Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P61106 (RAB14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-14
Gene names
Name:RAB14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes By similarity. Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion. Ref.17

Subunit structure

Interacts with KIF16B By similarity. Interacts with ZFYVE20. Ref.19

Subcellular location

Recycling endosome. Early endosome membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side By similarity. Golgi apparatustrans-Golgi network membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Recruited to recycling endosomes by DENND6A. Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.13 Ref.16 Ref.17

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence caution

The sequence CAI12361.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasmic vesicle
Endosome
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay Ref.19. Source: GOC

Golgi to endosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

embryo development

Inferred from sequence or structural similarity. Source: UniProtKB

endocytic recycling

Inferred from direct assay Ref.17. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular transport

Non-traceable author statement PubMed 15004230. Source: UniProtKB

membrane organization

Traceable author statement. Source: Reactome

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of protein localization

Inferred from direct assay Ref.17. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

vesicle-mediated transport

Non-traceable author statement PubMed 15004230. Source: UniProtKB

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi stack

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

intracellular

Inferred from direct assay. Source: LIFEdb

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

late endosome

Inferred from sequence or structural similarity. Source: UniProtKB

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear outer membrane-endoplasmic reticulum membrane network

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

phagocytic vesicle

Inferred from direct assay Ref.16. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome

Inferred from direct assay Ref.17. Source: UniProtKB

rough endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

trans-Golgi network transport vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGDP binding

Inferred from direct assay Ref.19. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.19. Source: UniProtKB

GTPase activity

Inferred from direct assay Ref.19. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

OCRLQ019683EBI-1056404,EBI-6148898

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 215214Ras-related protein Rab-14
PRO_0000121185

Regions

Nucleotide binding18 – 269GTP
Nucleotide binding66 – 705GTP
Nucleotide binding124 – 1274GTP
Nucleotide binding154 – 1563GTP
Motif40 – 489Effector region By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.12 Ref.14 Ref.18
Modified residue2151Cysteine methyl ester By similarity
Lipidation2131S-geranylgeranyl cysteine By similarity
Lipidation2151S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant41A → T. Ref.2 Ref.7 Ref.12
VAR_012986

Secondary structure

............................... 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61106 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: BC8A8B98FB9944AC

FASTA21523,897
        10         20         30         40         50         60 
MATAPYNYSY IFKYIIIGDM GVGKSCLLHQ FTEKKFMADC PHTIGVEFGT RIIEVSGQKI 

        70         80         90        100        110        120 
KLQIWDTAGQ ERFRAVTRSY YRGAAGALMV YDITRRSTYN HLSSWLTDAR NLTNPNTVII 

       130        140        150        160        170        180 
LIGNKADLEA QRDVTYEEAK QFAEENGLLF LEASAKTGEN VEDAFLEAAK KIYQNIQDGS 

       190        200        210 
LDLNAAESGV QHKPSAPQGG RLTSEPQPQR EGCGC 

« Hide

References

« Hide 'large scale' references
[1]"Human Rab14 cloning and intracellular localization to the biosynthetic/secretory trafficking pathway."
Proikas-Cezanne T., Jenkins J.R.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-4.
Tissue: Liver.
[2]"Cloning and characterization of human small GTPase Rab14."
Ren Y.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-4.
[3]"Screening and identification of HCV F protein-binding protein 1."
Huang Y.-P., Wang L., Cheng J.
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[5]"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].
Tissue: Melanoma.
[6]"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].
Tissue: Amygdala and Placenta.
[7]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-4.
Tissue: Brain.
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]"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].
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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: Placenta.
[12]Bienvenut W.V., Claeys D.
Submitted (FEB-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-24; 36-59; 62-72; 83-95; 97-132 AND 141-171, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma and Platelet.
[13]"Rab14 is part of the early endosomal clathrin-coated TGN microdomain."
Proikas-Cezanne T., Gaugel A., Frickey T., Nordheim A.
FEBS Lett. 580:5241-5246(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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].
[16]"Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
Seto S., Tsujimura K., Koide Y.
Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[17]"Rab14 and its exchange factor FAM116 link endocytic recycling and adherens junction stability in migrating cells."
Linford A., Yoshimura S., Nunes Bastos R., Langemeyer L., Gerondopoulos A., Rigden D.J., Barr F.A.
Dev. Cell 22:952-966(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
Eathiraj S., Pan X., Ritacco C., Lambright D.G.
Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-175 IN COMPLEX WITH GDP, INTERACTION WITH ZFYVE20.
[20]"Crystal structure of human RAB14."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-181 IN COMPLEX WITH GDP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF152463 mRNA. Translation: AAF00150.1.
AF203689 mRNA. Translation: AAF19400.1.
AY553875 mRNA. Translation: AAS64573.1.
AF112206 mRNA. Translation: AAF17194.1.
AL162081 mRNA. Translation: CAB82414.1.
AK023524 mRNA. Translation: BAB14598.1.
AK090889 mRNA. Translation: BAG52243.1.
AF498949 mRNA. Translation: AAM21097.1.
AL137068 Genomic DNA. Translation: CAD20124.1.
AL137068 Genomic DNA. Translation: CAI12361.1. Sequence problems.
CR457394 mRNA. Translation: CAG33675.1.
CH471090 Genomic DNA. Translation: EAW87487.1.
BC006081 mRNA. Translation: AAH06081.1.
RefSeqNP_057406.2. NM_016322.3.
UniGeneHs.371563.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z0FX-ray2.15A2-175[»]
4DRZX-ray2.30A1-181[»]
ProteinModelPortalP61106.
SMRP61106. Positions 7-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119605. 21 interactions.
DIPDIP-42491N.
IntActP61106. 10 interactions.
MINTMINT-2882831.
STRING9606.ENSP00000362946.

PTM databases

PhosphoSiteP61106.

Polymorphism databases

DMDM85700392.

Proteomic databases

PaxDbP61106.
PeptideAtlasP61106.
PRIDEP61106.

Protocols and materials databases

DNASU51552.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373840; ENSP00000362946; ENSG00000119396.
GeneID51552.
KEGGhsa:51552.
UCSCuc004blc.3. human.

Organism-specific databases

CTD51552.
GeneCardsGC09M123940.
HGNCHGNC:16524. RAB14.
HPAHPA026419.
MIM612673. gene.
neXtProtNX_P61106.
PharmGKBPA34104.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOVERGENHBG009351.
InParanoidP61106.
KOK07881.
OMAASCPHTI.
OrthoDBEOG7QK0CV.
PhylomeDBP61106.
TreeFamTF300032.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
SignaLinkP61106.

Gene expression databases

BgeeP61106.
CleanExHS_RAB14.
GenevestigatorP61106.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAB14. human.
EvolutionaryTraceP61106.
GeneWikiRAB14.
GenomeRNAi51552.
NextBio55334.
PROP61106.
SOURCESearch...

Entry information

Entry nameRAB14_HUMAN
AccessionPrimary (citable) accession number: P61106
Secondary accession number(s): B3KR31 expand/collapse secondary AC list , P35287, Q5JVD4, Q6Q7K5, Q969L0, Q9UI11
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 120 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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