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Protein

Ankyrin repeat domain-containing protein 27

Gene

ANKRD27

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

Functioni

May be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and regulate endosome dynamics (PubMed:16525121, PubMed:18477474). May regulate the participation of VAMP7 in membrane fusion events; in vitro inhibits VAMP7-mediated SNARE complex formation by trapping VAMP7 in a closed, fusogenically inactive conformation (PubMed:23104059). Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with Rab32, Rab38 and VAMP7 (By similarity). Involved in the regulation of neurite growth; the function seems to require its GEF activity, probably towards Rab21, and VAMP7 but not Rab32/38 (By similarity). Proposed to be involved in Golgi sorting of VAMP7 and transport of VAMP7 vesicles to the cell surface; the function seems to implicate kinesin heavy chain isoform 5 proteins, GOLGA4, RAB21 and MACF1 (PubMed:22705394). Required for the colocalization of VAMP7 and Rab21, probably on TGN sites (PubMed:19745841). Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with VPS29 (PubMed:24856514).By similarity3 Publications2 Publications

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • guanyl-nucleotide exchange factor activity Source: MGI
  • Rab GTPase binding Source: UniProtKB
  • SNARE binding Source: GO_Central

GO - Biological processi

  • early endosome to late endosome transport Source: MGI
  • endosome to melanosome transport Source: Ensembl
  • negative regulation of SNARE complex assembly Source: UniProtKB
  • neuron projection morphogenesis Source: GO_Central
  • positive regulation of dendrite morphogenesis Source: Ensembl
  • positive regulation of GTPase activity Source: GOC
  • protein transport Source: UniProtKB-KW
  • retrograde transport, endosome to plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Guanine-nucleotide releasing factor

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Ankyrin repeat domain-containing protein 27
Alternative name(s):
VPS9 domain-containing protein
Gene namesi
Name:ANKRD27
ORF Names:PP12899
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:25310. ANKRD27.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • cytosol Source: GOC
  • early endosome Source: UniProtKB
  • late endosome Source: UniProtKB
  • lysosome Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • neuron projection Source: GO_Central
  • plasma membrane Source: UniProtKB
  • transport vesicle Source: GO_Central
  • tubular endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endosome, Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi432 – 4321H → A: Disrupts interaction with VPS29; when associated with A-434. 1 Publication
Mutagenesisi434 – 4341L → A: Disrupts interaction with VPS29; when associated with A-432. 1 Publication
Mutagenesisi509 – 5091Q → A: Disrupts interaction with RAB32. 1 Publication
Mutagenesisi513 – 5131L → D: Disrupts interaction with RAB32. 1 Publication
Mutagenesisi546 – 5461K → D: Impairs interaction with RAB32. 1 Publication
Mutagenesisi550 – 5501Y → A: Impairs interaction with RAB32. 1 Publication
Mutagenesisi679 – 6791D → A: Disrupts interaction with VAMP7. 1 Publication
Mutagenesisi681 – 6811D → A: Disrupts interaction with VAMP7. 1 Publication
Mutagenesisi684 – 6841M → D: Disrupts interaction with VAMP7. 1 Publication
Mutagenesisi687 – 6871Y → S: Disrupts interaction with VAMP7. 1 Publication
Mutagenesisi712 – 7121H → A: Disrupts interaction with VPS29; when associated with A-714. 1 Publication
Mutagenesisi714 – 7141L → A: Disrupts interaction with VPS29; when associated with A-712. 1 Publication

Organism-specific databases

PharmGKBiPA134893411.

Polymorphism and mutation databases

BioMutaiANKRD27.
DMDMi125987706.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10501050Ankyrin repeat domain-containing protein 27PRO_0000274556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei962 – 9621PhosphoserineBy similarity
Modified residuei1023 – 10231PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96NW4.
MaxQBiQ96NW4.
PaxDbiQ96NW4.
PRIDEiQ96NW4.

PTM databases

iPTMnetiQ96NW4.
PhosphoSiteiQ96NW4.

Expressioni

Gene expression databases

BgeeiQ96NW4.
CleanExiHS_ANKRD27.
ExpressionAtlasiQ96NW4. baseline and differential.
GenevisibleiQ96NW4. HS.

Organism-specific databases

HPAiHPA042769.

