Q13438 (OS9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein OS-9

Alternative name(s):
Amplified in osteosarcoma 9

Gene names

Name:

OS9

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	667 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17
Subunit structure	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. Ref.12 Ref.13 Ref.15 Ref.16
Subcellular location	Endoplasmic reticulum lumen Ref.11 Ref.13 Ref.15.
Tissue specificity	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.
Induction	Up-regulated in response to endoplasmic reticulum stress (at protein level). Ref.11 Ref.15
Post-translational modification	Intramolecular disulfide bonds. Isoform 1 and isoform 2 are N-glycosylated. Ref.11 Ref.13 Ref.15
Sequence similarities	Belongs to the OS-9 family. Contains 1 PRKCSH domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Ligand	Lectin
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype Ref.13Ref.11Ref.14. Source: UniProtKB protein retention in ER lumen Inferred from direct assay Ref.11. Source: UniProtKB protein targeting Inferred from electronic annotation. Source: Compara protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.15. Source: UniProtKB response to endoplasmic reticulum stress Inferred from direct assay Ref.15. Source: UniProtKB
Cellular_component	Hrd1p ubiquitin ligase complex Non-traceable author statement Ref.12Ref.15. Source: UniProtKB endoplasmic reticulum lumen Inferred from direct assay Ref.13Ref.11Ref.15. Source: UniProtKB
Molecular_function	glycoprotein binding Inferred from direct assay Ref.13Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EGLN1	Q9GZT9	4	EBI-1174342,EBI-1174818
HIF1A	Q16665	9	EBI-1174342,EBI-447269

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13438-1)

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.

Note: Major isoform.

Isoform 2 (identifier: Q13438-2)

Also known as: OS-9-2;

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

Note: Major isoform.

Isoform 3 (identifier: Q13438-3)

Also known as: OS-9-3;

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

Isoform 4 (identifier: Q13438-4)

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

Note: No experimental confirmation available.

Isoform 5 (identifier: Q13438-5)

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.

Isoform 6 (identifier: Q13438-6)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Chain

26 – 667

642

Protein OS-9

PRO_0000021951

Regions

Domain

108 – 178

71

PRKCSH

Compositional bias

414 – 429

16

Asp/Glu-rich (acidic)

Sites

Binding site

130

1

Carbohydrate

Binding site

182

1

Carbohydrate

Binding site

188

1

Carbohydrate

Binding site

212

1

Carbohydrate

Binding site

218

1

Carbohydrate

Amino acid modifications

Glycosylation

177

1

N-linked (GlcNAc...) Potential

Disulfide bond

110 ↔ 123

Ref.11 Ref.17

Disulfide bond

181 ↔ 216

Ref.11 Ref.17

Disulfide bond

196 ↔ 228

Ref.11 Ref.17

Natural variations

Alternative sequence

142 – 193

52

Missing in isoform 6.

VSP_046001

Alternative sequence

161 – 193

33

Missing in isoform 5.

VSP_044701

Alternative sequence

263

1

A → AV in isoform 5.

VSP_044702

Alternative sequence

456 – 470

15

Missing in isoform 3 and isoform 4.

VSP_004352

Alternative sequence

534 – 588

55

Missing in isoform 2, isoform 3, isoform 5 and isoform 6.

VSP_004353

Natural variant

305

1

D → N. Ref.4
Corresponds to variant rs141986192 [ dbSNP | Ensembl ].

VAR_069062

Natural variant

398

1

R → W.
Corresponds to variant rs1804598 [ dbSNP | Ensembl ].

VAR_011897

Natural variant

454

1

S → L.
Corresponds to variant rs34764811 [ dbSNP | Ensembl ].

VAR_034364

Experimental info

Mutagenesis

188

1

R → 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). Ref.11 Ref.13 Ref.14

Sequence conflict

7

1

L → V in CAG33072. Ref.5

Sequence conflict

194

1

F → V in BAG64798. Ref.4

Sequence conflict

497

1

L → F in BAG64798. Ref.4

Sequence conflict

522

1

V → I in BAG60733. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

667

Helix Strand Turn

Details...

