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Q3YEC7 (RABL6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rab-like protein 6
Alternative name(s):
GTP-binding protein Parf
Partner of ARF
Rab-like protein 1
Short name=RBEL1
Gene names
Name:RABL6
Synonyms:C9orf86, PARF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May enhance cellular proliferation. May reduce growth inhibitory activity of CDKN2A. Ref.1

Subcellular location

Isoform 1: Cytoplasm. Note: Predominantly cytoplasmic. Ref.1 Ref.2 Ref.3

Isoform 3: Nucleus. Note: Predominantly nuclear. Ref.1 Ref.2 Ref.3

Post-translational modification

Isoform 1 is O-glycosylated, while other isoforms are not. Ref.2

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence caution

The sequence AAH02945.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH21095.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH35786.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB14408.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB55213.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MDFIQ997502EBI-742029,EBI-724076
SPINK7P580623EBI-742029,EBI-1182445

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3YEC7-1)

Also known as: RBEL1A;

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.
Note: Predominant isoform. Overexpressed in about 67% of primary breast tumors.
Isoform 2 (identifier: Q3YEC7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     199-199: D → DS
Isoform 3 (identifier: Q3YEC7-3)

Also known as: RBEL1B;

The sequence of this isoform differs from the canonical sequence as follows:
     361-729: LFGTSPATEA...HPGGGDYEEL → PPPWGWRLRG...AYGSASGREP
Note: No experimental confirmation available.
Isoform 4 (identifier: Q3YEC7-4)

Also known as: RBEL1D;

The sequence of this isoform differs from the canonical sequence as follows:
     236-264: RETLLRQLETNQLDMDATLEELSVQQETE → VSTHHVGWSGCWSLTSFQVSPV
     265-729: Missing.
Isoform 5 (identifier: Q3YEC7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     199-199: D → DS
     236-264: RETLLRQLETNQLDMDATLEELSVQQETE → VSTHHVGWSGCWSLTSFQVSPV
     265-729: Missing.
Isoform 6 (identifier: Q3YEC7-6)

Also known as: RBEL1C;

The sequence of this isoform differs from the canonical sequence as follows:
     236-302: RETLLRQLET...PSPGSQSPVV → KDVRLAQERG...SSPLLSCSIP
     303-729: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Rab-like protein 6
PRO_0000274223

Regions

Nucleotide binding50 – 578GTP Potential
Nucleotide binding100 – 1045GTP Potential
Nucleotide binding177 – 1793GTP Potential
Region39 – 279241Small GTPase-like
Region655 – 69339Interaction with CDKN2A
Compositional bias293 – 38492Pro-rich
Compositional bias645 – 68541Lys-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16
Modified residue4021Phosphoserine Ref.10
Modified residue4251Phosphoserine Ref.12 Ref.13 Ref.15
Modified residue4271Phosphoserine Ref.12 Ref.13 Ref.15
Modified residue4701Phosphoserine By similarity
Modified residue4711Phosphoserine By similarity
Modified residue5771Phosphoserine Ref.9
Modified residue5961Phosphoserine Ref.9 Ref.13 Ref.15
Modified residue5991Phosphothreonine Ref.9 Ref.13 Ref.15

Natural variations

Alternative sequence1991D → DS in isoform 2 and isoform 5.
VSP_022646
Alternative sequence236 – 30267RETLL…QSPVV → KDVRLAQERGCAVVLVSEEV RMPAGWDCCWGRLGWKEGGS QTCPVPALLGRPLLPAEPSP HHWVDYSLESSPLLSCSIP in isoform 6.
VSP_042559
Alternative sequence236 – 26429RETLL…QQETE → VSTHHVGWSGCWSLTSFQVS PV in isoform 4 and isoform 5.
VSP_022647
Alternative sequence265 – 729465Missing in isoform 4 and isoform 5.
VSP_022648
Alternative sequence303 – 729427Missing in isoform 6.
VSP_042560
Alternative sequence361 – 729369LFGTS…DYEEL → PPPWGWRLRGALGRRGQWPP WGGGRACHCLGRHLPLYHRL CRCPVAAVCASELEEAGHWW SPGWALQVLGLQAQCEPALQ EGRGQLASARLGGHPGPLGA EPPVFLRDVTEAQEGPVRVC LQRLGRGRLAVGCALPRHLL ALRAHLGPQHAYGSASGREP in isoform 3.
VSP_022649
Natural variant3821E → Q. Ref.1 Ref.5 Ref.6 Ref.7
Corresponds to variant rs2811741 [ dbSNP | Ensembl ].
VAR_030210

