Skip Header

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

Q9H1K0

- RBNS5_HUMAN

UniProt

Q9H1K0 - RBNS5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Rabenosyn-5

Gene

ZFYVE20

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

Functioni

Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3).3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri14 – 3724C2H2-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri157 – 260104FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. endosomal transport Source: UniProtKB
  3. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Rabenosyn-5
Alternative name(s):
110 kDa protein
FYVE finger-containing Rab5 effector protein rabenosyn-5
Zinc finger FYVE domain-containing protein 20
Gene namesi
Name:ZFYVE20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:20759. ZFYVE20.

Subcellular locationi

GO - Cellular componenti

  1. endosome Source: UniProtKB
  2. endosome membrane Source: Reactome
  3. intracellular membrane-bounded organelle Source: HPA
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi626 – 6283NPF → APA: Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 662-APA-664. 1 Publication
Mutagenesisi662 – 6643NPF → APA: Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 626-APA-628. 1 Publication

Organism-specific databases

PharmGKBiPA134959491.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 784783Rabenosyn-5PRO_0000098711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation, Lipoprotein

Proteomic databases

MaxQBiQ9H1K0.
PaxDbiQ9H1K0.
PRIDEiQ9H1K0.

PTM databases

PhosphoSiteiQ9H1K0.

Expressioni

Gene expression databases

BgeeiQ9H1K0.
CleanExiHS_ZFYVE20.
ExpressionAtlasiQ9H1K0. baseline and differential.
GenevestigatoriQ9H1K0.

Organism-specific databases

HPAiHPA044878.

Interactioni

Subunit structurei

Interacts with EHD1, RAB4A, RAB5A, RAB14, RAB22A, RAB24 and VPS45. Binds simultaneously to RAB4A and RAB5A in vitro. Interacts with RAB4A and RAB5A that has been activated by GTP binding.4 Publications

Protein-protein interaction databases

BioGridi122084. 15 interactions.
IntActiQ9H1K0. 5 interactions.
MINTiMINT-2817361.
STRINGi9606.ENSP00000253699.

Structurei

Secondary structure

1
784
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi458 – 47518Combined sources
Helixi479 – 50022Combined sources
Helixi736 – 75520Combined sources
Helixi759 – 77921Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZMX-ray1.50A458-503[»]
1Z0JX-ray1.32B728-784[»]
1Z0KX-ray1.92B/D440-503[»]
ProteinModelPortaliQ9H1K0.
SMRiQ9H1K0. Positions 154-190, 441-501, 734-784.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H1K0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati496 – 51520UIMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 263164Necessary for the correct targeting to endosomesAdd
BLAST
Regioni264 – 784521Necessary for the interaction with EHD1Add
BLAST
Regioni264 – 500237Necessary for the interaction with RAB4AAdd
BLAST
Regioni627 – 784158Necessary for the interaction with RAB5AAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili378 – 41437Sequence AnalysisAdd
BLAST
Coiled coili472 – 53160Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi204 – 23936Ser-richAdd
BLAST
Compositional biasi665 – 6728Poly-Glu