Beta strand

111 – 115

5

Beta strand

118 – 123

6

Turn

124 – 126

3

Beta strand

127 – 131

5

Beta strand

143 – 155

13

Beta strand

169 – 176

8

Turn

182 – 184

3

Beta strand

189 – 196

8

Beta strand

206 – 214

9

Beta strand

217 – 224

8

Helix

225 – 227

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (OS-9-1) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 65BA3F66CEC58756	FASTA	667	75,562
	10 20 30 40 50 60 MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV MGGQSQSSDV 70 80 90 100 110 120 VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY 130 140 150 160 170 180 EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS AFDWDDETAK ASKQHRLKRY HSQTYGNGSK 190 200 210 220 230 240 CDLNGRPREA EVRFLCDEGA GISGDYIDRV DEPLSCSYVL TIRTPRLCPH PLLRPPPSAA 250 260 270 280 290 300 PQAILCHPSL QPEEYMAYVQ RQADSKQYGD KIIEELQDLG PQVWSETKSG VAPQKMAGAS 310 320 330 340 350 360 PTKDDSKDSD FWKMLNEPED QAPGGEEVPA EEQDPSPEAA DSASGAPNDF QNNVQVKVIR 370 380 390 400 410 420 SPADLIRFIE ELKGGTKKGK PNIGQEQPVD DAAEVPQREP EKERGDPERQ REMEEEEDED 430 440 450 460 470 480 EDEDEDEDER QLLGEFEKEL EGILLPSDRD RLRSEVKAGM ERELENIIQE TEKELDPDGL 490 500 510 520 530 540 KKESERDRAM LALTSTLNKL IKRLEEKQSP ELVKKHKKKR VVPKKPPPSP QPTEEDPEHR 550 560 570 580 590 600 VRVRVTKLRL GGPNQDLTVL EMKRENPQLK QIEGLVKELL EREGLTAAGK IEIKIVRPWA 610 620 630 640 650 660 EGTEEGARWL TDEDTRNLKE IFFNILVPGA EEAQKERQRQ KELESNYRRV WGSPGGEGTG DLDEFDF
	Isoform 2 (OS-9-2) [UniParc]. Checksum: 1FD06F7B23101015	FASTA	612	69,246
	10 20 30 40 50 60 MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV MGGQSQSSDV 70 80 90 100 110 120 VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY 130 140 150 160 170 180 EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS AFDWDDETAK ASKQHRLKRY HSQTYGNGSK 190 200 210 220 230 240 CDLNGRPREA EVRFLCDEGA GISGDYIDRV DEPLSCSYVL TIRTPRLCPH PLLRPPPSAA 250 260 270 280 290 300 PQAILCHPSL QPEEYMAYVQ RQADSKQYGD KIIEELQDLG PQVWSETKSG VAPQKMAGAS 310 320 330 340 350 360 PTKDDSKDSD FWKMLNEPED QAPGGEEVPA EEQDPSPEAA DSASGAPNDF QNNVQVKVIR 370 380 390 400 410 420 SPADLIRFIE ELKGGTKKGK PNIGQEQPVD DAAEVPQREP EKERGDPERQ REMEEEEDED 430 440 450 460 470 480 EDEDEDEDER QLLGEFEKEL EGILLPSDRD RLRSEVKAGM ERELENIIQE TEKELDPDGL 490 500 510 520 530 540 KKESERDRAM LALTSTLNKL IKRLEEKQSP ELVKKHKKKR VVPKKPPPSP QPTGKIEIKI 550 560 570 580 590 600 VRPWAEGTEE GARWLTDEDT RNLKEIFFNI LVPGAEEAQK ERQRQKELES NYRRVWGSPG 610 GEGTGDLDEF DF
	Isoform 3 (OS-9-3) [UniParc]. Checksum: 7D00C1EA449B3DA1	FASTA	597	67,505
	10 20 30 40 50 60 MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV MGGQSQSSDV 70 80 90 100 110 120 VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY 130 140 150 160 170 180 EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS AFDWDDETAK ASKQHRLKRY HSQTYGNGSK 190 200 210 220 230 240 CDLNGRPREA EVRFLCDEGA GISGDYIDRV DEPLSCSYVL TIRTPRLCPH PLLRPPPSAA 250 260 270 280 290 300 PQAILCHPSL QPEEYMAYVQ RQADSKQYGD KIIEELQDLG PQVWSETKSG VAPQKMAGAS 310 320 330 340 350 360 PTKDDSKDSD FWKMLNEPED QAPGGEEVPA EEQDPSPEAA DSASGAPNDF QNNVQVKVIR 370 380 390 400 410 420 SPADLIRFIE ELKGGTKKGK PNIGQEQPVD DAAEVPQREP EKERGDPERQ REMEEEEDED 430 440 450 460 470 480 EDEDEDEDER QLLGEFEKEL EGILLPSDRD RLRSETEKEL DPDGLKKESE RDRAMLALTS 490 500 510 520 530 540 TLNKLIKRLE EKQSPELVKK HKKKRVVPKK PPPSPQPTGK IEIKIVRPWA EGTEEGARWL 550 560 570 580 590 TDEDTRNLKE IFFNILVPGA EEAQKERQRQ KELESNYRRV WGSPGGEGTG DLDEFDF
