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Q13438

- OS9_HUMAN

UniProt

Q13438 - OS9_HUMAN

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Protein
Protein OS-9
Gene
OS9
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301Carbohydrate
Binding sitei182 – 1821Carbohydrate
Binding sitei188 – 1881Carbohydrate
Binding sitei212 – 2121Carbohydrate
Binding sitei218 – 2181Carbohydrate

GO - Molecular functioni

  1. glycoprotein binding Source: UniProtKB
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. protein retention in ER lumen Source: UniProtKB
  3. protein targeting Source: Ensembl
  4. protein ubiquitination Source: UniProtKB
  5. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  6. response to endoplasmic reticulum stress Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Protein OS-9
Alternative name(s):
Amplified in osteosarcoma 9
Gene namesi
Name:OS9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:16994. OS9.

Subcellular locationi

Endoplasmic reticulum lumen 3 Publications

GO - Cellular componenti

  1. Hrd1p ubiquitin ligase complex Source: UniProtKB
  2. endoplasmic reticulum lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi188 – 1881R → A: Loss of glycan-binding activity and partial inhibition of ERAD of the misfolded glycoprotein NHK (PubMed:19346256). Reduced interaction with SEL1L (PubMed:18264092) not confirmed in (PubMed:19346256). 3 Publications

Organism-specific databases

PharmGKBiPA164724245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed prediction
Add
BLAST
Chaini26 – 667642Protein OS-9
PRO_0000021951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi110 ↔ 1232 Publications
Glycosylationi177 – 1771N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi181 ↔ 2162 Publications
Disulfide bondi196 ↔ 2282 Publications

Post-translational modificationi

Intramolecular disulfide bonds.
Isoform 1 and isoform 2 are N-glycosylated.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ13438.
PaxDbiQ13438.
PRIDEiQ13438.

PTM databases

PhosphoSiteiQ13438.

Expressioni

Tissue specificityi

Ubiquitously expressed. Found as well in all tumor cell lines analyzed, amplified in sarcomas. Highly expressed in osteosarcoma SJSA-1 and rhabdomyosarcoma Rh30 cell lines. Isoform 2 is the major isoform detected in all cell types examined.

Inductioni

Up-regulated in response to endoplasmic reticulum stress (at protein level).2 Publications

Gene expression databases

ArrayExpressiQ13438.
BgeeiQ13438.
GenevestigatoriQ13438.

Organism-specific databases

HPAiCAB011518.
HPA013694.

Interactioni

Subunit structurei

Probably part of the HRD1 ubiquitin ligase complex composed at least of SYVN1/HRD1 and SEL1L with which it interacts directly. Through this complex it may interact with ERLEC1 and HSPA5. Interacts with DERL2. Interacts with HSP90B1 and CREB3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EGLN1Q9GZT94EBI-725454,EBI-1174818
HIF1AQ166659EBI-725454,EBI-447269

Protein-protein interaction databases

BioGridi116156. 46 interactions.
DIPiDIP-37493N.
IntActiQ13438. 24 interactions.
MINTiMINT-1187753.
STRINGi9606.ENSP00000318165.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi111 – 1155
Beta strandi118 – 1236
Turni124 – 1263
Beta strandi127 – 1315
Beta strandi143 – 15513
Beta strandi169 – 1768
Turni182 – 1843
Beta strandi189 – 1968
Beta strandi206 – 2149
Beta strandi217 – 2248
Helixi225 – 2273

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AIHX-ray2.10A/B108-229[»]
ProteinModelPortaliQ13438.
SMRiQ13438. Positions 109-228.

Miscellaneous databases

EvolutionaryTraceiQ13438.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini108 – 17871PRKCSH
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi414 – 42916Asp/Glu-rich (acidic)
Add
BLAST

Sequence similaritiesi

Belongs to the OS-9 family.
Contains 1 PRKCSH domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG309879.
HOGENOMiHOG000293348.
HOVERGENiHBG000974.
InParanoidiQ13438.
KOiK10088.
OMAiRYHSQTY.
OrthoDBiEOG7R8315.
PhylomeDBiQ13438.
TreeFamiTF314309.