Interactioni

Subunit structurei

Interacts with RAB21 (GDP-bound form), VPS29, RAB32 (GTP-bound form), RAB38 (GTP-bound form), VAMP7, KIF5A, KIF5C, GOLGA4. Interacts with low affinity with RAB5. ANKRD27:RAB32 heterodimers can homodimerize to form tetramers. Can interact with RAB38 or RAB32, VPS29 and VAMP7 simultaneously (PubMed:16525121, PubMed:18477474, PubMed:19745841, PubMed:22705394, PubMed:23104059, PubMed:24856514).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GOLGA4Q134392EBI-6125599,EBI-1037845
KIF5AQ128404EBI-6125599,EBI-713468
Kif5aP331752EBI-6125599,EBI-349710From a different organism.
Vamp7Q9JHW54EBI-6125599,EBI-919936From a different organism.

GO - Molecular functioni

  • Rab GTPase binding Source: UniProtKB
  • SNARE binding Source: GO_Central

Protein-protein interaction databases

BioGridi123874. 14 interactions.
DIPiDIP-57614N.
IntActiQ96NW4. 9 interactions.
MINTiMINT-1198049.
STRINGi9606.ENSP00000304292.

Structurei

Secondary structure

1
1050
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi466 – 4738Combined sources
Helixi476 – 4849Combined sources
Helixi499 – 5068Combined sources
Helixi509 – 5179Combined sources
Helixi532 – 5387Combined sources
Helixi542 – 55110Combined sources
Beta strandi552 – 5543Combined sources
Helixi568 – 5747Combined sources
Helixi578 – 5869Combined sources
Helixi601 – 6044Combined sources
Helixi608 – 6158Combined sources
Helixi668 – 67811Combined sources
Helixi682 – 6898Combined sources
Helixi747 – 7537Combined sources
Helixi759 – 7657Combined sources
Helixi780 – 7878Combined sources
Helixi790 – 7989Combined sources
Helixi813 – 8197Combined sources
Helixi823 – 8253Combined sources
Helixi826 – 8316Combined sources
Helixi846 – 8527Combined sources
Helixi856 – 8649Combined sources
Helixi880 – 8823Combined sources
Helixi888 – 8925Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B93X-ray2.00B659-921[»]
4CYMX-ray2.80D/E/F450-640[»]
4CZ2X-ray2.97D/E/F450-640[»]
ProteinModelPortaliQ96NW4.
SMRiQ96NW4. Positions 147-375, 404-906.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini233 – 371139VPS9PROSITE-ProRule annotationAdd
BLAST
Repeati396 – 42631ANK 1Add
BLAST
Repeati462 – 49130ANK 2Add
BLAST
Repeati495 – 52430ANK 3Add
BLAST
Repeati528 – 56033ANK 4Add
BLAST
Repeati564 – 59330ANK 5Add
BLAST
Repeati597 – 62731ANK 6Add
BLAST
Repeati668 – 69831ANK 7Add
BLAST
Repeati743 – 77230ANK 8Add
BLAST
Repeati776 – 80530ANK 9Add
BLAST
Repeati809 – 83830ANK 10Add
BLAST
Repeati842 – 87130ANK 11Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 372372Sufficient for GEF activity towards RAB211 PublicationAdd
BLAST
Regioni396 – 46065Sufficient for interaction with VPS291 PublicationAdd
BLAST
Regioni451 – 730280Interaction with RAB32By similarityAdd
BLAST
Regioni451 – 600150Interaction with RAB38By similarity1 PublicationAdd
BLAST
Regioni658 – 70750Required for interaction with VAMP7By similarity2 PublicationsAdd
BLAST
Regioni692 – 74655Sufficient for interaction with VPS291 PublicationAdd
BLAST

Sequence similaritiesi

Contains 11 ANK repeats.PROSITE-ProRule annotation
Contains 1 VPS9 domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiENOG410IQ81. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00780000121977.
HOGENOMiHOG000033958.
HOVERGENiHBG080845.
InParanoidiQ96NW4.
OMAiIDCLFKH.
OrthoDBiEOG7NCV2S.
PhylomeDBiQ96NW4.
TreeFamiTF351261.

Family and domain databases

Gene3Di1.25.40.20. 6 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR003123. VPS9.
[Graphical view]
PfamiPF12796. Ank_2. 3 hits.
PF13606. Ank_3. 1 hit.
PF02204. VPS9. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 8 hits.
SM00167. VPS9. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 8 hits.
PS51205. VPS9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96NW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALYDEDLLK NPFYLALQKC RPDLCSKVAQ IHGIVLVPCK GSLSSSIQST
60 70 80 90 100
CQFESYILIP VEEHFQTLNG KDVFIQGNRI KLGAGFACLL SVPILFEETF
110 120 130 140 150
YNEKEESFSI LCIAHPLEKR ESSEEPLAPS DPFSLKTIED VREFLGRHSE
160 170 180 190 200
RFDRNIASFH RTFRECERKS LRHHIDSANA LYTKCLQQLL RDSHLKMLAK
210 220 230 240 250
QEAQMNLMKQ AVEIYVHHEI YNLIFKYVGT MEASEDAAFN KITRSLQDLQ
260 270 280 290 300
QKDIGVKPEF SFNIPRAKRE LAQLNKCTSP QQKLVCLRKV VQLITQSPSQ
310 320 330 340 350
RVNLETMCAD DLLSVLLYLL VKTEIPNWMA NLSYIKNFRF SSLAKDELGY
360 370 380 390 400
CLTSFEAAIE YIRQGSLSAK PPESEGFGDR LFLKQRMSLL SQMTSSPTDC
410 420 430 440 450
LFKHIASGNQ KEVERLLSQE DHDKDTVQKM CHPLCFCDDC EKLVSGRLND
460 470 480 490 500
PSVVTPFSRD DRGHTPLHVA AVCGQASLID LLVSKGAMVN ATDYHGATPL
510 520 530 540 550
HLACQKGYQS VTLLLLHYKA SAEVQDNNGN TPLHLACTYG HEDCVKALVY
560 570 580 590 600
YDVESCRLDI GNEKGDTPLH IAARWGYQGV IETLLQNGAS TEIQNRLKET
610 620 630 640 650
PLKCALNSKI LSVMEAYHLS FERRQKSSEA PVQSPQRSVD SISQESSTSS
660 670 680 690 700
FSSMSASSRQ EETKKDYREV EKLLRAVADG DLEMVRYLLE WTEEDLEDAE
710 720 730 740 750
DTVSAADPEF CHPLCQCPKC APAQKRLAKV PASGLGVNVT SQDGSSPLHV
760 770 780 790 800
AALHGRADLI PLLLKHGANA GARNADQAVP LHLACQQGHF QVVKCLLDSN
810 820 830 840 850
AKPNKKDLSG NTPLIYACSG GHHELVALLL QHGASINASN NKGNTALHEA
860 870 880 890 900
VIEKHVFVVE LLLLHGASVQ VLNKRQRTAV DCAEQNSKIM ELLQVVPSCV
910 920 930 940 950
ASLDDVAETD RKEYVTVKIR KKWNSKLYDL PDEPFTRQFY FVHSAGQFKG
960 970 980 990 1000
KTSREIMARD RSVPNLTEGS LHEPGRQSVT LRQNNLPAQS GSHAAEKGNS
1010 1020 1030 1040 1050
DWPERPGLTQ TGPGHRRMLR RHTVEDAVVS QGPEAAGPLS TPQEVSASRS
Length:1,050
Mass (Da):116,984
Last modified:February 6, 2007 - v2
Checksum:iC47A96AA15E420F9
GO

Sequence cautioni

The sequence BAB70755.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 17516HRTFR…LRHHI → LIEHSENARERASVTT in AAQ04657 (PubMed:15498874).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti657 – 6571S → G.1 Publication
Corresponds to variant rs2287669 [ dbSNP | Ensembl ].
VAR_030317
Natural varianti761 – 7611P → R.1 Publication
Corresponds to variant rs2302970 [ dbSNP | Ensembl ].
VAR_030318

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136784 mRNA. Translation: CAB66718.1.
AK054561 mRNA. Translation: BAB70755.1. Different initiation.
BC050529 mRNA. Translation: AAH50529.1.
AF447882 mRNA. Translation: AAQ04657.1.
AL834335 mRNA. Translation: CAD39003.1.
CCDSiCCDS32986.1.
RefSeqiNP_115515.2. NM_032139.2.
XP_006723475.1. XM_006723412.2.
UniGeneiHs.59236.

Genome annotation databases

EnsembliENST00000306065; ENSP00000304292; ENSG00000105186.
GeneIDi84079.
KEGGihsa:84079.
UCSCiuc002ntn.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136784 mRNA. Translation: CAB66718.1.
AK054561 mRNA. Translation: BAB70755.1. Different initiation.
BC050529 mRNA. Translation: AAH50529.1.
AF447882 mRNA. Translation: AAQ04657.1.
AL834335 mRNA. Translation: CAD39003.1.
CCDSiCCDS32986.1.
RefSeqiNP_115515.2. NM_032139.2.
XP_006723475.1. XM_006723412.2.
UniGeneiHs.59236.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B93X-ray2.00B659-921[»]
4CYMX-ray2.80D/E/F450-640[»]
4CZ2X-ray2.97D/E/F450-640[»]
ProteinModelPortaliQ96NW4.
SMRiQ96NW4. Positions 147-375, 404-906.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123874. 14 interactions.
DIPiDIP-57614N.
IntActiQ96NW4. 9 interactions.
MINTiMINT-1198049.
STRINGi9606.ENSP00000304292.