	Isoform 4 [UniParc]. Checksum: 7D44F2347B609055	FASTA	652	73,821
	10 20 30 40 50 60 MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV MGGQSQSSDV 70 80 90 100 110 120 VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY 130 140 150 160 170 180 EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS AFDWDDETAK ASKQHRLKRY HSQTYGNGSK 190 200 210 220 230 240 CDLNGRPREA EVRFLCDEGA GISGDYIDRV DEPLSCSYVL TIRTPRLCPH PLLRPPPSAA 250 260 270 280 290 300 PQAILCHPSL QPEEYMAYVQ RQADSKQYGD KIIEELQDLG PQVWSETKSG VAPQKMAGAS 310 320 330 340 350 360 PTKDDSKDSD FWKMLNEPED QAPGGEEVPA EEQDPSPEAA DSASGAPNDF QNNVQVKVIR 370 380 390 400 410 420 SPADLIRFIE ELKGGTKKGK PNIGQEQPVD DAAEVPQREP EKERGDPERQ REMEEEEDED 430 440 450 460 470 480 EDEDEDEDER QLLGEFEKEL EGILLPSDRD RLRSETEKEL DPDGLKKESE RDRAMLALTS 490 500 510 520 530 540 TLNKLIKRLE EKQSPELVKK HKKKRVVPKK PPPSPQPTEE DPEHRVRVRV TKLRLGGPNQ 550 560 570 580 590 600 DLTVLEMKRE NPQLKQIEGL VKELLEREGL TAAGKIEIKI VRPWAEGTEE GARWLTDEDT 610 620 630 640 650 RNLKEIFFNI LVPGAEEAQK ERQRQKELES NYRRVWGSPG GEGTGDLDEF DF
	Isoform 5 [UniParc]. Checksum: BE4EEA80CF8EA076	FASTA	580	65,520
	10 20 30 40 50 60 MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV MGGQSQSSDV 70 80 90 100 110 120 VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY 130 140 150 160 170 180 EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS AFDWDDETAK FLCDEGAGIS GDYIDRVDEP 190 200 210 220 230 240 LSCSYVLTIR TPRLCPHPLL RPPPSAAPQA ILCHPSLQPE EYMAYVQRQA VDSKQYGDKI 250 260 270 280 290 300 IEELQDLGPQ VWSETKSGVA PQKMAGASPT KDDSKDSDFW KMLNEPEDQA PGGEEVPAEE 310 320 330 340 350 360 QDPSPEAADS ASGAPNDFQN NVQVKVIRSP ADLIRFIEEL KGGTKKGKPN IGQEQPVDDA 370 380 390 400 410 420 AEVPQREPEK ERGDPERQRE MEEEEDEDED EDEDEDERQL LGEFEKELEG ILLPSDRDRL 430 440 450 460 470 480 RSEVKAGMER ELENIIQETE KELDPDGLKK ESERDRAMLA LTSTLNKLIK RLEEKQSPEL 490 500 510 520 530 540 VKKHKKKRVV PKKPPPSPQP TGKIEIKIVR PWAEGTEEGA RWLTDEDTRN LKEIFFNILV 550 560 570 580 PGAEEAQKER QRQKELESNY RRVWGSPGGE GTGDLDEFDF
	Isoform 6 [UniParc]. Checksum: EBF3F8A812BDAF60	FASTA	560	63,155
	10 20 30 40 50 60 MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV MGGQSQSSDV 70 80 90 100 110 120 VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY 130 140 150 160 170 180 EFCYGRHIQQ YHMEDSEIKG EFLCDEGAGI SGDYIDRVDE PLSCSYVLTI RTPRLCPHPL 190 200 210 220 230 240 LRPPPSAAPQ AILCHPSLQP EEYMAYVQRQ ADSKQYGDKI IEELQDLGPQ VWSETKSGVA 250 260 270 280 290 300 PQKMAGASPT KDDSKDSDFW KMLNEPEDQA PGGEEVPAEE QDPSPEAADS ASGAPNDFQN 310 320 330 340 350 360 NVQVKVIRSP ADLIRFIEEL KGGTKKGKPN IGQEQPVDDA AEVPQREPEK ERGDPERQRE 370 380 390 400 410 420 MEEEEDEDED EDEDEDERQL LGEFEKELEG ILLPSDRDRL RSEVKAGMER ELENIIQETE 430 440 450 460 470 480 KELDPDGLKK ESERDRAMLA LTSTLNKLIK RLEEKQSPEL VKKHKKKRVV PKKPPPSPQP 490 500 510 520 530 540 TGKIEIKIVR PWAEGTEEGA RWLTDEDTRN LKEIFFNILV PGAEEAQKER QRQKELESNY 550 560 RRVWGSPGGE GTGDLDEFDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 AND 6), 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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 ENDOPLASMIC RETICULUM 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U41635 mRNA. Translation: AAB06495.1.
AB002805 Genomic DNA. Translation: BAA24362.1.
AB002806 mRNA. Translation: BAA24363.1.
AK291374 mRNA. Translation: BAF84063.1.
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: 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.