Family and domain databases

Gene3Di2.70.130.10. 1 hit.
InterProiIPR009011. Man6P_isomerase_rcpt-bd_dom.
IPR012913. PRKCSH.
[Graphical view]
PfamiPF07915. PRKCSH. 1 hit.
[Graphical view]
SUPFAMiSSF50911. SSF50911. 1 hit.

Sequences (8)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 8 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13438-1) [UniParc]FASTAAdd to Basket

Also known as: OS-9-1

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

MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV    50
MGGQSQSSDV VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE 100
LLSPMRDAPC LLKTKDWWTY EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS 150
AFDWDDETAK ASKQHRLKRY HSQTYGNGSK CDLNGRPREA EVRFLCDEGA 200
GISGDYIDRV DEPLSCSYVL TIRTPRLCPH PLLRPPPSAA PQAILCHPSL 250
QPEEYMAYVQ RQADSKQYGD KIIEELQDLG PQVWSETKSG VAPQKMAGAS 300
PTKDDSKDSD FWKMLNEPED QAPGGEEVPA EEQDPSPEAA DSASGAPNDF 350
QNNVQVKVIR SPADLIRFIE ELKGGTKKGK PNIGQEQPVD DAAEVPQREP 400
EKERGDPERQ REMEEEEDED EDEDEDEDER QLLGEFEKEL EGILLPSDRD 450
RLRSEVKAGM ERELENIIQE TEKELDPDGL KKESERDRAM LALTSTLNKL 500
IKRLEEKQSP ELVKKHKKKR VVPKKPPPSP QPTEEDPEHR VRVRVTKLRL 550
GGPNQDLTVL EMKRENPQLK QIEGLVKELL EREGLTAAGK IEIKIVRPWA 600
EGTEEGARWL TDEDTRNLKE IFFNILVPGA EEAQKERQRQ KELESNYRRV 650
WGSPGGEGTG DLDEFDF 667

Note: Major isoform.

Length:667
Mass (Da):75,562
Last modified:November 1, 1996 - v1
Checksum:i65BA3F66CEC58756
GO
Isoform 2 (identifier: Q13438-2) [UniParc]FASTAAdd to Basket

Also known as: OS-9-2

The sequence of this isoform differs from the canonical sequence as follows:
     534-588: Missing.

Note: Major isoform.

Show »
Length:612
Mass (Da):69,246
Checksum:i1FD06F7B23101015
GO
Isoform 3 (identifier: Q13438-3) [UniParc]FASTAAdd to Basket

Also known as: OS-9-3

The sequence of this isoform differs from the canonical sequence as follows:
     456-470: Missing.
     534-588: Missing.

Show »
Length:597
Mass (Da):67,505
Checksum:i7D00C1EA449B3DA1
GO
Isoform 4 (identifier: Q13438-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     456-470: Missing.

Note: No experimental confirmation available.

Show »
Length:652
Mass (Da):73,821
Checksum:i7D44F2347B609055
GO
Isoform 5 (identifier: Q13438-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     161-193: Missing.
     263-263: A → AV
     534-588: Missing.

Note: No experimental confirmation available.

Show »
Length:580
Mass (Da):65,520
Checksum:iBE4EEA80CF8EA076
GO
Isoform 6 (identifier: Q13438-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     142-193: Missing.
     534-588: Missing.

Note: No experimental confirmation available.

Show »
Length:560
Mass (Da):63,155
Checksum:iEBF3F8A812BDAF60
GO
Isoform 7 (identifier: Q13438-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     263-263: A → AV
     534-588: Missing.

Note: Gene prediction based on EST data.

Show »
Length:613
Mass (Da):69,346
Checksum:i353DE17278AB9546
GO
Isoform 8 (identifier: Q13438-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-113: Missing.
     456-470: Missing.
     534-588: Missing.

Note: No experimental confirmation available.

