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Q13438 (OS9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein OS-9
Alternative name(s):
Amplified in osteosarcoma 9
Gene names
Name:OS9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length667 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 detectedin 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EGLN1Q9GZT94EBI-725454,EBI-1174818
HIF1AQ166659EBI-725454,EBI-447269

Alternative products

This entry describes 8 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.
Isoform 7 (identifier: Q13438-7)

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.
Isoform 8 (identifier: Q13438-8)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 667642Protein OS-9
PRO_0000021951

Regions

Domain108 – 17871PRKCSH
Compositional bias414 – 42916Asp/Glu-rich (acidic)

Sites

Binding site1301Carbohydrate
Binding site1821Carbohydrate
Binding site1881Carbohydrate
Binding site2121Carbohydrate
Binding site2181Carbohydrate

Amino acid modifications

Glycosylation1771N-linked (GlcNAc...) Potential
Disulfide bond110 ↔ 123 Ref.11 Ref.17
Disulfide bond181 ↔ 216 Ref.11 Ref.17
Disulfide bond196 ↔ 228 Ref.11 Ref.17

Natural variations

Alternative sequence55 – 11359Missing in isoform 8.
VSP_046770
Alternative sequence142 – 19352Missing in isoform 6.
VSP_046001
Alternative sequence161 – 19333Missing in isoform 5.
VSP_044701
Alternative sequence2631A → AV in isoform 5 and isoform 7.
VSP_044702
Alternative sequence456 – 47015Missing in isoform 3, isoform 4 and isoform 8.
VSP_004352
Alternative sequence534 – 58855Missing in isoform 2, isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_004353
Natural variant3051D → N. Ref.4
Corresponds to variant rs141986192 [ dbSNP | Ensembl ].
VAR_069062
Natural variant3981R → W.
Corresponds to variant rs1804598 [ dbSNP | Ensembl ].
VAR_011897
Natural variant4541S → L.
Corresponds to variant rs34764811 [ dbSNP | Ensembl ].
VAR_034364

Experimental info

Mutagenesis1881R → 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 conflict71L → V in CAG33072. Ref.5
Sequence conflict1941F → V in BAG64798. Ref.4
Sequence conflict3711E → G in BAG56939. Ref.4
Sequence conflict4971L → F in BAG64798. Ref.4
Sequence conflict5221V → I in BAG60733. Ref.4
Sequence conflict6531S → P in BAG56939. Ref.4

Secondary structure

.................... 667
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (OS-9-1) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 65BA3F66CEC58756

FASTA66775,562
        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 

« Hide

Isoform 2 (OS-9-2) [UniParc].

Checksum: 1FD06F7B23101015
Show »

FASTA61269,246
Isoform 3 (OS-9-3) [UniParc].

Checksum: 7D00C1EA449B3DA1
Show »

FASTA59767,505
Isoform 4 [UniParc].

Checksum: 7D44F2347B609055
Show »

FASTA65273,821
Isoform 5 [UniParc].

Checksum: BE4EEA80CF8EA076
Show »

FASTA58065,520
Isoform 6 [UniParc].

Checksum: EBF3F8A812BDAF60
Show »

FASTA56063,155
Isoform 7 [UniParc].

Checksum: 353DE17278AB9546
Show »

FASTA61369,346
Isoform 8 [UniParc].

Checksum: 30188F4A2A67AD8E
Show »

FASTA53860,847

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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 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.
+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.
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.
PIRJC5889.
RefSeqNP_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.
UniGeneHs.527861.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AIHX-ray2.10A/B108-229[»]
ProteinModelPortalQ13438.
SMRQ13438. Positions 109-228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116156. 45 interactions.
DIPDIP-37493N.
IntActQ13438. 24 interactions.
MINTMINT-1187753.
STRING9606.ENSP00000318165.

PTM databases

PhosphoSiteQ13438.

Polymorphism databases

DMDM3024310.

Proteomic databases

PaxDbQ13438.
PRIDEQ13438.

Protocols and materials databases

DNASU10956.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257966; 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]
GeneID10956.
KEGGhsa:10956.
UCSCuc001spj.3. human. [Q13438-1]
uc001spk.3. human. [Q13438-4]
uc001spn.3. human.

Organism-specific databases

CTD10956.
GeneCardsGC12P058088.
HGNCHGNC:16994. OS9.
HPACAB011518.
HPA013694.
MIM609677. gene.
neXtProtNX_Q13438.
PharmGKBPA164724245.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG309879.
HOGENOMHOG000293348.
HOVERGENHBG000974.
InParanoidQ13438.
KOK10088.
OMARYHSQTY.
OrthoDBEOG7R8315.
PhylomeDBQ13438.
TreeFamTF314309.

Gene expression databases

ArrayExpressQ13438.
BgeeQ13438.
GenevestigatorQ13438.

Family and domain databases

Gene3D2.70.130.10. 1 hit.
InterProIPR009011. Man6P_isomerase_rcpt-bd_dom.
IPR012913. PRKCSH.
[Graphical view]
PfamPF07915. PRKCSH. 1 hit.
[Graphical view]
SUPFAMSSF50911. SSF50911. 1 hit.
ProtoNetSearch...

Other

ChiTaRSOS9. human.
EvolutionaryTraceQ13438.
GeneWikiOS9_(gene).
GenomeRNAi10956.
NextBio35464261.
PROQ13438.
SOURCESearch...

Entry information

Entry nameOS9_HUMAN
AccessionPrimary (citable) accession number: Q13438
Secondary accession number(s): A6NDD1 expand/collapse secondary AC list , A6NFR7, A6NLB2, A8K5Q9, B4DE28, B4DPX1, B4E1I6, E7ENT8, E7EW91, F8VUH2, G3XA88, O00579, Q6IBL2, Q8IZ58, Q9BW99
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM