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Q9BXB4

- OSB11_HUMAN

UniProt

Q9BXB4 - OSB11_HUMAN

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Protein

Oxysterol-binding protein-related protein 11

Gene

OSBPL11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. fat cell differentiation Source: BHF-UCL
  2. lipid transport Source: UniProtKB-KW
  3. positive regulation of sequestering of triglyceride Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein-related protein 11
Short name:
ORP-11
Short name:
OSBP-related protein 11
Gene namesi
Name:OSBPL11
Synonyms:ORP11, OSBP12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:16397. OSBPL11.

Subcellular locationi

Late endosome membrane 1 Publication. Golgi apparatustrans-Golgi network membrane 1 Publication
Note: Localizes at the Golgi-late endosome interface.

GO - Cellular componenti

  1. endosome Source: UniProtKB-KW
  2. Golgi apparatus Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32825.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 747747Oxysterol-binding protein-related protein 11PRO_0000100381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei27 – 271Phosphothreonine4 Publications
Modified residuei62 – 621Phosphotyrosine1 Publication
Modified residuei172 – 1721Phosphoserine1 Publication
Modified residuei174 – 1741Phosphoserine1 Publication
Modified residuei177 – 1771PhosphoserineBy similarity
Modified residuei181 – 1811Phosphoserine4 Publications
Modified residuei189 – 1891Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BXB4.
PaxDbiQ9BXB4.
PRIDEiQ9BXB4.

PTM databases

PhosphoSiteiQ9BXB4.

Expressioni

Tissue specificityi

Present at highest levels in ovary, testis, kidney, liver, stomach, brain, and adipose tissue. Strong expression (at protein level) in epithelial cells of kidney tubules, testicular tubules, caecum, and skin.1 Publication

Gene expression databases

BgeeiQ9BXB4.
CleanExiHS_OSBPL11.
ExpressionAtlasiQ9BXB4. baseline and differential.
GenevestigatoriQ9BXB4.

Organism-specific databases

HPAiHPA039144.

Interactioni

Subunit structurei

Heterodimer with OSBPL9.1 Publication

Protein-protein interaction databases

BioGridi125386. 15 interactions.
IntActiQ9BXB4. 1 interaction.
STRINGi9606.ENSP00000296220.

Structurei

Secondary structure

1
747
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi62 – 709
Turni71 – 733
Beta strandi74 – 829
Turni84 – 863
Beta strandi88 – 947
Helixi95 – 973
Beta strandi98 – 1003
Beta strandi103 – 1075
Beta strandi117 – 1215
Beta strandi123 – 1253
Beta strandi128 – 1303
Beta strandi133 – 1353
Helixi140 – 16021

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9XNMR-A59-165[»]
ProteinModelPortaliQ9BXB4.
SMRiQ9BXB4. Positions 59-165, 368-747.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BXB4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 15598PHPROSITE-ProRule annotationAdd
BLAST