IPI

IPI00186581.
IPI00329760.
IPI00398855.
IPI00604451.
IPI00791882.
IPI00793206.
IPI00873981.

PIR

JC5889.

RefSeq

NP_001017956.1. NM_001017956.2.
NP_001017957.1. NM_001017957.2.
NP_001017958.1. NM_001017958.2.
NP_001248349.1. NM_001261420.1.
NP_001248350.1. NM_001261421.1.
NP_001248351.1. NM_001261422.1.
NP_001248352.1. NM_001261423.1.
NP_006803.1. NM_006812.3.

UniGene

Hs.527861.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3AIH	X-ray	2.10	A/B	108-229	[»]

ProteinModelPortal

Q13438.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37493N.

IntAct

Q13438. 20 interactions.

MINT

MINT-1187753.

STRING

9606.ENSP00000318165.

PTM databases

PhosphoSite

Q13438.

Polymorphism databases

DMDM

3024310.

Proteomic databases

PaxDb

Q13438.

PRIDE

Q13438.

Protocols and materials databases

DNASU

10956.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000315970; ENSP00000318165; ENSG00000135506.
ENST00000389142; ENSP00000373794; ENSG00000135506.
ENST00000389146; ENSP00000373798; ENSG00000135506.
ENST00000435406; ENSP00000389632; ENSG00000135506.
ENST00000551035; ENSP00000447866; ENSG00000135506.
ENST00000552285; ENSP00000450010; ENSG00000135506.

GeneID

10956.

KEGG

hsa:10956.

UCSC

uc001spj.3. human.

Organism-specific databases

CTD

10956.

GeneCards

GC12P058088.

HGNC

HGNC:16994. OS9.

HPA

CAB011518.
HPA013694.

MIM

609677. gene.

neXtProt

NX_Q13438.

PharmGKB

PA164724245.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG309879.

HOGENOM

HOG000293348.

HOVERGEN

HBG000974.

InParanoid

Q13438.

KO

K10088.

OMA

RYHSQTY.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1apathway. Hypoxic and oxygen homeostasis regulation of HIF-1-alpha.

Gene expression databases

ArrayExpress

Q13438.

Bgee

Q13438.

Genevestigator

Q13438.

GermOnline

ENSG00000135506. Homo sapiens.

Family and domain databases

InterPro

IPR009011. Man6P_isomerase_rcpt-bd_dom.
IPR012913. PRKCSH.
[Graphical view]

Pfam

PF07915. PRKCSH. 1 hit.
[Graphical view]

SUPFAM

SSF50911. Man6php_recept. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

OS9. human.

EvolutionaryTrace

Q13438.

GenomeRNAi

10956.

NextBio

35464261.

SOURCE

Search...

Entry information

Entry name

OS9_HUMAN

Accession

Primary (citable) accession number: Q13438
Secondary accession number(s): A6NDD1 , A6NFR7, A6NLB2, A8K5Q9, B4DPX1, B4E1I6, E7ENT8, F8VUH2, O00579, Q6IBL2, Q8IZ58, Q9BW99

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.