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Protein

Ankyrin repeat domain-containing protein 27

Gene

Ankrd27

Organism
Mus musculus (Mouse)
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 (By similarity). 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 (By similarity). Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with Rab32, Rab38 and VAMP7 (PubMed:19403694, PubMed:21187289). Involved in the regulation of neurite growth; the function seems to require its GEF activity, probably towards Rab21, and VAMP7 but not Rab32/38 (PubMed:19745841, PubMed:22171327). 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. Required for the colocalization of VAMP7 and Rab21, probably on TGN sites (By similarity). Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with VPS29 (By similarity).By similarity2 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: UniProtKB

GO - Biological processi

  • early endosome to late endosome transport Source: MGI
  • endosome to melanosome transport Source: UniProtKB
  • negative regulation of SNARE complex assembly Source: MGI
  • neuron projection morphogenesis Source: UniProtKB
  • positive regulation of dendrite morphogenesis Source: UniProtKB
  • positive regulation of GTPase activity Source: MGI
  • protein transport Source: UniProtKB-KW
  • retrograde transport, endosome to plasma membrane Source: MGI
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
VPS9-ankyrin-repeat protein
Gene namesi
Name:Ankrd27
Synonyms:Varp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2444103. Ankrd27.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endosome, Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi310 – 3101D → A: Inhibits dendrite formation. 1 Publication
Mutagenesisi350 – 3501Y → A: Inhibits dendrite formation. 1 Publication
Mutagenesisi509 – 5091Q → A: Disrupts interaction with RAB32 and RAB38; inhibits peripheral distribution of TYRP1 in melanocytes; no effect on dendrite formation in melanocytes. 2 Publications
Mutagenesisi550 – 5501Y → A: Disrupts interaction with RAB32 and RAB38; inhibits peripheral distribution of TYRP1 in melanocytes; no effect on dendrite formation in melanocytes. 2 Publications
Mutagenesisi575 – 5751W → A: Impairs interaction with RAB32 and RAB38. 1 Publication
Mutagenesisi577 – 5771Y → A: Impairs interaction with RAB32 and RAB38. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10481048Ankyrin repeat domain-containing protein 27PRO_0000274557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei961 – 9611PhosphoserineCombined sources
Modified residuei969 – 9691PhosphoserineBy similarity
Modified residuei1022 – 10221PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3UMR0.
MaxQBiQ3UMR0.
PaxDbiQ3UMR0.
PRIDEiQ3UMR0.

PTM databases

iPTMnetiQ3UMR0.
PhosphoSiteiQ3UMR0.

Expressioni

Gene expression databases

BgeeiQ3UMR0.
CleanExiMM_ANKRD27.
ExpressionAtlasiQ3UMR0. baseline and differential.
GenevisibleiQ3UMR0. MM.

Interactioni

Subunit structurei

Interacts with RAB21 (GDP-bound form), VPS29, KIF5A, KIF5C, GOLGA4 (By similarity). Interacts with RAB32 (GTP-bound form), RAB38 (GTP-bound form), VAMP7 (PubMed:19403694, PubMed:21187289). Interacts with low affinity with RAB5 (By similarity). ANKRD27:RAB32 heterodimers can homodimerize to form tetramers (By similarity). Can interact with RAB38 or RAB32, VPS29 and VAMP7 simultaneously (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Rab38Q8QZZ85EBI-1993429,EBI-1993463

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi232848. 1 interaction.
IntActiQ3UMR0. 2 interactions.
STRINGi10090.ENSMUSP00000041751.