PTM databases

iPTMnetiQ96NW4.
PhosphoSiteiQ96NW4.

Polymorphism and mutation databases

BioMutaiANKRD27.
DMDMi125987706.

Proteomic databases

EPDiQ96NW4.
MaxQBiQ96NW4.
PaxDbiQ96NW4.
PRIDEiQ96NW4.

Protocols and materials databases

DNASUi84079.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306065; ENSP00000304292; ENSG00000105186.
GeneIDi84079.
KEGGihsa:84079.
UCSCiuc002ntn.2. human.

Organism-specific databases

CTDi84079.
GeneCardsiANKRD27.
HGNCiHGNC:25310. ANKRD27.
HPAiHPA042769.
neXtProtiNX_Q96NW4.
PharmGKBiPA134893411.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQ81. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00780000121977.
HOGENOMiHOG000033958.
HOVERGENiHBG080845.
InParanoidiQ96NW4.
OMAiIDCLFKH.
OrthoDBiEOG7NCV2S.
PhylomeDBiQ96NW4.
TreeFamiTF351261.

Miscellaneous databases

ChiTaRSiANKRD27. human.
GeneWikiiANKRD27.
GenomeRNAii84079.
PROiQ96NW4.

Gene expression databases

BgeeiQ96NW4.
CleanExiHS_ANKRD27.
ExpressionAtlasiQ96NW4. baseline and differential.
GenevisibleiQ96NW4. HS.

Family and domain databases

Gene3Di1.25.40.20. 6 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR003123. VPS9.
[Graphical view]
PfamiPF12796. Ank_2. 3 hits.
PF13606. Ank_3. 1 hit.
PF02204. VPS9. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 8 hits.
SM00167. VPS9. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 8 hits.
PS51205. VPS9. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLY-657 AND ARG-761.
    Tissue: Testis.
  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].
    Tissue: Spleen.
  3. "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: Testis.
  4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-175.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 644-1050.
    Tissue: Testis.
  6. "Varp is a Rab21 guanine nucleotide exchange factor and regulates endosome dynamics."
    Zhang X., He X., Fu X.-Y., Chang Z.
    J. Cell Sci. 119:1053-1062(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAB21 AND RAB5A, SUBCELLULAR LOCATION.
  7. "Varp interacts with Rab38 and functions as its potential effector."
    Wang F., Zhang H., Zhang X., Wang Y., Ren F., Zhang X., Zhai Y., Chang Z.
    Biochem. Biophys. Res. Commun. 372:162-167(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAB38 AND RAB21.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1023, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Role of Varp, a Rab21 exchange factor and TI-VAMP/VAMP7 partner, in neurite growth."
    Burgo A., Sotirakis E., Simmler M.C., Verraes A., Chamot C., Simpson J.C., Lanzetti L., Proux-Gillardeaux V., Galli T.
    EMBO Rep. 10:1117-1124(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAB21 AND VAMP7, SUBCELLULAR LOCATION.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "A molecular network for the transport of the TI-VAMP/VAMP7 vesicles from cell center to periphery."
    Burgo A., Proux-Gillardeaux V., Sotirakis E., Bun P., Casano A., Verraes A., Liem R.K., Formstecher E., Coppey-Moisan M., Galli T.
    Dev. Cell 23:166-180(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KIF5A; KIF5C AND GOLGA4.
  12. "The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation."
    Schafer I.B., Hesketh G.G., Bright N.A., Gray S.R., Pryor P.R., Evans P.R., Luzio J.P., Owen D.J.
    Nat. Struct. Mol. Biol. 19:1300-1309(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 659-921 IN COMPLEX WITH VAMP7, SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-679; ASP-681; MET-684 AND TYR-687.
  13. "VARP is recruited on to endosomes by direct interaction with retromer, where together they function in export to the cell surface."
    Hesketh G.G., Perez-Dorado I., Jackson L.P., Wartosch L., Schafer I.B., Gray S.R., McCoy A.J., Zeldin O.B., Garman E.F., Harbour M.E., Evans P.R., Seaman M.N., Luzio J.P., Owen D.J.
    Dev. Cell 29:591-606(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 450-640 IN COMPLEX WITH RAB32, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS29, MUTAGENESIS OF HIS-432; LEU-434; GLN-509; LEU-513; LYS-546; TYR-550; HIS-712 AND LEU-714.

Entry informationi

Entry nameiANR27_HUMAN
AccessioniPrimary (citable) accession number: Q96NW4
Secondary accession number(s): Q71MF5
, Q86UC3, Q8ND80, Q9H0I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: June 8, 2016
This is version 115 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 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.