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation
Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri14 – 3724C2H2-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri157 – 260104FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG257999.
GeneTreeiENSGT00390000007159.
HOGENOMiHOG000154082.
HOVERGENiHBG067237.
InParanoidiQ9H1K0.
KOiK12481.
OMAiKLRLCME.
OrthoDBiEOG76MK7V.
PhylomeDBiQ9H1K0.
TreeFamiTF106125.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR021565. Rbsn.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF11464. Rbsn. 2 hits.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS50178. ZF_FYVE. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 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: Q9H1K0-1) [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
MASLDDPGEV REGFLCPLCL KDLQSFYQLH SHYEEEHSGE DRDVKGQIKS
60 70 80 90 100
LVQKAKKAKD RLLKREGDDR AESGTQGYES FSYGGVDPYM WEPQELGAVR
110 120 130 140 150
SHLSDFKKHR AARIDHYVVE VNKLIIRLEK LTAFDRTNTE SAKIRAIEKS
160 170 180 190 200
VVPWVNDQDV PFCPDCGNKF SIRNRRHHCR LCGSIMCKKC MELISLPLAN
210 220 230 240 250
KLTSASKESL STHTSPSQSP NSVHGSRRGS ISSMSSVSSV LDEKDDDRIR
260 270 280 290 300
CCTHCKDTLL KREQQIDEKE HTPDIVKLYE KLRLCMEKVD QKAPEYIRMA
310 320 330 340 350
ASLNAGETTY SLEHASDLRV EVQKVYELID ALSKKILTLG LNQDPPPHPS
360 370 380 390 400
NLRLQRMIRY SATLFVQEKL LGLMSLPTKE QFEELKKKRK EEMERKRAVE
410 420 430 440 450
RQAALESQRR LEERQSGLAS RAANGEVASL RRGPAPLRKA EGWLPLSGGQ
460 470 480 490 500
GQSEDSDPLL QQIHNITSFI RQAKAAGRMD EVRTLQENLR QLQDEYDQQQ
510 520 530 540 550
TEKAIELSRR QAEEEDLQRE QLQMLREREL EREREQFRVA SLHTRTRSLD
560 570 580 590 600
FREIGPFQLE PSREPRTHLA YALDLGSSPV PSSTAPKTPS LSSTQPTRVW
610 620 630 640 650
SGPPAVGQER LPQSSMPQQH EGPSLNPFDE EDLSSPMEEA TTGPPAAGVS
660 670 680 690 700
LDPSARILKE YNPFEEEDEE EEAVAGNPFI QPDSPAPNPF SEEDEHPQQR
710 720 730 740 750
LSSPLVPGNP FEEPTCINPF EMDSDSGPEA EEPIEEELLL QQIDNIKAYI
760 770 780
FDAKQCGRLD EVEVLTENLR ELKHTLAKQK GGTD
Length:784
Mass (Da):88,870
Last modified:June 13, 2006 - v2
Checksum:iD49E0E5A95B18616
GO
Isoform 2 (identifier: Q9H1K0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     200-208: NKLTSASKE → KITTLHGES
     209-784: Missing.

Note: No experimental confirmation available.

Show »
Length:208
Mass (Da):23,794
Checksum:iB416981A82661172
GO

Sequence cautioni

The sequence BAC03860.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD92910.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061F → L in AAG33246. (PubMed:11062261)Curated
Sequence conflicti720 – 7201F → L in AAG33246. (PubMed:11062261)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti591 – 5911L → P.
Corresponds to variant rs9868848 [ dbSNP | Ensembl ].
VAR_052982
Natural varianti641 – 6411T → A.
Corresponds to variant rs9851219 [ dbSNP | Ensembl ].
VAR_052983
Natural varianti722 – 7221M → I.
Corresponds to variant rs9830744 [ dbSNP | Ensembl ].
VAR_052984

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei200 – 2089NKLTSASKE → KITTLHGES in isoform 2. 1 PublicationVSP_056003
Alternative sequencei209 – 784576Missing in isoform 2. 1 PublicationVSP_056004Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY009133 mRNA. Translation: AAG33246.1.
AK092312 mRNA. Translation: BAC03860.1. Different initiation.
AK301735 mRNA. Translation: BAG63200.1.
AC090954 Genomic DNA. No translation available.
BC106940 mRNA. Translation: AAI06941.1.
AB209673 mRNA. Translation: BAD92910.1. Different initiation.
CCDSiCCDS2623.1. [Q9H1K0-1]
RefSeqiNP_071735.2. NM_022340.2. [Q9H1K0-1]
XP_005265440.1. XM_005265383.2. [Q9H1K0-1]
XP_005265441.1. XM_005265384.2. [Q9H1K0-1]
XP_005265442.1. XM_005265385.2. [Q9H1K0-1]
UniGeneiHs.475565.
Hs.706478.

Genome annotation databases

EnsembliENST00000253699; ENSP00000253699; ENSG00000131381. [Q9H1K0-1]
ENST00000476527; ENSP00000422551; ENSG00000131381. [Q9H1K0-1]
GeneIDi64145.
KEGGihsa:64145.
UCSCiuc003bzm.1. human. [Q9H1K0-1]

