Skip Header

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

Q15276

- RABE1_HUMAN

UniProt

Q15276 - RABE1_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

Rab GTPase-binding effector protein 1

Gene

RABEP1

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

Functioni

Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A.4 Publications

GO - Molecular functioni

  1. GTPase activator activity Source: InterPro
  2. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. endocytosis Source: ProtInc
  3. membrane fusion Source: ProtInc
  4. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Endocytosis, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Rab GTPase-binding effector protein 1
Alternative name(s):
Rabaptin-4
Rabaptin-5
Rabaptin-5alpha
Renal carcinoma antigen NY-REN-17
Gene namesi
Name:RABEP1
Synonyms:RAB5EP, RABPT5, RABPT5A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:17677. RABEP1.

Subcellular locationi

GO - Cellular componenti

  1. early endosome Source: ProtInc
  2. endocytic vesicle Source: UniProtKB
  3. endosome Source: UniProtKB
  4. intracellular membrane-bounded organelle Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi812 – 8121D → K: No effect on RAB5A binding affinity. 1 Publication
Mutagenesisi815 – 8151E → K: No effect on RAB5A binding affinity. 1 Publication
Mutagenesisi818 – 8181Q → W: Strongly decreases RAB5A binding affinity. 1 Publication
Mutagenesisi820 – 8201D → K: Strongly decreases RAB5A binding affinity. 1 Publication
Mutagenesisi821 – 8211F → R: Strongly decreases RAB5A binding affinity. 1 Publication
Mutagenesisi822 – 8221V → D: Strongly decreases RAB5A binding affinity. 1 Publication
Mutagenesisi826 – 8261Q → A: Strongly decreases RAB5A binding affinity. 1 Publication
Mutagenesisi829 – 8291Q → A: Strongly decreases RAB5A binding affinity. 1 Publication

Organism-specific databases

PharmGKBiPA134884097.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 862861Rab GTPase-binding effector protein 1PRO_0000187556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei282 – 2821N6-acetyllysine1 Publication
Modified residuei407 – 4071Phosphoserine5 Publications
Modified residuei410 – 4101Phosphoserine3 Publications

Post-translational modificationi

Proteolytic cleavage by caspases in apoptotic cells causes loss of endosome fusion activity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15276.
PaxDbiQ15276.
PRIDEiQ15276.

PTM databases

PhosphoSiteiQ15276.

Miscellaneous databases

PMAP-CutDBQ15276.

Expressioni

Gene expression databases

BgeeiQ15276.
CleanExiHS_RABEP1.
ExpressionAtlasiQ15276. baseline and differential.
GenevestigatoriQ15276.

Organism-specific databases

HPAiCAB004549.
HPA019669.
HPA024235.
HPA024691.

Interactioni

Subunit structurei

Homodimer when bound to RAB5A. Heterodimer with RABGEF1. The heterodimer binds RAB4A and RAB5A that have been activated by GTP-binding. Binds TSC2, GGA1, GGA2, GGA3, AP1G1 and AP1G2. Interacts with ECM29.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AP1G1O437472EBI-447043,EBI-447609
AP1G2O758432EBI-447043,EBI-373637
GGA1Q9UJY58EBI-447043,EBI-447141
GGA2Q9UJY46EBI-447043,EBI-447646
GGA3Q9NZ524EBI-447043,EBI-447404

Protein-protein interaction databases

BioGridi114583. 41 interactions.
DIPiDIP-29350N.
IntActiQ15276. 20 interactions.
MINTiMINT-126137.
STRINGi9606.ENSP00000262477.

Structurei

Secondary structure

1
862
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi553 – 63987
Helixi805 – 83632
Helixi841 – 8477

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P4UX-ray2.20B435-447[»]
1TU3X-ray2.31F/G/H/I/J789-862[»]
1X79X-ray2.41B/C551-661[»]
4N3YX-ray2.20B/C552-642[»]
4N3ZX-ray3.10B/C552-642[»]
4Q9UX-ray4.62C/D/G/H552-642[»]
ProteinModelPortaliQ15276.
SMRiQ15276. Positions 553-640, 802-854.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15276.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili11 – 345335Sequence AnalysisAdd
BLAST
Coiled coili534 – 816283Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the rabaptin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG237924.
GeneTreeiENSGT00530000063743.
HOGENOMiHOG000234329.
HOVERGENiHBG055335.
InParanoidiQ15276.
KOiK12480.
OMAiQKEVHNA.
OrthoDBiEOG7WHH8T.
PhylomeDBiQ15276.
TreeFamiTF329365.

Family and domain databases

InterProiIPR003914. Rabaptin.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view]
PfamiPF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 2 hits.
[Graphical view]
PRINTSiPR01432. RABAPTIN.