Structurei

3D structure databases

ProteinModelPortaliQ3UMR0.
SMRiQ3UMR0. Positions 147-393, 404-922.
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 – 55730ANK 4Add
BLAST
Repeati564 – 59330ANK 5Add
BLAST
Repeati597 – 62731ANK 6Add
BLAST
Repeati668 – 69831ANK 7Add
BLAST
Repeati742 – 77130ANK 8Add
BLAST
Repeati775 – 80430ANK 9Add
BLAST
Repeati808 – 83730ANK 10Add
BLAST
Repeati841 – 87030ANK 11Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 372372Sufficient for GEF activity towards RAB21By similarityAdd
BLAST
Regioni396 – 46065Sufficient for interaction with VPS29By similarityAdd
BLAST
Regioni451 – 729279Interaction with RAB321 PublicationAdd
BLAST
Regioni451 – 600150Interaction with RAB381 PublicationAdd
BLAST
Regioni658 – 70750Required for interaction with VAMP7By similarity1 PublicationAdd
BLAST
Regioni692 – 74554Sufficient for interaction with VPS29By similarityAdd
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.
InParanoidiQ3UMR0.
KOiK20175.
OMAiIDCLFKH.
OrthoDBiEOG7NCV2S.
PhylomeDBiQ3UMR0.
TreeFamiTF351261.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR003123. VPS9.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3UMR0-1) [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
MALYDEDLLK NPFYLALQKW RPDLCSKVAQ IHGIVLVPCR GSLPGSVQAS
60 70 80 90 100
CQFESYVLVP TEGHFQTLDG KAVVIEGNRI KLGAGFACLL SVPILFEETF
110 120 130 140 150
YNEKEESFSI LCIAHPLERR ETSEEPSAPA DPFSLKTIED VREFLGRHSE
160 170 180 190 200
KFDKNIASFH RTFRECERKS LRHHIDSVNA LYTKCLQQLL RDSHLKVLAK
210 220 230 240 250
QEAQMNLMKQ AVEMYVHHDI YDLIFKYVGT MEASEDAAFN KITRSLQDLQ
260 270 280 290 300
QKDIGVKPEF SFNIPRAKRE LGQLNKCTSP QQKLLCLRKV VQLMTQSPSQ
310 320 330 340 350
RVNLETMCAD DLLSVLLYLL VKTEIPNWMA NLSYIKNFRF SSSAKDELGY
360 370 380 390 400
CLTSVEAAIE YIRQGSLSTK TPDAEGFGDR LFLKQRMNLL SQMTSTPIDC
410 420 430 440 450
LFKHIASGNQ KEVERLLSQD DQDKDAMQKM CHPLCSCEDC EKLISGRLND
460 470 480 490 500
PSVVTPFSRD DRGQTPLHVA ALCGQASLID FLVSKGAVVN ATDYHGSTPL
510 520 530 540 550
HLACQKGFQS VTLLLLHYKA STEVQDNNGN TPLHLACTYG QEDCVKALVY
560 570 580 590 600
YDVQACRLDI GNEKGDTALH IAARWGYEGI IETLLQNGAP TAVQNRLKET
610 620 630 640 650
PLKCALNSKI LSIMEAHHLS SDRRPRPSEV PAQSPTRSVD SISQGSSTSS
660 670 680 690 700
FSSISVSFRQ EEVKKDYREV EKLLRAVADG DLEMVRYLLE WTEDDLDDVE
710 720 730 740 750
DAISTVDLEF CHPLCQCPKC APAQKLARIS ANGLSVNVTN QDGFSPLHMA
760 770 780 790 800
ALHGRTDLVP LLLKHGAYSG ARNTSQAVPL HLACQQGHFQ VAKCLLDSNA
810 820 830 840 850
KPNKKDLSGN TPLICACSAG HHEVAALLLQ HGASINACNN KGNTALHEAV
860 870 880 890 900
MGRHTLVVEL LLFYGASVDI LNKRQYTAAD CAEQDSKIME LLQVVPGCVA
910 920 930 940 950
SLDSVEEADH EGYVTVEIRR KWNPKMYNLP EEPLRRQFCL INPGGRFQER
960 970 980 990 1000
TSRETMGRDR SVPDLAGRSL QEPEKQRVTG KQSDLSDLSR YQTSEEGNKG
1010 1020 1030 1040
LPERPVSRQA APGHRPMVRR HTVNDAAILQ VPEVTVHLTT HEASVPQS
Length:1,048
Mass (Da):116,809
Last modified:February 6, 2007 - v2
Checksum:i63636820D0CC4D2C
GO
Isoform 2 (identifier: Q3UMR0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     670-724: Missing.

Note: No experimental confirmation available.
Show »
Length:993
Mass (Da):110,604
Checksum:i855BDE37439764D2
GO
Isoform 3 (identifier: Q3UMR0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     630-670: Missing.

Note: No experimental confirmation available.
Show »
Length:1,007
Mass (Da):112,333
Checksum:iD14EAB10424F63F5
GO

Sequence cautioni

The sequence AAP94281.1 differs from that shown. Reason: Frameshift at positions 920 and 929. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 31030QQKLL…TMCAD → TAEAAVPEEGGPAHDTISQP ESELGDHVCR in BAC39537 (PubMed:16141072).CuratedAdd
BLAST
Sequence conflicti371 – 3722TP → PQ in BAD21367 (PubMed:15449545).Curated
Sequence conflicti373 – 3775DAEGF → VRSPC in AAH16493 (PubMed:15489334).Curated
Sequence conflicti601 – 6011P → Q in BAE26038 (PubMed:16141072).Curated
Sequence conflicti609 – 6091K → KV in BAD21367 (PubMed:15449545).Curated
Sequence conflicti730 – 7301S → P in AAP94281 (PubMed:16525121).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei630 – 67041Missing in isoform 3. 1 PublicationVSP_022791Add
BLAST
Alternative sequencei670 – 72455Missing in isoform 2. 1 PublicationVSP_022792Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY336500 mRNA. Translation: AAP94281.1. Frameshift.
AK085796 mRNA. Translation: BAC39537.1.
AK144733 mRNA. Translation: BAE26038.1.
BC016493 mRNA. Translation: AAH16493.1.
BC065093 mRNA. Translation: AAH65093.1.
AK131117 Transcribed RNA. Translation: BAD21367.1.
CCDSiCCDS21154.1. [Q3UMR0-1]
RefSeqiNP_663608.3. NM_145633.3. [Q3UMR0-1]
NP_839994.1. NM_178263.3.
UniGeneiMm.272620.