Polymorphism databases

DMDMi108935884.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY009133 mRNA. Translation: AAG33246.1 .
AK092312 mRNA. Translation: BAC03860.1 . Different initiation.
AK301735 mRNA. Translation: BAG63200.1 .
AC090954 Genomic DNA. No translation available.
BC106940 mRNA. Translation: AAI06941.1 .
AB209673 mRNA. Translation: BAD92910.1 . Different initiation.
CCDSi CCDS2623.1. [Q9H1K0-1 ]
RefSeqi NP_071735.2. NM_022340.2. [Q9H1K0-1 ]
XP_005265440.1. XM_005265383.2. [Q9H1K0-1 ]
XP_005265441.1. XM_005265384.2. [Q9H1K0-1 ]
XP_005265442.1. XM_005265385.2. [Q9H1K0-1 ]
UniGenei Hs.475565.
Hs.706478.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YZM X-ray 1.50 A 458-503 [» ]
1Z0J X-ray 1.32 B 728-784 [» ]
1Z0K X-ray 1.92 B/D 440-503 [» ]
ProteinModelPortali Q9H1K0.
SMRi Q9H1K0. Positions 154-190, 441-501, 734-784.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122084. 15 interactions.
IntActi Q9H1K0. 5 interactions.
MINTi MINT-2817361.
STRINGi 9606.ENSP00000253699.

PTM databases

PhosphoSitei Q9H1K0.

Polymorphism databases

DMDMi 108935884.

Proteomic databases

MaxQBi Q9H1K0.
PaxDbi Q9H1K0.
PRIDEi Q9H1K0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253699 ; ENSP00000253699 ; ENSG00000131381 . [Q9H1K0-1 ]
ENST00000476527 ; ENSP00000422551 ; ENSG00000131381 . [Q9H1K0-1 ]
GeneIDi 64145.
KEGGi hsa:64145.
UCSCi uc003bzm.1. human. [Q9H1K0-1 ]

Organism-specific databases

CTDi 64145.
GeneCardsi GC03M015111.
HGNCi HGNC:20759. ZFYVE20.
HPAi HPA044878.
MIMi 609511. gene.
neXtProti NX_Q9H1K0.
PharmGKBi PA134959491.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG257999.
GeneTreei ENSGT00390000007159.
HOGENOMi HOG000154082.
HOVERGENi HBG067237.
InParanoidi Q9H1K0.
KOi K12481.
OMAi KLRLCME.
OrthoDBi EOG76MK7V.
PhylomeDBi Q9H1K0.
TreeFami TF106125.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi ZFYVE20. human.
EvolutionaryTracei Q9H1K0.
GeneWikii ZFYVE20.
GenomeRNAii 64145.
NextBioi 35475849.
PROi Q9H1K0.
SOURCEi Search...

Gene expression databases

Bgeei Q9H1K0.
CleanExi HS_ZFYVE20.
ExpressionAtlasi Q9H1K0. baseline and differential.
Genevestigatori Q9H1K0.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
InterProi IPR021565. Rbsn.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF01363. FYVE. 1 hit.
PF11464. Rbsn. 2 hits.
[Graphical view ]
SMARTi SM00064. FYVE. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 2 hits.
PROSITEi PS50178. ZF_FYVE. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain."
    Nielsen E., Christoforidis S., Uttenweiler-Joseph S., Miaczynska M., Dewitte F., Wilm M., Hoflack B., Zerial M.
    J. Cell Biol. 151:601-612(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH PTDINSP3; GTP-BOUND RAB5A AND VPS45A, SUBCELLULAR LOCATION.
    Tissue: Cervix carcinoma.
  2. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 501-784 (ISOFORM 1).
    Tissue: Brain and Testis.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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).
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-755 (ISOFORM 1).
    Tissue: Brain.
  6. "Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes."
    de Renzis S., Soennichsen B., Zerial M.
    Nat. Cell Biol. 4:124-133(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH RAB4A AND RAB5A, SUBCELLULAR LOCATION.
  7. "Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane."
    Naslavsky N., Boehm M., Backlund P.S. Jr., Caplan S.
    Mol. Biol. Cell 15:2410-2422(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH EHD1, MUTAGENESIS OF 626-ASN--PHE-628 AND 662-ASN--PHE-664, SUBCELLULAR LOCATION.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "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 (1.32 ANGSTROMS) OF 458-503 AND 728-784 IN COMPLEX WITH RAB22A, INTERACTION WITH RAB4A; RAB5A; RAB14; RAB22A AND RAB24.

Entry informationi

Entry nameiRBNS5_HUMAN
AccessioniPrimary (citable) accession number: Q9H1K0
Secondary accession number(s): B4DWY8
, C9J4P5, Q3KP30, Q59EY8, Q8NAQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: June 13, 2006
Last modified: November 26, 2014
This is version 124 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3