Experimental info

Sequence conflict1371Y → C in BAB14408. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RBEL1A) [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: 6C3FDB38C7FD7D59

FASTA72979,549
        10         20         30         40         50         60 
MFSALKKLVG SDQAPGRDKN IPAGLQSMNQ ALQRRFAKGV QYNMKIVIRG DRNTGKTALW 

        70         80         90        100        110        120 
HRLQGRPFVE EYIPTQEIQV TSIHWSYKTT DDIVKVEVWD VVDKGKCKKR GDGLKMENDP 

       130        140        150        160        170        180 
QEAESEMALD AEFLDVYKNC NGVVMMFDIT KQWTFNYILR ELPKVPTHVP VCVLGNYRDM 

       190        200        210        220        230        240 
GEHRVILPDD VRDFIDNLDR PPGSSYFRYA ESSMKNSFGL KYLHKFFNIP FLQLQRETLL 

       250        260        270        280        290        300 
RQLETNQLDM DATLEELSVQ QETEDQNYGI FLEMMEARSR GHASPLAANG QSPSPGSQSP 

       310        320        330        340        350        360 
VVPAGAVSTG SSSPGTPQPA PQLPLNAAPP SSVPPVPPSE ALPPPACPSA PAPRRSIISR 

       370        380        390        400        410        420 
LFGTSPATEA APPPPEPVPA AEGPATVQSV EDFVPDDRLD RSFLEDTTPA RDEKKVGAKA 

       430        440        450        460        470        480 
AQQDSDSDGE ALGGNPMVAG FQDDVDLEDQ PRGSPPLPAG PVPSQDITLS SEEEAEVAAP 

       490        500        510        520        530        540 
TKGPAPAPQQ CSEPETKWSS IPASKPRRGT APTRTAAPPW PGGVSVRTGP EKRSSTRPPA 

       550        560        570        580        590        600 
EMEPGKGEQA SSSESDPEGP IAAQMLSFVM DDPDFESEGS DTQRRADDFP VRDDPSDVTD 

       610        620        630        640        650        660 
EDEGPAEPPP PPKLPLPAFR LKNDSDLFGL GLEEAGPKES SEEGKEGKTP SKEKKKKKKK 

       670        680        690        700        710        720 
GKEEEEKAAK KKSKHKKSKD KEEGKEERRR RQQRPPRSRE RTAADELEAF LGGGAPGGRH 


PGGGDYEEL 

« Hide

Isoform 2 [UniParc].

Checksum: 76CED43E38D6167F
Show »

FASTA73079,636
Isoform 3 (RBEL1B) [UniParc].

Checksum: ABB2BD2287F358BF
Show »

FASTA52057,397
Isoform 4 (RBEL1D) [UniParc].

Checksum: B086094A0AA8FCB0
Show »

FASTA25729,585
Isoform 5 [UniParc].

Checksum: 99980CF4224BDA2F
Show »

FASTA25829,672
Isoform 6 (RBEL1C) [UniParc].

Checksum: 64FCC800FAB9C14E
Show »

