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Protein

Amphoterin-induced protein 1

Gene

Amigo1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes growth and fasciculation of neurites from cultured hippocampal neurons. May be involved in fasciculation as well as myelination of developing neural axons. May have a role in regeneration as well as neural plasticity in the adult nervous system. May mediate homophilic as well as heterophilic cell-cell interaction and contribute to signal transduction through its intracellular domain (By similarity). Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 (PubMed:22056818).By similarity1 Publication

GO - Molecular functioni

  • potassium channel regulator activity Source: UniProtKB

GO - Biological processi

  • axonal fasciculation Source: UniProtKB
  • axonogenesis Source: MGI
  • cell adhesion Source: MGI
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: UniProtKB
  • myelination Source: UniProtKB
  • positive regulation of axonogenesis Source: UniProtKB
  • positive regulation of potassium ion transmembrane transport Source: UniProtKB
  • positive regulation of synapse assembly Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion, Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Amphoterin-induced protein 1
Alternative name(s):
AMIGO-1
Alivin-2
Gene namesi
Name:Amigo1Imported
Synonyms:Ali2Imported, Amigo1 Publication, Kiaa1163Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2653612. Amigo1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 371344ExtracellularSequence analysisAdd
BLAST
Transmembranei372 – 39221HelicalSequence analysisAdd
BLAST
Topological domaini393 – 492100CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • dendrite Source: UniProtKB
  • integral component of membrane Source: MGI
  • integral component of plasma membrane Source: InterPro
  • neuronal cell body membrane Source: UniProtKB
  • perikaryon Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi348 – 3481N → A: Prevents from leaving the ER. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 492465Amphoterin-induced protein 1Sequence analysisPRO_0000014507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 40PROSITE-ProRule annotation1 Publication
Disulfide bondi38 ↔ 47PROSITE-ProRule annotation1 Publication
Glycosylationi72 – 721N-linked (GlcNAc...)1 Publication
Disulfide bondi225 ↔ 253PROSITE-ProRule annotation1 Publication
Disulfide bondi227 ↔ 270PROSITE-ProRule annotation1 Publication
Glycosylationi269 – 2691N-linked (GlcNAc...)1 Publication
Disulfide bondi290 ↔ 340PROSITE-ProRule annotation1 Publication
Glycosylationi315 – 3151N-linked (GlcNAc...)1 Publication
Glycosylationi348 – 3481N-linked (GlcNAc...)1 Publication
Glycosylationi359 – 3591N-linked (GlcNAc...)1 Publication
Modified residuei476 – 4761PhosphoserineCombined sources
Modified residuei480 – 4801PhosphoserineCombined sources

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ80ZD8.
PaxDbiQ80ZD8.
PRIDEiQ80ZD8.

PTM databases

iPTMnetiQ80ZD8.
PhosphoSiteiQ80ZD8.

Expressioni

Tissue specificityi

Expressed in hippocampal and cortical neurons (at protein level) (PubMed:22056818). High levels in cerebellum, cerebrum, and retina. Low levels in liver, kidney, small intestine, spleen, lung and heart.2 Publications

Gene expression databases

BgeeiQ80ZD8.
CleanExiMM_AMIGO1.
ExpressionAtlasiQ80ZD8. baseline and differential.
GenevisibleiQ80ZD8. MM.

Interactioni

Subunit structurei

Homodimer, and heterodimer with AMIGO2 and AMIGO3 (PubMed:21983541). Interacts with KCNB1 (PubMed:22056818).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Kcnb1Q037174EBI-7511393,EBI-7511364

Protein-protein interaction databases

IntActiQ80ZD8. 1 interaction.
MINTiMINT-8298633.
STRINGi10090.ENSMUSP00000061244.

Structurei

Secondary structure

1
492
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 413Combined sources
Beta strandi44 – 463Combined sources
Beta strandi64 – 674Combined sources
Beta strandi80 – 834Combined sources
Beta strandi90 – 923Combined sources
Turni103 – 1086Combined sources
Beta strandi114 – 1163Combined sources
Turni127 – 1326Combined sources
Beta strandi138 – 1403Combined sources
Turni151 – 1566Combined sources
Beta strandi162 – 1643Combined sources
Helixi175 – 1773Combined sources
Beta strandi189 – 1913Combined sources
Helixi202 – 2076Combined sources
Helixi210 – 2134Combined sources
Helixi227 – 23812Combined sources
Helixi242 – 2454Combined sources
Helixi248 – 2503Combined sources
Beta strandi252 – 2576Combined sources
Helixi262 – 2643Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi286 – 2883Combined sources
Beta strandi298 – 3025Combined sources
Beta strandi314 – 3218Combined sources
Beta strandi324 – 3296Combined sources
Beta strandi336 – 3438Combined sources
Beta strandi348 – 36013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XOTX-ray2.00A/B28-370[»]
ProteinModelPortaliQ80ZD8.
SMRiQ80ZD8. Positions 31-363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 6134LRRNTAdd
BLAST
Repeati62 – 8322LRR 11 PublicationAdd
BLAST
Repeati87 – 10822LRR 21 PublicationAdd
BLAST
Repeati111 – 13222LRR 31 PublicationAdd
BLAST
Repeati135 – 15622LRR 41 PublicationAdd
BLAST
Repeati159 – 18022LRR 51 PublicationAdd
BLAST
Repeati186 – 20621LRR 61 PublicationAdd
BLAST
Domaini208 – 27265LRRCTAdd
BLAST
Domaini269 – 35284Ig-like C2-typeSequence analysisAdd
BLAST

Domaini

The LRR repeat region mediates homodimerization.

Sequence similaritiesi

Contains 6 LRR (leucine-rich) repeats.Sequence analysis
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IGN4. Eukaryota.
ENOG410ZZH4. LUCA.
GeneTreeiENSGT00530000063545.
HOGENOMiHOG000231327.
HOVERGENiHBG080231.
InParanoidiQ80ZD8.
OMAiCSEYKER.
TreeFamiTF326838.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR031283. AMIGO.
IPR031284. AMIGO1.
IPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PANTHERiPTHR24368. PTHR24368. 1 hit.
PTHR24368:SF1. PTHR24368:SF1. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF13855. LRR_8. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 5 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 6 hits.
[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. AlignAdd to basket

Isoform 11 Publication (identifier: Q80ZD8-1) [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
MQPQRDLRGL WLLLLSVFLL LFEVARAGRS VVSCPANCLC ASNILSCSKQ
60 70 80 90 100
QLPNVPQSLP SYTALLDLSH NNLSRLRAEW TPTRLTNLHS LLLSHNHLNF
110 120 130 140 150
ISSEAFVPVP NLRYLDLSSN HLHTLDEFLF SDLQALEVLL LYNNHIVVVD
160 170 180 190 200
RNAFEDMAQL QKLYLSQNQI SRFPVELIKD GNKLPKLMLL DLSSNKLKKL
210 220 230 240 250
PLTDLQKLPA WVKNGLYLHN NPLECDCKLY QLFSHWQYRQ LSSVMDFQED
260 270 280 290 300
LYCMHSKKLH NIFSLDFFNC SEYKESAWEA HLGDTLTIRC DTKQQGMTKV
310 320 330 340 350
WVSPSNEQVL SQGSNGSVSV RNGDLFFKKV QVEDGGVYTC YAMGETFNET
360 370 380 390 400
LSVELKVYNF TLHGHHDTLN TAYTTLVGCI LSVVLVLIYL YLTPCRCWCR
410 420 430 440 450
GVEKPSSHQG DSLSSSMLST TPNHDPMAGG DKDDGFDRRV AFLEPAGPGQ
460 470 480 490
GQNGKLKPGN TLPVPEATGK GQRRMSDPES VSSVFSDTPI VV
Length:492
Mass (Da):55,343
Last modified:June 1, 2003 - v1
Checksum:iEF1CCD6BA61FE222
GO
Isoform 2Curated (identifier: Q80ZD8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     290-309: CDTKQQGMTKVWVSPSNEQV → TLPPTVYTRLANLRAHGLYN
     310-492: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:309
Mass (Da):35,661
Checksum:i26C3E666ECEBDA8E
GO

Sequence cautioni

The sequence AAH22907.1 differs from that shown. Reason: Frameshift at position 113. Curated
The sequence BAD32396.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei290 – 30920CDTKQ…SNEQV → TLPPTVYTRLANLRAHGLYN in isoform 2. 1 PublicationVSP_014166Add
BLAST
Alternative sequencei310 – 492183Missing in isoform 2. 1 PublicationVSP_014167Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY237008 mRNA. Translation: AAO48949.1.
AB167509 mRNA. Translation: BAD12541.1.
AK035960 mRNA. Translation: BAC29259.1.
AK173118 mRNA. Translation: BAD32396.1. Different initiation.
AL671854 Genomic DNA. Translation: CAM27260.1.
BC010598 mRNA. Translation: AAH10598.2.
BC022907 mRNA. Translation: AAH22907.1. Frameshift.
CCDSiCCDS17753.1. [Q80ZD8-1]
CCDS71305.1. [Q80ZD8-2]
RefSeqiNP_001004293.1. NM_001004293.2. [Q80ZD8-1]
NP_001274022.1. NM_001287093.1. [Q80ZD8-2]
NP_666249.2. NM_146137.3. [Q80ZD8-1]
UniGeneiMm.275752.