Show »
Length:538
Mass (Da):60,847
Checksum:i30188F4A2A67AD8E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti305 – 3051D → N.1 Publication
Corresponds to variant rs141986192 [ dbSNP | Ensembl ].
VAR_069062
Natural varianti398 – 3981R → W.
Corresponds to variant rs1804598 [ dbSNP | Ensembl ].
VAR_011897
Natural varianti454 – 4541S → L.
Corresponds to variant rs34764811 [ dbSNP | Ensembl ].
VAR_034364

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei55 – 11359Missing in isoform 8.
VSP_046770Add
BLAST
Alternative sequencei142 – 19352Missing in isoform 6.
VSP_046001Add
BLAST
Alternative sequencei161 – 19333Missing in isoform 5.
VSP_044701Add
BLAST
Alternative sequencei263 – 2631A → AV in isoform 5 and isoform 7.
VSP_044702
Alternative sequencei456 – 47015Missing in isoform 3, isoform 4 and isoform 8.
VSP_004352Add
BLAST
Alternative sequencei534 – 58855Missing in isoform 2, isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_004353Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71L → V in CAG33072. 1 Publication
Sequence conflicti194 – 1941F → V in BAG64798. 1 Publication
Sequence conflicti371 – 3711E → G in BAG56939. 1 Publication
Sequence conflicti497 – 4971L → F in BAG64798. 1 Publication
Sequence conflicti522 – 5221V → I in BAG60733. 1 Publication
Sequence conflicti653 – 6531S → P in BAG56939. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U41635 mRNA. Translation: AAB06495.1.
AB002805 Genomic DNA. Translation: BAA24362.1.
AB002806 mRNA. Translation: BAA24363.1.
AK291374 mRNA. Translation: BAF84063.1.
AK293435 mRNA. Translation: BAG56939.1.
AK296770 mRNA. Translation: BAG59349.1.
AK298532 mRNA. Translation: BAG60733.1.
AK303858 mRNA. Translation: BAG64798.1.
CR456791 mRNA. Translation: CAG33072.1.
AC025165 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97045.1.
CH471054 Genomic DNA. Translation: EAW97046.1.
CH471054 Genomic DNA. Translation: EAW97047.1.
BC000532 mRNA. Translation: AAH00532.1.
BC007254 mRNA. Translation: AAH07254.1.
BC023513 mRNA. Translation: AAH23513.2.
U81031 Genomic DNA. Translation: AAC39523.2.
CCDSiCCDS31843.1. [Q13438-1]
CCDS31844.1. [Q13438-2]
CCDS31845.1. [Q13438-4]
CCDS31846.1. [Q13438-3]
CCDS58246.1. [Q13438-6]
CCDS58247.1. [Q13438-7]
CCDS58248.1. [Q13438-5]
CCDS58249.1. [Q13438-8]
PIRiJC5889.
RefSeqiNP_001017956.1. NM_001017956.2. [Q13438-2]
NP_001017957.1. NM_001017957.2. [Q13438-3]
NP_001017958.1. NM_001017958.2. [Q13438-4]
NP_001248349.1. NM_001261420.1. [Q13438-7]
NP_001248350.1. NM_001261421.1. [Q13438-5]
NP_001248351.1. NM_001261422.1. [Q13438-6]
NP_001248352.1. NM_001261423.1. [Q13438-8]
NP_006803.1. NM_006812.3. [Q13438-1]
UniGeneiHs.527861.

Genome annotation databases

EnsembliENST00000257966; ENSP00000257966; ENSG00000135506. [Q13438-7]
ENST00000315970; ENSP00000318165; ENSG00000135506. [Q13438-1]
ENST00000389142; ENSP00000373794; ENSG00000135506. [Q13438-3]
ENST00000389146; ENSP00000373798; ENSG00000135506. [Q13438-4]
ENST00000435406; ENSP00000389632; ENSG00000135506. [Q13438-6]
ENST00000439210; ENSP00000407360; ENSG00000135506. [Q13438-8]
ENST00000551035; ENSP00000447866; ENSG00000135506. [Q13438-5]
ENST00000552285; ENSP00000450010; ENSG00000135506. [Q13438-2]
GeneIDi10956.
KEGGihsa:10956.
UCSCiuc001spj.3. human. [Q13438-1]
uc001spk.3. human. [Q13438-4]
uc001spn.3. human.

