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P61020

- RAB5B_HUMAN

UniProt

P61020 - RAB5B_HUMAN

Protein

Ras-related protein Rab-5B

Gene

RAB5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (26 Apr 2004)
      Previous versions | rss
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    Functioni

    Protein transport. Probably involved in vesicular traffic By similarity.By similarity

    Enzyme regulationi

    Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi27 – 359GTP
    Nucleotide bindingi75 – 795GTPBy similarity
    Nucleotide bindingi133 – 1364GTP
    Nucleotide bindingi163 – 1653GTP

    GO - Molecular functioni

    1. GDP binding Source: UniProtKB
    2. GTPase activity Source: ProtInc
    3. GTP binding Source: UniProtKB-KW
    4. GTP-dependent protein binding Source: UniProtKB
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation Source: UniProt
    2. endosome organization Source: Ensembl
    3. GTP catabolic process Source: GOC
    4. protein transport Source: UniProtKB-KW
    5. regulation of endocytosis Source: Ensembl
    6. small GTPase mediated signal transduction Source: InterPro

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-5B
    Gene namesi
    Name:RAB5B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9784. RAB5B.

    Subcellular locationi

    Cell membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication. Early endosome membrane 1 Publication; Lipid-anchor 1 Publication. Melanosome 1 Publication
    Note: Enriched in stage I melanosomes.

    GO - Cellular componenti

    1. early endosome membrane Source: UniProtKB-SubCell
    2. endocytic vesicle Source: Ensembl
    3. endosome Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. intracellular Source: LIFEdb
    6. melanosome Source: UniProtKB-SubCell
    7. membrane Source: ProtInc
    8. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi34 – 341S → N: Constitutively inactivated. Strongly reduces interaction with RIN2. 1 Publication
    Mutagenesisi79 – 791Q → L: Constitutively active. 1 Publication

    Organism-specific databases

    PharmGKBiPA34144.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 215214Ras-related protein Rab-5BPRO_0000121107Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Lipidationi212 – 2121S-geranylgeranyl cysteineBy similarity
    Lipidationi213 – 2131S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Prenylation

    Proteomic databases

    MaxQBiP61020.
    PaxDbiP61020.
    PRIDEiP61020.

    PTM databases

    PhosphoSiteiP61020.

    Expressioni

    Gene expression databases

    BgeeiP61020.
    CleanExiHS_RAB5B.
    GenevestigatoriP61020.

    Organism-specific databases

    HPAiCAB010224.

    Interactioni

    Subunit structurei

    Binds EEA1. Interacts with RIN2 and RIN3, which probably regulate its pathway, possibly by acting as GEFs.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EEA1Q150753EBI-399401,EBI-298113
    LRRK2Q5S0074EBI-399401,EBI-5323863

    Protein-protein interaction databases

    BioGridi111807. 26 interactions.
    IntActiP61020. 8 interactions.
    MINTiMINT-3022222.
    STRINGi9606.ENSP00000353444.

    Structurei

    Secondary structure

    1
    215
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 268
    Helixi33 – 4210
    Beta strandi54 – 563
    Beta strandi58 – 625
    Beta strandi69 – 746
    Helixi83 – 853
    Helixi86 – 905
    Beta strandi95 – 1017
    Helixi105 – 12117
    Beta strandi127 – 1337
    Helixi135 – 1406
    Helixi145 – 15410
    Beta strandi158 – 1614
    Turni164 – 1663
    Helixi170 – 18011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HEIX-ray1.55A/B15-191[»]
    ProteinModelPortaliP61020.
    SMRiP61020. Positions 17-183.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61020.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi49 – 579Effector regionSequence Analysis

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOVERGENiHBG009351.
    InParanoidiP61020.
    KOiK07888.
    OMAiPKNDGAN.
    OrthoDBiEOG77DJ7M.
    PhylomeDBiP61020.
    TreeFamiTF300199.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view]
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00175. RAB. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51419. RAB. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P61020-1) [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

    MTSRSTARPN GQPQASKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEYQE    50
    STIGAAFLTQ SVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY 100
    DITNQETFAR AKTWVKELQR QASPSIVIAL AGNKADLANK RMVEYEEAQA 150
    YADDNSLLFM ETSAKTAMNV NDLFLAIAKK LPKSEPQNLG GAAGRSRGVD 200
    LHEQSQQNKS QCCSN 215
    Length:215
    Mass (Da):23,707
    Last modified:April 26, 2004 - v1
    Checksum:iD47AD834BCF8B591
    GO
    Isoform 2 (identifier: P61020-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         106-146: Missing.

    Show »
    Length:174
    Mass (Da):19,090
    Checksum:i90D1C43B99761B6E
    GO

    Sequence cautioni

    The sequence AAH40143.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei106 – 14641Missing in isoform 2. 1 PublicationVSP_045301Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54871 mRNA. Translation: CAA38653.1.
    AF498937 mRNA. Translation: AAM21085.1.
    AK292597 mRNA. Translation: BAF85286.1.
    AK296517 mRNA. Translation: BAG59149.1.
    BX537408 mRNA. Translation: CAD97650.1.
    AC034102 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96862.1.
    CH471054 Genomic DNA. Translation: EAW96864.1.
    BC032740 mRNA. Translation: AAH32740.1.
    BC040143 mRNA. Translation: AAH40143.1. Different initiation.
    BC050558 mRNA. Translation: AAH50558.2.
    BC056422 mRNA. Translation: AAH56422.2.
    BC065298 mRNA. Translation: AAH65298.2.
    CCDSiCCDS58244.1. [P61020-2]
    CCDS8900.1. [P61020-1]
    PIRiA43925.
    RefSeqiNP_001238965.1. NM_001252036.1. [P61020-1]
    NP_001238966.1. NM_001252037.1. [P61020-2]
    NP_002859.1. NM_002868.3. [P61020-1]
    XP_005269108.1. XM_005269051.1. [P61020-1]
    XP_005269109.1. XM_005269052.1. [P61020-1]
    UniGeneiHs.157659.

    Genome annotation databases

    EnsembliENST00000360299; ENSP00000353444; ENSG00000111540. [P61020-1]
    ENST00000448789; ENSP00000391319; ENSG00000111540. [P61020-2]
    ENST00000553116; ENSP00000450168; ENSG00000111540. [P61020-1]
    GeneIDi5869.
    KEGGihsa:5869.
    UCSCiuc001siv.3. human. [P61020-1]
    uc010spz.2. human.

    Polymorphism databases

    DMDMi46577637.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54871 mRNA. Translation: CAA38653.1 .
    AF498937 mRNA. Translation: AAM21085.1 .
    AK292597 mRNA. Translation: BAF85286.1 .
    AK296517 mRNA. Translation: BAG59149.1 .
    BX537408 mRNA. Translation: CAD97650.1 .
    AC034102 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96862.1 .
    CH471054 Genomic DNA. Translation: EAW96864.1 .
    BC032740 mRNA. Translation: AAH32740.1 .
    BC040143 mRNA. Translation: AAH40143.1 . Different initiation.
    BC050558 mRNA. Translation: AAH50558.2 .
    BC056422 mRNA. Translation: AAH56422.2 .
    BC065298 mRNA. Translation: AAH65298.2 .
    CCDSi CCDS58244.1. [P61020-2 ]
    CCDS8900.1. [P61020-1 ]
    PIRi A43925.
    RefSeqi NP_001238965.1. NM_001252036.1. [P61020-1 ]
    NP_001238966.1. NM_001252037.1. [P61020-2 ]
    NP_002859.1. NM_002868.3. [P61020-1 ]
    XP_005269108.1. XM_005269051.1. [P61020-1 ]
    XP_005269109.1. XM_005269052.1. [P61020-1 ]
    UniGenei Hs.157659.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HEI X-ray 1.55 A/B 15-191 [» ]
    ProteinModelPortali P61020.
    SMRi P61020. Positions 17-183.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111807. 26 interactions.
    IntActi P61020. 8 interactions.
    MINTi MINT-3022222.
    STRINGi 9606.ENSP00000353444.

    PTM databases

    PhosphoSitei P61020.

    Polymorphism databases

    DMDMi 46577637.

    Proteomic databases

    MaxQBi P61020.
    PaxDbi P61020.
    PRIDEi P61020.

    Protocols and materials databases

    DNASUi 5869.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360299 ; ENSP00000353444 ; ENSG00000111540 . [P61020-1 ]
    ENST00000448789 ; ENSP00000391319 ; ENSG00000111540 . [P61020-2 ]
    ENST00000553116 ; ENSP00000450168 ; ENSG00000111540 . [P61020-1 ]
    GeneIDi 5869.
    KEGGi hsa:5869.
    UCSCi uc001siv.3. human. [P61020-1 ]
    uc010spz.2. human.

    Organism-specific databases

    CTDi 5869.
    GeneCardsi GC12P056368.
    HGNCi HGNC:9784. RAB5B.
    HPAi CAB010224.
    MIMi 179514. gene.
    neXtProti NX_P61020.
    PharmGKBi PA34144.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOVERGENi HBG009351.
    InParanoidi P61020.
    KOi K07888.
    OMAi PKNDGAN.
    OrthoDBi EOG77DJ7M.
    PhylomeDBi P61020.
    TreeFami TF300199.

    Miscellaneous databases

    ChiTaRSi RAB5B. human.
    EvolutionaryTracei P61020.
    GeneWikii RAB5B.
    GenomeRNAii 5869.
    NextBioi 22794.
    PROi P61020.
    SOURCEi Search...

    Gene expression databases

    Bgeei P61020.
    CleanExi HS_RAB5B.
    Genevestigatori P61020.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00175. RAB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and subcellular localization of human rab5b, a new member of the ras-related superfamily of GTPases."
      Wilson D.B., Wilson M.P.
      J. Clin. Invest. 89:996-1005(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORMS 1 AND 2).
      Tissue: Testis and Thalamus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Endometrium.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1).
      Tissue: Eye, PNS and Skin.
    8. Cited for: INTERACTION WITH EEA1.
    9. "A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5."
      Saito K., Murai J., Kajiho H., Kontani K., Kurosu H., Katada T.
      J. Biol. Chem. 277:3412-3418(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RIN2 AND RIN3, MUTAGENESIS OF SER-34 AND GLN-79.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Crystal structure of human RAB5B in complex with GDP."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 15-191 IN COMPLEX WITH GDP.

    Entry informationi

    Entry nameiRAB5B_HUMAN
    AccessioniPrimary (citable) accession number: P61020
    Secondary accession number(s): A8K982
    , B4DKD7, P35239, P35277, Q6PIK9, Q86TH0, Q8IXL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: April 26, 2004
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3