Genome annotation databases

EnsembliENSMUST00000040844; ENSMUSP00000041751; ENSMUSG00000034867. [Q3UMR0-1]
ENSMUST00000190503; ENSMUSP00000140259; ENSMUSG00000034867. [Q3UMR0-2]
GeneIDi245886.
KEGGimmu:245886.
UCSCiuc009gkd.1. mouse. [Q3UMR0-1]
uc012fin.1. mouse. [Q3UMR0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY336500 mRNA. Translation: AAP94281.1. Frameshift.
AK085796 mRNA. Translation: BAC39537.1.
AK144733 mRNA. Translation: BAE26038.1.
BC016493 mRNA. Translation: AAH16493.1.
BC065093 mRNA. Translation: AAH65093.1.
AK131117 Transcribed RNA. Translation: BAD21367.1.
CCDSiCCDS21154.1. [Q3UMR0-1]
RefSeqiNP_663608.3. NM_145633.3. [Q3UMR0-1]
NP_839994.1. NM_178263.3.
UniGeneiMm.272620.

3D structure databases

ProteinModelPortaliQ3UMR0.
SMRiQ3UMR0. Positions 147-393, 404-922.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi232848. 1 interaction.
IntActiQ3UMR0. 2 interactions.
STRINGi10090.ENSMUSP00000041751.

PTM databases

iPTMnetiQ3UMR0.
PhosphoSiteiQ3UMR0.

Proteomic databases

EPDiQ3UMR0.
MaxQBiQ3UMR0.
PaxDbiQ3UMR0.
PRIDEiQ3UMR0.

Protocols and materials databases

DNASUi245886.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040844; ENSMUSP00000041751; ENSMUSG00000034867. [Q3UMR0-1]
ENSMUST00000190503; ENSMUSP00000140259; ENSMUSG00000034867. [Q3UMR0-2]
GeneIDi245886.
KEGGimmu:245886.
UCSCiuc009gkd.1. mouse. [Q3UMR0-1]
uc012fin.1. mouse. [Q3UMR0-2]

Organism-specific databases

CTDi84079.
MGIiMGI:2444103. Ankrd27.

Phylogenomic databases

eggNOGiENOG410IQ81. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00780000121977.
HOGENOMiHOG000033958.
HOVERGENiHBG080845.
InParanoidiQ3UMR0.
KOiK20175.
OMAiIDCLFKH.
OrthoDBiEOG7NCV2S.
PhylomeDBiQ3UMR0.
TreeFamiTF351261.

Miscellaneous databases

ChiTaRSiAnkrd27. mouse.
PROiQ3UMR0.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UMR0.
CleanExiMM_ANKRD27.
ExpressionAtlasiQ3UMR0. baseline and differential.
GenevisibleiQ3UMR0. MM.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR003123. VPS9.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/cJ.
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Heart and Lung.
  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] (ISOFORM 2).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Kidney.
  4. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
    DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 371-1048 (ISOFORM 3).
    Tissue: Embryonic tail.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-961, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "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 VAMP7, SUBCELLULAR LOCATION.
  7. "Varp is a novel Rab32/38-binding protein that regulates Tyrp1 trafficking in melanocytes."
    Tamura K., Ohbayashi N., Maruta Y., Kanno E., Itoh T., Fukuda M.
    Mol. Biol. Cell 20:2900-2908(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAB32 AND RAB38, SUBCELLULAR LOCATION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-961, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Spleen.
  9. "Structure-function analysis of VPS9-ankyrin-repeat protein (Varp) in the trafficking of tyrosinase-related protein 1 in melanocytes."
    Tamura K., Ohbayashi N., Ishibashi K., Fukuda M.
    J. Biol. Chem. 286:7507-7521(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAB32; RAB38 AND VAMP7, MUTAGENESIS OF GLN-509; TYR-550; TRP-575 AND TYR-577.
  10. "The Rab21-GEF activity of Varp, but not its Rab32/38 effector function, is required for dendrite formation in melanocytes."
    Ohbayashi N., Yatsu A., Tamura K., Fukuda M.
    Mol. Biol. Cell 23:669-678(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-310; TYR-350; GLN-509 AND TYR-550.

Entry informationi

Entry nameiANR27_MOUSE
AccessioniPrimary (citable) accession number: Q3UMR0
Secondary accession number(s): Q6KAU0
, Q6P1F9, Q7TNY8, Q8BUD2, Q91W65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: July 6, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.