FASTA31435,809

References

« Hide 'large scale' references
[1]"Identification of novel ARF binding proteins by two-hybrid screening."
Tompkins V., Hagen J., Zediak V.P., Quelle D.E.
Cell Cycle 5:641-646(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-382, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDKN2A.
[2]"RBEL1 is a novel gene that encodes a nucleocytoplasmic Ras superfamily GTP-binding protein and is overexpressed in breast cancer."
Montalbano J., Jin W., Sheikh M.S., Huang Y.
J. Biol. Chem. 282:37640-37649(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING, GLYCOSYLATION, SUBCELLULAR LOCATION.
[3]"Identification and characterization of RBEL1 subfamily of GTPases in the Ras superfamily involved in cell growth regulation."
Montalbano J., Lui K., Sheikh M.S., Huang Y.
J. Biol. Chem. 284:18129-18142(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 6), SUBCELLULAR LOCATION.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Lin L., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Wen S., Zhou G., Yang S.
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-382.
[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] (ISOFORMS 1; 2 AND 3), VARIANT GLN-382.
Tissue: Brain and Kidney.
[7]"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. expand/collapse author list , 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] OF 45-729 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-729 (ISOFORM 1), VARIANT GLN-382.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 251-719.
Tissue: Brain.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577; SER-596 AND THR-599, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-427; SER-596 AND THR-599, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-427; SER-596 AND THR-599, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ141240 mRNA. Translation: AAZ73768.1.
EF156752 mRNA. Translation: ABO84837.1.
EF156753 mRNA. Translation: ABO84838.1.
GQ169126 mRNA. Translation: ACS45171.1.
GQ169127 mRNA. Translation: ACS45172.1.
AL355987 Genomic DNA. Translation: CAI12685.1.
AL355987 Genomic DNA. Translation: CAI12686.1.
DQ099383 mRNA. Translation: AAZ13759.1.
BC002945 mRNA. Translation: AAH02945.2. Different initiation.
BC021095 mRNA. Translation: AAH21095.2. Different initiation.
BC035786 mRNA. Translation: AAH35786.1. Different initiation.
AK023107 mRNA. Translation: BAB14408.1. Different initiation.
AK027586 mRNA. Translation: BAB55213.1. Different initiation.
AL713707 mRNA. Translation: CAD28504.1.
CCDSCCDS48058.1. [Q3YEC7-1]
CCDS55352.1. [Q3YEC7-2]
CCDS55353.1. [Q3YEC7-6]
RefSeqNP_001167459.1. NM_001173988.1. [Q3YEC7-2]
NP_001167460.1. NM_001173989.2. [Q3YEC7-6]
NP_078994.3. NM_024718.4. [Q3YEC7-1]
UniGeneHs.370555.

3D structure databases

ProteinModelPortalQ3YEC7.
SMRQ3YEC7. Positions 41-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120812. 20 interactions.
IntActQ3YEC7. 5 interactions.

PTM databases

PhosphoSiteQ3YEC7.

Polymorphism databases

DMDM125957950.

Proteomic databases

MaxQBQ3YEC7.
PaxDbQ3YEC7.
PRIDEQ3YEC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311502; ENSP00000311134; ENSG00000196642. [Q3YEC7-1]
ENST00000357466; ENSP00000350056; ENSG00000196642. [Q3YEC7-3]
ENST00000371663; ENSP00000360727; ENSG00000196642. [Q3YEC7-2]
ENST00000371671; ENSP00000360736; ENSG00000196642. [Q3YEC7-6]
GeneID55684.
KEGGhsa:55684.
UCSCuc004cjh.3. human. [Q3YEC7-6]
uc004cji.1. human. [Q3YEC7-1]
uc004cjj.1. human. [Q3YEC7-2]
uc004cjm.2. human. [Q3YEC7-4]

Organism-specific databases

CTD55684.
GeneCardsGC09P139702.
HGNCHGNC:24703. RABL6.
HPAHPA044037.
MIM610615. gene.
neXtProtNX_Q3YEC7.
PharmGKBPA134868176.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG138310.
HOGENOMHOG000015428.
HOVERGENHBG080325.
InParanoidQ3YEC7.
OMAGRACHCL.
PhylomeDBQ3YEC7.
TreeFamTF313974.

Gene expression databases

ArrayExpressQ3YEC7.
BgeeQ3YEC7.
GenevestigatorQ3YEC7.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR001806. Small_GTPase.
[Graphical view]
PfamPF08477. Miro. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSC9orf86. human.
GeneWikiC9orf86.
GenomeRNAi55684.
NextBio60481.
PROQ3YEC7.
SOURCESearch...

Entry information

Entry nameRABL6_HUMAN
AccessionPrimary (citable) accession number: Q3YEC7
Secondary accession number(s): A8QVZ7 expand/collapse secondary AC list , A8QVZ8, C6K8I4, C6K8I5, Q4F968, Q5T5R7, Q8IWK1, Q8TCL4, Q8WU94, Q96SR8, Q9BU21, Q9H935
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: July 9, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM