Q9BXB4 (OSB11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Oxysterol-binding protein-related protein 11
Short name=ORP-11
Short name=OSBP-related protein 11

Gene names

Name:	OSBPL11
Synonyms:	ORP11, OSBP12

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	747 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Tissue specificity	Widely expressed.
Sequence similarities	Belongs to the OSBP family. Contains 1 PH domain.

Ontologies

Keywords
Biological process	Lipid transport Transport
Coding sequence diversity	Polymorphism
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fat cell differentiation Inferred from mutant phenotype PubMed 23028956. Source: BHF-UCL lipid transport Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of sequestering of triglyceride Inferred from mutant phenotype PubMed 23028956. Source: BHF-UCL
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 747

747

Oxysterol-binding protein-related protein 11

PRO_0000100381

Regions

Domain

58 – 155

98

PH

Amino acid modifications

Modified residue

13

1

Phosphoserine By similarity

Modified residue

15

1

Phosphoserine By similarity

Modified residue

27

1

Phosphothreonine Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

62

1

Phosphotyrosine Ref.11

Modified residue

172

1

Phosphoserine Ref.11

Modified residue

174

1

Phosphoserine Ref.11

Modified residue

177

1

Phosphoserine By similarity

Modified residue

181

1

Phosphoserine Ref.7 Ref.10 Ref.11 Ref.12

Modified residue

184

1

Phosphoserine By similarity

Modified residue

189

1

Phosphoserine Ref.6 Ref.10 Ref.12 Ref.14

Natural variations

Natural variant

184

1

S → L in a breast cancer sample; somatic mutation. Ref.16

VAR_036100

Secondary structure

1

.

.

.

.

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.

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.

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.

.

.

.

.

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.

.

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.

747

Helix Strand Turn

Details...

Beta strand

62 – 70

9

Turn

71 – 73

3

Beta strand

74 – 82

9

Turn

84 – 86

3

Beta strand

88 – 94

7

Helix

95 – 97

3

Beta strand

98 – 100

3

Beta strand

103 – 107

5

Beta strand

117 – 121

5

Beta strand

123 – 125

3

Beta strand

128 – 130

3

Beta strand

133 – 135

3

Helix

140 – 160

21

Sequences

	Sequence		Length	Mass (Da)
	Q9BXB4 [UniParc]. Last modified February 11, 2002. Version 2. Checksum: B443D3BDE8AE5FB6	FASTA	747	83,643
	10 20 30 40 50 60 MQGGEPVSTM KVSESEGKLE GQATAVTPNK NSSCGGGISS SSSSRGGSAK GWQYSDHMEN 70 80 90 100 110 120 VYGYLMKYTN LVTGWQYRFF VLNNEAGLLE YFVNEQSRNQ KPRGTLQLAG AVISPSDEDS 130 140 150 160 170 180 HTFTVNAASG EQYKLRATDA KERQHWVSRL QICTQHHTEA IGKNNPPLKS RSFSLASSSN 190 200 210 220 230 240 SPISQRRPSQ NAISFFNVGH SKLQSLSKRT NLPPDHLVEV REMMSHAEGQ QRDLIRRIEC 250 260 270 280 290 300 LPTSGHLSSL DQDLLMLKAT SMATMNCLND CFHILQLQHA SHQKGSLPSG TTIEWLEPKI 310 320 330 340 350 360 SLSNHYKNGA DQPFATDQSK PVAVPEEQPV AESGLLAREP EEINADDEIE DTCDHKEDDL 370 380 390 400 410 420 GAVEEQRSVI LHLLSQLKLG MDLTRVVLPT FILEKRSLLE MYADFMSHPD LFIAITNGAT 430 440 450 460 470 480 AEDRMIRFVE YYLTSFHEGR KGAIAKKPYN PIIGETFHCS WKMPKSEVAS SVFSSSSTQG 490 500 510 520 530 540 VTNHAPLSGE SLTQVGSDCY TVRFVAEQVS HHPPVSGFYA ECTERKMCVN AHVWTKSKFL 550 560 570 580 590 600 GMSIGVTMVG EGILSLLEHG EEYTFSLPCA YARSILTVPW VELGGKVSVN CAKTGYSASI 610 620 630 640 650 660 TFHTKPFYGG KLHRVTAEVK HNITNTVVCR VQGEWNSVLE FTYSNGETKY VDLTKLAVTK 670 680 690 700 710 720 KRVRPLEKQD PFESRRLWKN VTDSLRESEI DKATEHKHTL EERQRTEERH RTETGTPWKT 730 740 KYFIKEGDGW VYHKPLWKII PTTQPAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A family of 12 human genes containing oxysterol-binding domains." Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R. Genomics 78:185-196(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]. Tissue: Thymus.
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: Skin.
[5]	"The OSBP-related protein family in humans." Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C., Staels B., Ikonen E., Olkkonen V.M. J. Lipid Res. 42:1203-1213(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-315.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27; SER-181 AND SER-189, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27; TYR-62; SER-172; SER-174 AND SER-181, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27; SER-181 AND SER-189, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, MASS SPECTROMETRY.
[15]	"Solution structure of the PH domain of oxysterol binding protein-related protein 11 from human." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 59-165.
[16]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-184.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF392454 mRNA. Translation: AAL40667.1.
AK292702 mRNA. Translation: BAF85391.1.
CH471052 Genomic DNA. Translation: EAW79389.1.
BC065213 mRNA. Translation: AAH65213.1.
AF346292 mRNA. Translation: AAK31141.1.

IPI

IPI00032970.

RefSeq

NP_073613.2. NM_022776.4.

UniGene

Hs.477440.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D9X	NMR	-	A	59-165	[»]

ProteinModelPortal

Q9BXB4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BXB4. 1 interaction.

PTM databases

PhosphoSite

Q9BXB4.

Polymorphism databases

DMDM

20139127.

Proteomic databases

PaxDb

Q9BXB4.

PRIDE

Q9BXB4.

Protocols and materials databases

DNASU

114885.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296220; ENSP00000296220; ENSG00000144909.

GeneID

114885.

KEGG

hsa:114885.

UCSC

uc003eic.3. human.

Organism-specific databases

CTD

114885.

GeneCards

GC03M125278.

HGNC

HGNC:16397. OSBPL11.

HPA

HPA039144.

MIM

606739. gene.

neXtProt

NX_Q9BXB4.

PharmGKB

PA32825.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG262374.

HOGENOM

HOG000233871.

HOVERGEN

HBG053376.

InParanoid

Q9BXB4.

OMA

TMVGEGI.

OrthoDB

EOG4TQM8K.

PhylomeDB

Q9BXB4.

Gene expression databases

ArrayExpress

Q9BXB4.

Bgee

Q9BXB4.

CleanEx

HS_OSBPL11.

Genevestigator

Q9BXB4.

GermOnline

ENSG00000144909. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]

PANTHER

PTHR10972. PTHR10972. 1 hit.

Pfam

PF01237. Oxysterol_BP. 2 hits.
PF00169. PH. 1 hit.
[Graphical view]

SMART

SM00233. PH. 1 hit.
[Graphical view]

PROSITE

PS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

OSBPL11. human.

EvolutionaryTrace

Q9BXB4.

GenomeRNAi

114885.

NextBio

79389.

SOURCE

Search...

Entry information

Entry name

OSB11_HUMAN

Accession

Primary (citable) accession number: Q9BXB4
Secondary accession number(s): A8K9I7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 11, 2002
Last sequence update:	February 11, 2002
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 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.