Polymorphism databases

DMDMi3024310.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U41635 mRNA. Translation: AAB06495.1 .
AB002805 Genomic DNA. Translation: BAA24362.1 .
AB002806 mRNA. Translation: BAA24363.1 .
AK291374 mRNA. Translation: BAF84063.1 .
AK293435 mRNA. Translation: BAG56939.1 .
AK296770 mRNA. Translation: BAG59349.1 .
AK298532 mRNA. Translation: BAG60733.1 .
AK303858 mRNA. Translation: BAG64798.1 .
CR456791 mRNA. Translation: CAG33072.1 .
AC025165 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97045.1 .
CH471054 Genomic DNA. Translation: EAW97046.1 .
CH471054 Genomic DNA. Translation: EAW97047.1 .
BC000532 mRNA. Translation: AAH00532.1 .
BC007254 mRNA. Translation: AAH07254.1 .
BC023513 mRNA. Translation: AAH23513.2 .
U81031 Genomic DNA. Translation: AAC39523.2 .
CCDSi CCDS31843.1. [Q13438-1 ]
CCDS31844.1. [Q13438-2 ]
CCDS31845.1. [Q13438-4 ]
CCDS31846.1. [Q13438-3 ]
CCDS58246.1. [Q13438-6 ]
CCDS58247.1. [Q13438-7 ]
CCDS58248.1. [Q13438-5 ]
CCDS58249.1. [Q13438-8 ]
PIRi JC5889.
RefSeqi NP_001017956.1. NM_001017956.2. [Q13438-2 ]
NP_001017957.1. NM_001017957.2. [Q13438-3 ]
NP_001017958.1. NM_001017958.2. [Q13438-4 ]
NP_001248349.1. NM_001261420.1. [Q13438-7 ]
NP_001248350.1. NM_001261421.1. [Q13438-5 ]
NP_001248351.1. NM_001261422.1. [Q13438-6 ]
NP_001248352.1. NM_001261423.1. [Q13438-8 ]
NP_006803.1. NM_006812.3. [Q13438-1 ]
UniGenei Hs.527861.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3AIH X-ray 2.10 A/B 108-229 [» ]
ProteinModelPortali Q13438.
SMRi Q13438. Positions 109-228.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116156. 46 interactions.
DIPi DIP-37493N.
IntActi Q13438. 24 interactions.
MINTi MINT-1187753.
STRINGi 9606.ENSP00000318165.

PTM databases

PhosphoSitei Q13438.

Polymorphism databases

DMDMi 3024310.

Proteomic databases

MaxQBi Q13438.
PaxDbi Q13438.
PRIDEi Q13438.

Protocols and materials databases

DNASUi 10956.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257966 ; ENSP00000257966 ; ENSG00000135506 . [Q13438-7 ]
ENST00000315970 ; ENSP00000318165 ; ENSG00000135506 . [Q13438-1 ]
ENST00000389142 ; ENSP00000373794 ; ENSG00000135506 . [Q13438-3 ]
ENST00000389146 ; ENSP00000373798 ; ENSG00000135506 . [Q13438-4 ]
ENST00000435406 ; ENSP00000389632 ; ENSG00000135506 . [Q13438-6 ]
ENST00000439210 ; ENSP00000407360 ; ENSG00000135506 . [Q13438-8 ]
ENST00000551035 ; ENSP00000447866 ; ENSG00000135506 . [Q13438-5 ]
ENST00000552285 ; ENSP00000450010 ; ENSG00000135506 . [Q13438-2 ]
GeneIDi 10956.
KEGGi hsa:10956.
UCSCi uc001spj.3. human. [Q13438-1 ]
uc001spk.3. human. [Q13438-4 ]
uc001spn.3. human.

Organism-specific databases

CTDi 10956.
GeneCardsi GC12P058088.
HGNCi HGNC:16994. OS9.
HPAi CAB011518.
HPA013694.
MIMi 609677. gene.
neXtProti NX_Q13438.
PharmGKBi PA164724245.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG309879.
HOGENOMi HOG000293348.
HOVERGENi HBG000974.
InParanoidi Q13438.
KOi K10088.
OMAi RYHSQTY.
OrthoDBi EOG7R8315.
PhylomeDBi Q13438.
TreeFami TF314309.

