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Protein

Starch-binding domain-containing protein 1

Gene

STBD1

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

Functioni

Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes.3 Publications

GO - Molecular functioni

  • glycogen binding Source: GO_Central
  • starch binding Source: InterPro

GO - Biological processi

  • glycogen catabolic process Source: GO_Central
  • glycophagy Source: GO_Central
  • muscle contraction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Autophagy, Carbohydrate metabolism, Glycogen metabolism

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Starch-binding domain-containing protein 11 Publication
Alternative name(s):
Genethonin-11 Publication
Glycophagy cargo receptor STBD1Curated
Gene namesi
Name:STBD11 Publication
ORF Names:GENX-3414
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:24854. STBD1.

Subcellular locationi

  • Preautophagosomal structure membrane 1 Publication1 Publication; Single-pass type III membrane protein 1 Publication
  • Endoplasmic reticulum membrane 1 Publication; Single-pass type III membrane protein 1 Publication

  • Note: Distributed in the transverse tubules and/or near the junctional sarcoplasmic reticulum (PubMed:9794794). Concentrates at perinuclear structures (PubMed:21893048).2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66ExtracellularSequence analysis
Transmembranei7 – 2317HelicalSequence analysisAdd
BLAST
Topological domaini24 – 358335CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: ProtInc
  • membrane Source: GO_Central
  • perinuclear region of cytoplasm Source: GO_Central
  • pre-autophagosomal structure membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi203 – 2031W → A: Abolishes interaction with GABARAPL1. 1 Publication
Mutagenesisi206 – 2061V → A: Abolishes interaction with GABARAPL1. 1 Publication
Mutagenesisi293 – 2931W → G or L: Abolishes GYS2- and glycogen-binding, and leads to rapid degradation. 2 Publications

Organism-specific databases

PharmGKBiPA162405002.

Polymorphism and mutation databases

BioMutaiSTBD1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Starch-binding domain-containing protein 1PRO_0000087476Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651PhosphoserineBy similarity
Modified residuei117 – 1171PhosphoserineCombined sources
Modified residuei148 – 1481PhosphoserineCombined sources
Modified residuei175 – 1751PhosphoserineBy similarity
Modified residuei188 – 1881PhosphoserineCombined sources
Modified residuei194 – 1941PhosphoserineCombined sources
Modified residuei210 – 2101PhosphoserineCombined sources
Modified residuei211 – 2111PhosphoserineCombined sources
Modified residuei220 – 2201PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated, which leads to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO95210.
MaxQBiO95210.
PaxDbiO95210.
PeptideAtlasiO95210.
PRIDEiO95210.

PTM databases

iPTMnetiO95210.
PhosphoSiteiO95210.

Expressioni

Tissue specificityi

Expressed at high level in skeletal and cardiac muscles. Moderately expressed in liver and placenta. No expression is found in pancreas, kidney or lung. Present in skeletal muscle, heart and placenta (at protein level).1 Publication

Gene expression databases

BgeeiO95210.
CleanExiHS_STBD1.
GenevisibleiO95210. HS.

Organism-specific databases

HPAiHPA011952.
HPA012849.

Interactioni

Subunit structurei

Interacts with the ATG8 family proteins GABARAP and GABARAPL1 (PubMed:20810658, PubMed:21893048). Interacts with several glycogen-associated proteins, such as GYS2 (liver glycogen synthase), GDE (glycogen debranching enzyme), GBE1 (glycogen branching enzyme 1) and EPM2A (Laforin) (PubMed:24837458).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC155Q8N6L03EBI-2947137,EBI-749265
GABARAPO951665EBI-2947137,EBI-712001
GABARAPL1Q9H0R87EBI-2947137,EBI-746969
GABARAPL2P605205EBI-2947137,EBI-720116
MAP1LC3BQ9GZQ82EBI-2947137,EBI-373144

Protein-protein interaction databases

BioGridi114469. 21 interactions.
IntActiO95210. 6 interactions.
MINTiMINT-5003946.

Structurei

3D structure databases

ProteinModelPortaliO95210.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini258 – 357100CBM20PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi200 – 2067LIR1 Publication

Domaini

The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family protein GABARAPL1.1 Publication
The C-terminal CBM20 domain is required for the interaction with glycogen and glycogen-associated proteins.2 Publications

Sequence similaritiesi

Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJ19. Eukaryota.
ENOG410Y3IB. LUCA.
GeneTreeiENSGT00390000007731.
HOGENOMiHOG000065763.
HOVERGENiHBG048985.
InParanoidiO95210.
OMAiMGAVWSA.
OrthoDBiEOG7W9RVP.
PhylomeDBiO95210.
TreeFamiTF338505.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
[Graphical view]
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95210-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAVWSALLV GGGLAGALFV WLLRGGPGDT GKDGDAEQEK DAPLGGAAIP
60 70 80 90 100
GGHQSGSSGL SPGPSGQELV TKPEHLQESN GHLISKTKDL GKLQAASWRL
110 120 130 140 150
QNPSREVCDN SREHVPSGQF PDTEAPATSE TSNSRSYSEV SRNESLESPM
160 170 180 190 200
GEWGFQKGQE ISAKAATCFA EKLPSSNLLK NRAKEEMSLS DLNSQDRVDH
210 220 230 240 250
EEWEMVPRHS SWGDVGVGGS LKAPVLNLNQ GMDNGRSTLV EARGQQVHGK
260 270 280 290 300
MERVAVMPAG SQQVSVRFQV HYVTSTDVQF IAVTGDHECL GRWNTYIPLH
310 320 330 340 350
YNKDGFWSHS IFLPADTVVE WKFVLVENGG VTRWEECSNR FLETGHEDKV

VHAWWGIH
Length:358
Mass (Da):39,007
Last modified:May 1, 1999 - v1
Checksum:i9C98018B82B1578C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062534 mRNA. Translation: AAC78827.1.
AK123795 mRNA. Translation: BAG53961.1.
CH471057 Genomic DNA. Translation: EAX05783.1.
BC022301 mRNA. Translation: AAH22301.1.
CCDSiCCDS3578.1.
RefSeqiNP_003934.1. NM_003943.4.
UniGeneiHs.109590.

Genome annotation databases

EnsembliENST00000237642; ENSP00000237642; ENSG00000118804.
GeneIDi8987.
KEGGihsa:8987.
UCSCiuc003hka.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062534 mRNA. Translation: AAC78827.1.
AK123795 mRNA. Translation: BAG53961.1.
CH471057 Genomic DNA. Translation: EAX05783.1.
BC022301 mRNA. Translation: AAH22301.1.
CCDSiCCDS3578.1.
RefSeqiNP_003934.1. NM_003943.4.
UniGeneiHs.109590.

3D structure databases

ProteinModelPortaliO95210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114469. 21 interactions.
IntActiO95210. 6 interactions.
MINTiMINT-5003946.

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.

PTM databases

iPTMnetiO95210.
PhosphoSiteiO95210.

Polymorphism and mutation databases

BioMutaiSTBD1.

Proteomic databases

EPDiO95210.
MaxQBiO95210.
PaxDbiO95210.
PeptideAtlasiO95210.
PRIDEiO95210.

Protocols and materials databases

DNASUi8987.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000237642; ENSP00000237642; ENSG00000118804.
GeneIDi8987.
KEGGihsa:8987.
UCSCiuc003hka.4. human.

Organism-specific databases

CTDi8987.
GeneCardsiSTBD1.
HGNCiHGNC:24854. STBD1.
HPAiHPA011952.
HPA012849.
MIMi607406. gene.
neXtProtiNX_O95210.
PharmGKBiPA162405002.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ19. Eukaryota.
ENOG410Y3IB. LUCA.
GeneTreeiENSGT00390000007731.
HOGENOMiHOG000065763.
HOVERGENiHBG048985.
InParanoidiO95210.
OMAiMGAVWSA.
OrthoDBiEOG7W9RVP.
PhylomeDBiO95210.
TreeFamiTF338505.

Miscellaneous databases

GenomeRNAii8987.
PROiO95210.
SOURCEiSearch...

Gene expression databases

BgeeiO95210.
CleanExiHS_STBD1.
GenevisibleiO95210. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
[Graphical view]
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional expression of a novel human gene encoding two 41-43 kDa skeletal muscle internal membrane proteins."
    Bouju S., Lignon M.-F., Pietu G., Le Cunff M., Leger J.-J., Auffray C., Dechesne C.A.
    Biochem. J. 335:549-556(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Muscle.
  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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Lung.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Starch binding domain-containing protein 1/genethonin 1 is a novel participant in glycogen metabolism."
    Jiang S., Heller B., Tagliabracci V.S., Zhai L., Irimia J.M., DePaoli-Roach A.A., Wells C.D., Skurat A.V., Roach P.J.
    J. Biol. Chem. 285:34960-34971(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GABARAP AND GABARAPL1, DOMAIN, SUBCELLULAR LOCATION, FUNCTION, GLYCOGEN-BINDING, MUTAGENESIS OF TRP-293.
  7. "Starch-binding domain-containing protein 1 (Stbd1) and glycogen metabolism: Identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1."
    Jiang S., Wells C.D., Roach P.J.
    Biochem. Biophys. Res. Commun. 413:420-425(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GABARAPL1, DOMAIN, MUTAGENESIS OF TRP-203 AND VAL-206, SUBCELLULAR LOCATION, FUNCTION.
  8. "The carbohydrate-binding domain of overexpressed STBD1 is important for its stability and protein-protein interactions."
    Zhu Y., Zhang M., Kelly A.R., Cheng A.
    Biosci. Rep. 34:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, GLYCOGEN-BINDING, MUTAGENESIS OF TRP-293, UBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH GYS2; AGL; GBE1 AND EPM2A, FUNCTION.
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-188; SER-194; SER-210; SER-211 AND SER-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "A motif of a microbial starch-binding domain found in human genethonin."
    Janecek S.
    Bioinformatics 18:1534-1537(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 260-358, PUTATIVE FUNCTION OF STARCH-BINDING DOMAIN.

Entry informationi

Entry nameiSTBD1_HUMAN
AccessioniPrimary (citable) accession number: O95210
Secondary accession number(s): B3KVZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 130 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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.