Genome annotation databases

EnsembliENSMUST00000050909; ENSMUSP00000061244; ENSMUSG00000050947. [Q80ZD8-1]
ENSMUST00000106656; ENSMUSP00000102267; ENSMUSG00000050947. [Q80ZD8-1]
ENSMUST00000106659; ENSMUSP00000102270; ENSMUSG00000050947. [Q80ZD8-2]
GeneIDi229715.
KEGGimmu:229715.
UCSCiuc008qyg.2. mouse. [Q80ZD8-1]
uc033hze.1. mouse. [Q80ZD8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY237008 mRNA. Translation: AAO48949.1.
AB167509 mRNA. Translation: BAD12541.1.
AK035960 mRNA. Translation: BAC29259.1.
AK173118 mRNA. Translation: BAD32396.1. Different initiation.
AL671854 Genomic DNA. Translation: CAM27260.1.
BC010598 mRNA. Translation: AAH10598.2.
BC022907 mRNA. Translation: AAH22907.1. Frameshift.
CCDSiCCDS17753.1. [Q80ZD8-1]
CCDS71305.1. [Q80ZD8-2]
RefSeqiNP_001004293.1. NM_001004293.2. [Q80ZD8-1]
NP_001274022.1. NM_001287093.1. [Q80ZD8-2]
NP_666249.2. NM_146137.3. [Q80ZD8-1]
UniGeneiMm.275752.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XOTX-ray2.00A/B28-370[»]
ProteinModelPortaliQ80ZD8.
SMRiQ80ZD8. Positions 31-363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80ZD8. 1 interaction.
MINTiMINT-8298633.
STRINGi10090.ENSMUSP00000061244.

PTM databases

iPTMnetiQ80ZD8.
PhosphoSiteiQ80ZD8.

Proteomic databases

MaxQBiQ80ZD8.
PaxDbiQ80ZD8.
PRIDEiQ80ZD8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000050909; ENSMUSP00000061244; ENSMUSG00000050947. [Q80ZD8-1]
ENSMUST00000106656; ENSMUSP00000102267; ENSMUSG00000050947. [Q80ZD8-1]
ENSMUST00000106659; ENSMUSP00000102270; ENSMUSG00000050947. [Q80ZD8-2]
GeneIDi229715.
KEGGimmu:229715.
UCSCiuc008qyg.2. mouse. [Q80ZD8-1]
uc033hze.1. mouse. [Q80ZD8-2]

Organism-specific databases

CTDi57463.
MGIiMGI:2653612. Amigo1.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IGN4. Eukaryota.
ENOG410ZZH4. LUCA.
GeneTreeiENSGT00530000063545.
HOGENOMiHOG000231327.
HOVERGENiHBG080231.
InParanoidiQ80ZD8.
OMAiCSEYKER.
TreeFamiTF326838.

Miscellaneous databases

PROiQ80ZD8.
SOURCEiSearch...

Gene expression databases

BgeeiQ80ZD8.
CleanExiMM_AMIGO1.
ExpressionAtlasiQ80ZD8. baseline and differential.
GenevisibleiQ80ZD8. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR031283. AMIGO.
IPR031284. AMIGO1.
IPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PANTHERiPTHR24368. PTHR24368. 1 hit.
PTHR24368:SF1. PTHR24368:SF1. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF13855. LRR_8. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 5 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "AMIGO, a transmembrane protein implicated in axon tract development, defines a novel protein family with leucine-rich repeats."
    Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A., Rauvala H.
    J. Cell Biol. 160:963-973(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Strain: C57BL/6JImported.
    Tissue: Brain1 Publication.
  2. Ono T.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: BrainImported.
  3. "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: Cerebellum.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-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., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal brainImported.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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] (ISOFORMS 1 AND 2).
    Strain: FVB/NImported.
    Tissue: Mammary glandImported.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney and Lung.
  8. "AMIGO is an auxiliary subunit of the Kv2.1 potassium channel."
    Peltola M.A., Kuja-Panula J., Lauri S.E., Taira T., Rauvala H.
    EMBO Rep. 12:1293-1299(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Crystal structure and role of glycans and dimerization in folding of neuronal leucine-rich repeat protein AMIGO-1."
    Kajander T., Kuja-Panula J., Rauvala H., Goldman A.
    J. Mol. Biol. 413:1001-1015(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-370, DISULFIDE BONDS, LEUCINE-RICH REPEATS, SUBUNIT, GLYCOSYLATION AT ASN-72; ASN-269; ASN-315; ASN-348 AND ASN-359, MUTAGENESIS OF ASN-348, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiAMGO1_MOUSE
AccessioniPrimary (citable) accession number: Q80ZD8
Secondary accession number(s): A2AE40
, Q69ZQ0, Q8R5D4, Q921U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 1, 2003
Last modified: June 8, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.