Miscellaneous databases

ChiTaRSi OS9. human.
EvolutionaryTracei Q13438.
GeneWikii OS9_(gene).
GenomeRNAii 10956.
NextBioi 35464261.
PROi Q13438.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13438.
Bgeei Q13438.
Genevestigatori Q13438.

Family and domain databases

Gene3Di 2.70.130.10. 1 hit.
InterProi IPR009011. Man6P_isomerase_rcpt-bd_dom.
IPR012913. PRKCSH.
[Graphical view ]
Pfami PF07915. PRKCSH. 1 hit.
[Graphical view ]
SUPFAMi SSF50911. SSF50911. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequence analysis of a gene (OS-9) ubiquitously expressed in human tissues and amplified in sarcomas."
    Su Y.A., Hutter C.M., Trent J.M., Meltzer P.S.
    Mol. Carcinog. 15:270-275(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Genomic organization of the OS-9 gene amplified in human sarcomas."
    Kimura Y., Nakazawa M., Tsuchiya N., Asakawa S., Shimizu N., Yamada M.
    J. Biochem. 122:1190-1195(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  3. "Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines."
    Kimura Y., Nakazawa M., Yamada M.
    J. Biochem. 123:876-882(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), CHARACTERIZATION, ALTERNATIVE SPLICING (ISOFORMS 2 AND 3).
    Tissue: Promyelocytic leukemia.
  4. "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] (ISOFORMS 2; 4; 5; 6 AND 8), VARIANT ASN-305.
    Tissue: Brain, Tongue and Trachea.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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).
    Tissue: Muscle.
  9. "Transcript mapping in a 46-kb sequenced region at the core of 12q13.3 amplification in human cancers."
    Elkahloun A.G., Krizman D.B., Wang Z., Hofmann T.A., Roe B.A., Meltzer P.S.
    Genomics 42:295-301(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-667.
  10. "OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum."
    Wang Y., Fu X., Gaiser S., Koettgen M., Kramer-Zucker A., Walz G., Wegierski T.
    J. Biol. Chem. 282:36561-36570(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRPV4 MATURATION.
  11. "A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal."
    Bernasconi R., Pertel T., Luban J., Molinari M.
    J. Biol. Chem. 283:16446-16454(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, DISULFIDE BONDS, GLYCOSYLATION, INDUCTION, MUTAGENESIS OF ARG-188.
  12. "Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP."
    Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K.
    J. Biol. Chem. 283:20914-20924(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERLEC1; HSPA5; SEL1L AND SYVN1.
  13. "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD."
    Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.
    Nat. Cell Biol. 10:272-282(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSP90B1; SEL1L AND SYVN1, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ARG-188.
  14. "Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans."
    Hosokawa N., Kamiya Y., Kamiya D., Kato K., Nagata K.
    J. Biol. Chem. 284:17061-17068(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A LECTIN, MUTAGENESIS OF ARG-188.
  15. "Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins."
    Alcock F., Swanton E.
    J. Mol. Biol. 385:1032-1042(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MISFOLDED GLYCOPROTEIN UBIQUITINATION, SUBCELLULAR LOCATION, GLYCOSYLATION, INTERACTION WITH DERL2; HRD1 AND SEL1L, INDUCTION BY ER STRESS.
  16. "DC-STAMP interacts with ER-resident transcription factor LUMAN which becomes activated during DC maturation."
    Eleveld-Trancikova D., Sanecka A., van Hout-Kuijer M.A., Looman M.W., Hendriks I.A., Jansen B.J., Adema G.J.
    Mol. Immunol. 47:1963-1973(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CREB3.
  17. "Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation."
    Satoh T., Chen Y., Hu D., Hanashima S., Yamamoto K., Yamaguchi Y.
    Mol. Cell 40:905-916(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 108-229 IN COMPLEX WITH MANNOPENTAOSE, FUNCTION, DISULFIDE BONDS.

Entry informationi

Entry nameiOS9_HUMAN
AccessioniPrimary (citable) accession number: Q13438
Secondary accession number(s): A6NDD1
, A6NFR7, A6NLB2, A8K5Q9, B4DE28, B4DPX1, B4E1I6, E7ENT8, E7EW91, F8VUH2, G3XA88, O00579, Q6IBL2, Q8IZ58, Q9BW99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 123 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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