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Protein

Atlastin-3

Gene

ATL3

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

Functioni

GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi67 – 748GTPBy similarity
Nucleotide bindingi114 – 1163GTPBy similarity
Nucleotide bindingi213 – 2142GTPBy similarity
Nucleotide bindingi272 – 2754GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: UniProtKB

GO - Biological processi

  • endoplasmic reticulum organization Source: UniProtKB
  • Golgi organization Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Atlastin-3 (EC:3.6.5.-)
Gene namesi
Name:ATL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:24526. ATL3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 445445Cytoplasmic1 PublicationAdd
BLAST
Transmembranei446 – 46621HelicalSequence analysisAdd
BLAST
Topological domaini467 – 4671LumenalSequence analysis
Transmembranei468 – 48821HelicalSequence analysisAdd
BLAST
Topological domaini489 – 54153Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Neuropathy, hereditary sensory, 1F (HSN1F)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant sensory neuropathy affecting the lower limbs. Distal sensory impairment becomes apparent during the second or third decade of life, resulting in painless ulceration of the feet with poor healing, which can progress to osteomyelitis, bone destruction, and amputation. There is no autonomic involvement, spasticity, or cognitive impairment.
See also OMIM:615632
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti192 – 1921Y → C in HSN1F; causes mislocalization of the protein; the mutant protein accumulates in condensed structures near the nucleus and localizes to unbranched tubules; has a dominant-negative disruptive effect on the regular structure of the endoplasmic reticulum. 1 Publication
VAR_070973

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731K → A: Alters endoplasmic reticulum morphogenesis. 1 Publication
Mutagenesisi213 – 2131R → Q: Alters endoplasmic reticulum morphogenesis. 1 Publication

Keywords - Diseasei

Disease mutation, Neuropathy

Organism-specific databases

MalaCardsiATL3.
MIMi615632. phenotype.
Orphaneti36386. Hereditary sensory and autonomic neuropathy type 1.
PharmGKBiPA164716353.

Polymorphism and mutation databases

BioMutaiATL3.
DMDMi74736374.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 541541Atlastin-3PRO_0000287109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei391 – 3911N6-acetyllysineCombined sources
Modified residuei535 – 5351PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6DD88.
MaxQBiQ6DD88.
PaxDbiQ6DD88.
PeptideAtlasiQ6DD88.
PRIDEiQ6DD88.
TopDownProteomicsiQ6DD88.

PTM databases

iPTMnetiQ6DD88.
PhosphoSiteiQ6DD88.
SwissPalmiQ6DD88.

Expressioni

Tissue specificityi

Expressed in the central nervous system and in dorsal root ganglia neurons. Expressed in peripheral tissues (at protein level).2 Publications

Gene expression databases

BgeeiQ6DD88.
CleanExiHS_ATL3.
ExpressionAtlasiQ6DD88. baseline and differential.
GenevisibleiQ6DD88. HS.

Interactioni

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117423. 79 interactions.
IntActiQ6DD88. 46 interactions.
MINTiMINT-3308360.
STRINGi9606.ENSP00000381844.

Structurei

3D structure databases

ProteinModelPortaliQ6DD88.
SMRiQ6DD88. Positions 23-436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 305249GB1/RHD3-type GAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
GeneTreeiENSGT00390000008959.
HOGENOMiHOG000234332.
HOVERGENiHBG062891.
InParanoidiQ6DD88.
KOiK17339.
OMAiWAFIRYS.
OrthoDBiEOG7H4DTH.
PhylomeDBiQ6DD88.
TreeFamiTF105251.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030386. G_GB1_RHD3_dom.
IPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02263. GBP. 1 hit.
PF02841. GBP_C. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6DD88-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSPQRVAAA ASRGADDAME SSKPGPVQVV LVQKDQHSFE LDEKALASIL
60 70 80 90 100
LQDHIRDLDV VVVSVAGAFR KGKSFILDFM LRYLYSQKES GHSNWLGDPE
110 120 130 140 150
EPLTGFSWRG GSDPETTGIQ IWSEVFTVEK PGGKKVAVVL MDTQGAFDSQ
160 170 180 190 200
STVKDCATIF ALSTMTSSVQ IYNLSQNIQE DDLQQLQLFT EYGRLAMDEI
210 220 230 240 250
FQKPFQTLMF LVRDWSFPYE YSYGLQGGMA FLDKRLQVKE HQHEEIQNVR
260 270 280 290 300
NHIHSCFSDV TCFLLPHPGL QVATSPDFDG KLKDIAGEFK EQLQALIPYV
310 320 330 340 350
LNPSKLMEKE INGSKVTCRG LLEYFKAYIK IYQGEDLPHP KSMLQATAEA
360 370 380 390 400
NNLAAAASAK DIYYNNMEEV CGGEKPYLSP DILEEKHCEF KQLALDHFKK
410 420 430 440 450
TKKMGGKDFS FRYQQELEEE IKELYENFCK HNGSKNVFST FRTPAVLFTG
460 470 480 490 500
IVALYIASGL TGFIGLEVVA QLFNCMVGLL LIALLTWGYI RYSGQYRELG
510 520 530 540
GAIDFGAAYV LEQASSHIGN STQATVRDAV VGRPSMDKKA Q
Length:541
Mass (Da):60,542
Last modified:August 16, 2004 - v1
Checksum:iE5C58A53F93B42D0
GO

Sequence cautioni

The sequence BAC05111.1 differs from that shown.Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491I → T in BAB14552 (PubMed:14702039).Curated
Sequence conflicti158 – 1581T → A in CAB56010 (PubMed:17974005).Curated
Sequence conflicti173 – 1731N → S in BAC05111 (PubMed:14702039).Curated
Sequence conflicti202 – 2021Q → R in CAB56010 (PubMed:17974005).Curated
Sequence conflicti215 – 2151W → R in CAB56010 (PubMed:17974005).Curated
Sequence conflicti351 – 3511N → Y in CAB56010 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti192 – 1921Y → C in HSN1F; causes mislocalization of the protein; the mutant protein accumulates in condensed structures near the nucleus and localizes to unbranched tubules; has a dominant-negative disruptive effect on the regular structure of the endoplasmic reticulum. 1 Publication
VAR_070973

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK097588 mRNA. Translation: BAC05111.1. Sequence problems.
AK023383 mRNA. Translation: BAB14552.1.
AL117600 mRNA. Translation: CAB56010.2.
BC077727 mRNA. Translation: AAH77727.1.
CCDSiCCDS41663.1.
PIRiT17320.
RefSeqiNP_001276977.1. NM_001290048.1.
NP_056274.3. NM_015459.4.
UniGeneiHs.356719.

Genome annotation databases

EnsembliENST00000398868; ENSP00000381844; ENSG00000184743.
GeneIDi25923.
KEGGihsa:25923.
UCSCiuc001nxk.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK097588 mRNA. Translation: BAC05111.1. Sequence problems.
AK023383 mRNA. Translation: BAB14552.1.
AL117600 mRNA. Translation: CAB56010.2.
BC077727 mRNA. Translation: AAH77727.1.
CCDSiCCDS41663.1.
PIRiT17320.
RefSeqiNP_001276977.1. NM_001290048.1.
NP_056274.3. NM_015459.4.
UniGeneiHs.356719.

3D structure databases

ProteinModelPortaliQ6DD88.
SMRiQ6DD88. Positions 23-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117423. 79 interactions.
IntActiQ6DD88. 46 interactions.
MINTiMINT-3308360.
STRINGi9606.ENSP00000381844.

PTM databases

iPTMnetiQ6DD88.
PhosphoSiteiQ6DD88.
SwissPalmiQ6DD88.

Polymorphism and mutation databases

BioMutaiATL3.
DMDMi74736374.

Proteomic databases

EPDiQ6DD88.
MaxQBiQ6DD88.
PaxDbiQ6DD88.
PeptideAtlasiQ6DD88.
PRIDEiQ6DD88.
TopDownProteomicsiQ6DD88.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000398868; ENSP00000381844; ENSG00000184743.
GeneIDi25923.
KEGGihsa:25923.
UCSCiuc001nxk.2. human.

Organism-specific databases

CTDi25923.
GeneCardsiATL3.
HGNCiHGNC:24526. ATL3.
MalaCardsiATL3.
MIMi609369. gene.
615632. phenotype.
neXtProtiNX_Q6DD88.
Orphaneti36386. Hereditary sensory and autonomic neuropathy type 1.
PharmGKBiPA164716353.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
GeneTreeiENSGT00390000008959.
HOGENOMiHOG000234332.
HOVERGENiHBG062891.
InParanoidiQ6DD88.
KOiK17339.
OMAiWAFIRYS.
OrthoDBiEOG7H4DTH.
PhylomeDBiQ6DD88.
TreeFamiTF105251.

Miscellaneous databases

GenomeRNAii25923.
PROiQ6DD88.
SOURCEiSearch...

Gene expression databases

BgeeiQ6DD88.
CleanExiHS_ATL3.
ExpressionAtlasiQ6DD88. baseline and differential.
GenevisibleiQ6DD88. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030386. G_GB1_RHD3_dom.
IPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02263. GBP. 1 hit.
PF02841. GBP_C. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Ovary and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  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: Pancreas.
  4. "Cellular localization, oligomerization, and membrane association of the hereditary spastic paraplegia 3A (SPG3A) protein atlastin."
    Zhu P.-P., Patterson A., Lavoie B., Stadler J., Shoeb M., Patel R., Blackstone C.
    J. Biol. Chem. 278:49063-49071(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Atlastin GTPases are required for Golgi apparatus and ER morphogenesis."
    Rismanchi N., Soderblom C., Stadler J., Zhu P.-P., Blackstone C.
    Hum. Mol. Genet. 17:1591-1604(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-73 AND ARG-213, TISSUE SPECIFICITY.
  7. "A class of dynamin-like GTPases involved in the generation of the tubular ER network."
    Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A., Rapoport T.A., Blackstone C.
    Cell 138:549-561(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT HSN1F CYS-192, CHARACTERIZATION OF VARIANT HSN1F CYS-192.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATLA3_HUMAN
AccessioniPrimary (citable) accession number: Q6DD88
Secondary accession number(s): Q8N7W5, Q9H8Q5, Q9UFL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: August 16, 2004
Last modified: June 8, 2016
This is version 102 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. 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.