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: Q15276-1) [UniParc]FASTAAdd to Basket

Also known as: Rabaptin-5

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
MAQPGPASQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY
60 70 80 90 100
LAKEEDLKRQ NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ
110 120 130 140 150
EAIDEVKRQW REEVASLQAV MKETVRDYEH QFHLRLEQER TQWAQYRESA
160 170 180 190 200
EREIADLRRR LSEGQEEENL ENEMKKAQED AEKLRSVVMP MEKEIAALKD
210 220 230 240 250
KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV LNTQKSVLQE
260 270 280 290 300
DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR
310 320 330 340 350
MEIVLTSEQL RQVEELKKKD QEDDEQQRLN KRKDHKKADV EEEIKIPVVC
360 370 380 390 400
ALTQEESSAQ LSNEEEHLDS TRGSVHSLDA GLLLPSGDPF SKSDNDMFKD
410 420 430 440 450
GLRRAQSTDS LGTSGSLQSK ALGYNYKAKS AGNLDESDFG PLVGADSVSE
460 470 480 490 500
NFDTASLGSL QMPSGFMLTK DQERAIKAMT PEQEETASLL SSVTQGMESA
510 520 530 540 550
YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE KQLQGIQIQE
560 570 580 590 600
AETRDQVKKL QLMLRQANDQ LEKTMKDKQE LEDFIKQSSE DSSHQISALV
610 620 630 640 650
LRAQASEILL EELQQGLSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND
660 670 680 690 700
SLQGKHSLHV SLQQAEDFIL PDTTEALREL VLKYREDIIN VRTAADHVEE
710 720 730 740 750
KLKAEILFLK EQIQAEQCLK ENLEETLQLE IENCKEEIAS ISSLKAELER
760 770 780 790 800
IKVEKGQLES TLREKSQQLE SLQEIKISLE EQLKKETAAK ATVEQLMFEE
810 820 830 840 850
KNKAQRLQTE LDVSEQVQRD FVKLSQTLQV QLERIRQADS LERIRAILND
860
TKLTDINQLP ET
Length:862
Mass (Da):99,290
Last modified:October 17, 2006 - v2
Checksum:iCAAF91638B8ED516
GO
Isoform 2 (identifier: Q15276-2) [UniParc]FASTAAdd to Basket

Also known as: Rabaptin-4

The sequence of this isoform differs from the canonical sequence as follows:
     758-790: Missing.

Show »
Length:829
Mass (Da):95,479
Checksum:i5B9D6E6BDF9627CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491S → Y in CAA62580. (PubMed:8521472)Curated
Sequence conflicti149 – 1491S → Y in AAC70781. (PubMed:10698684)Curated
Sequence conflicti628 – 6281M → I in BAG36864. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti640 – 6401E → G.
Corresponds to variant rs3026099 [ dbSNP | Ensembl ].
VAR_028106

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei758 – 79033Missing in isoform 2. 1 PublicationVSP_010451Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91141 mRNA. Translation: CAA62580.1.
AF098638 mRNA. Translation: AAC70781.1.
AK314183 mRNA. Translation: BAG36864.1.
BC041700 mRNA. Translation: AAH41700.1.
CCDSiCCDS42243.1. [Q15276-2]
CCDS45592.1. [Q15276-1]
RefSeqiNP_001077054.1. NM_001083585.2. [Q15276-2]
NP_001278510.1. NM_001291581.1.
NP_004694.2. NM_004703.5. [Q15276-1]
UniGeneiHs.584784.
Hs.592121.
Hs.732542.

Genome annotation databases

EnsembliENST00000341923; ENSP00000339569; ENSG00000029725. [Q15276-2]
ENST00000537505; ENSP00000445408; ENSG00000029725. [Q15276-1]
GeneIDi9135.
KEGGihsa:9135.
UCSCiuc002gbl.4. human. [Q15276-2]
uc002gbm.4. human. [Q15276-1]

Polymorphism databases

DMDMi116242743.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91141 mRNA. Translation: CAA62580.1 .
AF098638 mRNA. Translation: AAC70781.1 .
AK314183 mRNA. Translation: BAG36864.1 .
BC041700 mRNA. Translation: AAH41700.1 .
CCDSi CCDS42243.1. [Q15276-2 ]
CCDS45592.1. [Q15276-1 ]
RefSeqi NP_001077054.1. NM_001083585.2. [Q15276-2 ]
NP_001278510.1. NM_001291581.1.
NP_004694.2. NM_004703.5. [Q15276-1 ]
UniGenei Hs.584784.
Hs.592121.
Hs.732542.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P4U X-ray 2.20 B 435-447 [» ]
1TU3 X-ray 2.31 F/G/H/I/J 789-862 [» ]
1X79 X-ray 2.41 B/C 551-661 [» ]
4N3Y X-ray 2.20 B/C 552-642 [» ]
4N3Z X-ray 3.10 B/C 552-642 [» ]
4Q9U X-ray 4.62 C/D/G/H 552-642 [» ]
ProteinModelPortali Q15276.
SMRi Q15276. Positions 553-640, 802-854.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114583. 41 interactions.
DIPi DIP-29350N.
IntActi Q15276. 20 interactions.
MINTi MINT-126137.
STRINGi 9606.ENSP00000262477.

