHOG000231282.
HOVERGENiHBG004961.
InParanoidiP26374.
OMAiYCLRHKV.
OrthoDBiEOG7Q5HCQ.
PhylomeDBiP26374.
TreeFamiTF320813.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR018203. 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.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

P26374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADNLPTEFD VVIIGTGLPE SILAAACSRS GQRVLHIDSR SYYGGNWASF
60 70 80 90 100
SFSGLLSWLK EYQQNNDIGE ESTVVWQDLI HETEEAITLR KKDETIQHTE
110 120 130 140 150
AFCYASQDME DNVEEIGALQ KNPSLGVSNT FTEVLDSALP EESQLSYFNS
160 170 180 190 200
DEMPAKHTQK SDTEISLEVT DVEESVEKEK YCGDKTCMHT VSDKDGDKDE
210 220 230 240 250
SKSTVEDKAD EPIRNRITYS QIVKEGRRFN IDLVSKLLYS QGLLIDLLIK
260 270 280 290 300
SDVSRYVEFK NVTRILAFRE GKVEQVPCSR ADVFNSKELT MVEKRMLMKF
310 320 330 340 350
LTFCLEYEQH PDEYQAFRQC SFSEYLKTKK LTPNLQHFVL HSIAMTSESS
360 370 380 390 400
CTTIDGLNAT KNFLQCLGRF GNTPFLFPLY GQGEIPQGFC RMCAVFGGIY
410 420 430 440 450
CLRHKVQCFV VDKESGRCKA IIDHFGQRIN AKYFIVEDSY LSEETCSNVQ
460 470 480 490 500
YKQISRAVLI TDQSILKTDL DQQTSILIVP PAEPGACAVR VTELCSSTMT
510 520 530 540 550
CMKDTYLVHL TCSSSKTARE DLESVVKKLF TPYTETEINE EELTKPRLLW
560 570 580 590 600
ALYFNMRDSS GISRSSYNGL PSNVYVCSGP DCGLGNEHAV KQAETLFQEI
610 620 630 640 650
FPTEEFCPPP PNPEDIIFDG DDKQPEAPGT NNVVMAKLES SEESKNLESP

EKHLQN
Length:656
Mass (Da):74,071
Last modified:May 10, 2004 - v2
Checksum:i478481966E30BE49
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031C → P in CAA45979 (PubMed:1301160).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64728 mRNA. Translation: CAA45979.1.
AF482426 Genomic DNA. Translation: AAO15716.1.
AK314125 mRNA. Translation: BAG36816.1.
AL133390 Genomic DNA. No translation available.
CH471098 Genomic DNA. Translation: EAW70100.1.
BC117360 mRNA. Translation: AAI17361.1.
CCDSiCCDS31073.1.
PIRiS23754. S38787.
RefSeqiNP_001812.2. NM_001821.3.
UniGeneiHs.654545.

Genome annotation databases

EnsembliENST00000366553; ENSP00000355511; ENSG00000203668.
GeneIDi1122.
KEGGihsa:1122.
UCSCiuc001hzd.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64728 mRNA. Translation: CAA45979.1.
AF482426 Genomic DNA. Translation: AAO15716.1.
AK314125 mRNA. Translation: BAG36816.1.
AL133390 Genomic DNA. No translation available.
CH471098 Genomic DNA. Translation: EAW70100.1.
BC117360 mRNA. Translation: AAI17361.1.
CCDSiCCDS31073.1.
PIRiS23754. S38787.
RefSeqiNP_001812.2. NM_001821.3.
UniGeneiHs.654545.

3D structure databases

ProteinModelPortaliP26374.
SMRiP26374. Positions 3-108, 214-620.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107546. 21 interactions.
IntActiP26374. 1 interaction.
STRINGi9606.ENSP00000355511.

PTM databases

iPTMnetiP26374.
PhosphoSiteiP26374.

Polymorphism and mutation databases

BioMutaiCHML.
DMDMi47117837.

Proteomic databases

EPDiP26374.
MaxQBiP26374.
PaxDbiP26374.
PRIDEiP26374.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366553; ENSP00000355511; ENSG00000203668.
GeneIDi1122.
KEGGihsa:1122.
UCSCiuc001hzd.4. human.

Organism-specific databases

CTDi1122.
GeneCardsiCHML.
HGNCiHGNC:1941. CHML.
HPAiHPA029628.
MIMi118825. gene.
neXtProtiNX_P26374.
PharmGKBiPA26472.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4405. Eukaryota.
COG5044. LUCA.
GeneTreeiENSGT00530000063044.
HOGENOMiHOG000231282.
HOVERGENiHBG004961.
InParanoidiP26374.
OMAiYCLRHKV.
OrthoDBiEOG7Q5HCQ.
PhylomeDBiP26374.
TreeFamiTF320813.

Miscellaneous databases

GeneWikiiCHML_(gene).
GenomeRNAii1122.
NextBioi4658.
PROiP26374.
SOURCEiSearch...

Gene expression databases

BgeeiP26374.
CleanExiHS_CHML.
GenevisibleiP26374. HS.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR018203. 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.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An autosomal homologue of the choroideremia gene colocalizes with the Usher syndrome type II locus on the distal part of chromosome 1q."
    Cremers F.P.M., Molloy C.M., van de Pol D.J.R., van den Hurk J.A.J.M., Bach I., Geurts van Kessel A.H.M., Ropers H.-H.
    Hum. Mol. Genet. 1:71-75(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Different structural organization of the encephalopsin gene in man and mouse."
    Kasper G., Taudien S., Staub E., Mennerich D., Rieder M., Hinzmann B., Dahl E., Schwidetzky U., Rosenthal A., Rump A.
    Gene 295:27-32(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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: Hippocampus.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Brain.
  7. "REP-2, a Rab escort protein encoded by the choroideremia-like gene."
    Cremers F.P.M., Armstrong S.A., Seabra M.C., Brown M.S., Goldstein J.L.
    J. Biol. Chem. 269:2111-2117(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  8. "Expression of mammalian Rab Escort protein-1 and -2 in yeast Saccharomyces cerevisiae."
    Sidorovitch V., Niculae A., Kan N., Ceacareanu A.C., Alexandrov K.
    Protein Expr. Purif. 26:50-58(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION.
  9. "Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease."
    Rak A., Pylypenko O., Niculae A., Pyatkov K., Goody R.S., Alexandrov K.
    Cell 117:749-760(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAB1A; RAB7A AND RAB27A, SUBUNIT.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRAE2_HUMAN
AccessioniPrimary (citable) accession number: P26374
Secondary accession number(s): B2RAB9, Q17RE0, Q9H1Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 10, 2004
Last modified: March 16, 2016
This is version 131 of the entry and version 2 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

Miscellaneous

Substitutes for REP-1 thereby preventing widespread tissue abnormalities in patients with choroideremia who lack REP-1.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.