PTM databases

PhosphoSitei Q15276.

Polymorphism databases

DMDMi 116242743.

Proteomic databases

MaxQBi Q15276.
PaxDbi Q15276.
PRIDEi Q15276.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341923 ; ENSP00000339569 ; ENSG00000029725 . [Q15276-2 ]
ENST00000537505 ; ENSP00000445408 ; ENSG00000029725 . [Q15276-1 ]
GeneIDi 9135.
KEGGi hsa:9135.
UCSCi uc002gbl.4. human. [Q15276-2 ]
uc002gbm.4. human. [Q15276-1 ]

Organism-specific databases

CTDi 9135.
GeneCardsi GC17P005185.
HGNCi HGNC:17677. RABEP1.
HPAi CAB004549.
HPA019669.
HPA024235.
HPA024691.
MIMi 603616. gene.
neXtProti NX_Q15276.
PharmGKBi PA134884097.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG237924.
GeneTreei ENSGT00530000063743.
HOGENOMi HOG000234329.
HOVERGENi HBG055335.
InParanoidi Q15276.
KOi K12480.
OMAi QKEVHNA.
OrthoDBi EOG7WHH8T.
PhylomeDBi Q15276.
TreeFami TF329365.

Miscellaneous databases

ChiTaRSi RABEP1. human.
EvolutionaryTracei Q15276.
GeneWikii RABEP1.
GenomeRNAii 9135.
NextBioi 34253.
PMAP-CutDB Q15276.
PROi Q15276.
SOURCEi Search...

Gene expression databases

Bgeei Q15276.
CleanExi HS_RABEP1.
ExpressionAtlasi Q15276. baseline and differential.
Genevestigatori Q15276.

Family and domain databases

InterProi IPR003914. Rabaptin.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view ]
Pfami PF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 2 hits.
[Graphical view ]
PRINTSi PR01432. RABAPTIN.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion."
    Stenmark H., Vitale G., Ulrich O., Zerial M.
    Cell 83:423-432(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A.
    Tissue: Cervix carcinoma.
  2. "Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to perinuclear recycling vesicles."
    Nagelkerken B., van Anken E., van Raak M., Gerez L., Mohrmann K., van Uden N., Holthuizen J., Pelkmans L., van der Sluijs P.
    Biochem. J. 346:593-601(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB4A AND RAB5A.
    Tissue: Cervix carcinoma.
  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] (ISOFORM 1).
    Tissue: Brain.
  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).
    Tissue: Testis.
  5. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 807-819, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  6. "A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function."
    Horiuchi H., Lippe R., McBride H.M., Rubino M., Woodman P., Stenmark H., Rybin V., Wilm M., Ashman K., Mann M., Zerial M.
    Cell 90:1149-1159(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABGEF1.
  7. "Cleavage of rabaptin-5 blocks endosome fusion during apoptosis."
    Cosulich S.C., Horiuchi H., Zerial M., Clarke P.R., Woodman P.G.
    EMBO J. 16:6182-6191(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC CLEAVAGE BY CASPASES IN APOPTOTIC CELLS.
  8. "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis."
    Xiao G.-H., Shoarinejad F., Jin F., Golemis E.A., Yeung R.S.
    J. Biol. Chem. 272:6097-6100(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSC2.
  9. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  10. "Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex."
    Lippe R., Miaczynska M., Rybin V., Runge A., Zerial M.
    Mol. Biol. Cell 12:2219-2228(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RABGEF1.
  11. "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex."
    Mattera R., Arighi C.N., Lodge R., Zerial M., Bonifacino J.S.
    EMBO J. 22:78-88(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2, SUBCELLULAR LOCATION.
  12. "Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and gamma(1)-adaptin in membrane recycling from endosomes."
    Deneka M., Neeft M., Popa I., van Oort M., Sprong H., Oorschot V., Klumperman J., Schu P., van der Sluijs P.
    EMBO J. 22:2645-2657(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAB4A AND AP1G1, SUBCELLULAR LOCATION.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. "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-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
    Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
    J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.
  20. "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-407 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-407 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Structural basis of Rab5-Rabaptin5 interaction in endocytosis."
    Zhu G., Zhai P., Liu J., Terzyan S., Li G., Zhang X.C.
    Nat. Struct. Mol. Biol. 11:975-983(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 789-862 IN COMPLEX WITH RAB5A, SUBUNIT, MUTAGENESIS OF ASP-812; GLU-815; GLN-818; ASO-820; PHE-821; VAL-822; GLN-826 AND GLN-829.

Entry informationi

Entry nameiRABE1_HUMAN
AccessioniPrimary (citable) accession number: Q15276
Secondary accession number(s): B2RAG7, O95369, Q8IVX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 138 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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