Domaini

The PH domain binds phosphoinositides.1 Publication

Sequence similaritiesi

Belongs to the OSBP family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG262374.
GeneTreeiENSGT00550000074515.
HOGENOMiHOG000233871.
HOVERGENiHBG053376.
InParanoidiQ9BXB4.
OMAiVTNHAPL.
OrthoDBiEOG7PK8ZG.
PhylomeDBiQ9BXB4.
TreeFamiTF312807.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 1 hit.
PfamiPF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BXB4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQGGEPVSTM KVSESEGKLE GQATAVTPNK NSSCGGGISS SSSSRGGSAK
60 70 80 90 100
GWQYSDHMEN VYGYLMKYTN LVTGWQYRFF VLNNEAGLLE YFVNEQSRNQ
110 120 130 140 150
KPRGTLQLAG AVISPSDEDS HTFTVNAASG EQYKLRATDA KERQHWVSRL
160 170 180 190 200
QICTQHHTEA IGKNNPPLKS RSFSLASSSN SPISQRRPSQ NAISFFNVGH
210 220 230 240 250
SKLQSLSKRT NLPPDHLVEV REMMSHAEGQ QRDLIRRIEC LPTSGHLSSL
260 270 280 290 300
DQDLLMLKAT SMATMNCLND CFHILQLQHA SHQKGSLPSG TTIEWLEPKI
310 320 330 340 350
SLSNHYKNGA DQPFATDQSK PVAVPEEQPV AESGLLAREP EEINADDEIE
360 370 380 390 400
DTCDHKEDDL GAVEEQRSVI LHLLSQLKLG MDLTRVVLPT FILEKRSLLE
410 420 430 440 450
MYADFMSHPD LFIAITNGAT AEDRMIRFVE YYLTSFHEGR KGAIAKKPYN
460 470 480 490 500
PIIGETFHCS WKMPKSEVAS SVFSSSSTQG VTNHAPLSGE SLTQVGSDCY
510 520 530 540 550
TVRFVAEQVS HHPPVSGFYA ECTERKMCVN AHVWTKSKFL GMSIGVTMVG
560 570 580 590 600
EGILSLLEHG EEYTFSLPCA YARSILTVPW VELGGKVSVN CAKTGYSASI
610 620 630 640 650
TFHTKPFYGG KLHRVTAEVK HNITNTVVCR VQGEWNSVLE FTYSNGETKY
660 670 680 690 700
VDLTKLAVTK KRVRPLEKQD PFESRRLWKN VTDSLRESEI DKATEHKHTL
710 720 730 740
EERQRTEERH RTETGTPWKT KYFIKEGDGW VYHKPLWKII PTTQPAE
Length:747
Mass (Da):83,643
Last modified:February 11, 2002 - v2
Checksum:iB443D3BDE8AE5FB6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti184 – 1841S → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_036100

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3033.1.
RefSeqiNP_073613.2. NM_022776.4.
UniGeneiHs.477440.

Genome annotation databases

EnsembliENST00000296220; ENSP00000296220; ENSG00000144909.
GeneIDi114885.
KEGGihsa:114885.
UCSCiuc003eic.3. human.

Polymorphism databases

DMDMi20139127.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3033.1.
RefSeqi NP_073613.2. NM_022776.4.
UniGenei Hs.477440.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D9X NMR - A 59-165 [» ]
ProteinModelPortali Q9BXB4.
SMRi Q9BXB4. Positions 59-165, 368-747.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125386. 15 interactions.
IntActi Q9BXB4. 1 interaction.
STRINGi 9606.ENSP00000296220.

PTM databases

PhosphoSitei Q9BXB4.

Polymorphism databases

DMDMi 20139127.

Proteomic databases

MaxQBi Q9BXB4.
PaxDbi Q9BXB4.
PRIDEi Q9BXB4.

Protocols and materials databases

DNASUi 114885.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296220 ; ENSP00000296220 ; ENSG00000144909 .
GeneIDi 114885.
KEGGi hsa:114885.
UCSCi uc003eic.3. human.

Organism-specific databases

CTDi 114885.
GeneCardsi GC03M125278.
HGNCi HGNC:16397. OSBPL11.
HPAi HPA039144.
MIMi 606739. gene.
neXtProti NX_Q9BXB4.
PharmGKBi PA32825.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262374.
GeneTreei ENSGT00550000074515.
HOGENOMi HOG000233871.
HOVERGENi HBG053376.
InParanoidi Q9BXB4.
OMAi VTNHAPL.
OrthoDBi EOG7PK8ZG.
PhylomeDBi Q9BXB4.
TreeFami TF312807.

Miscellaneous databases

ChiTaRSi OSBPL11. human.
EvolutionaryTracei Q9BXB4.
GeneWikii OSBPL11.
GenomeRNAii 114885.
NextBioi 79389.
PROi Q9BXB4.
SOURCEi Search...

Gene expression databases

Bgeei Q9BXB4.
CleanExi HS_OSBPL11.
ExpressionAtlasi Q9BXB4. baseline and differential.
Genevestigatori Q9BXB4.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
PANTHERi PTHR10972. PTHR10972. 1 hit.
Pfami PF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
[Graphical view ]
PROSITEi PS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27; SER-181 AND SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "OSBP-related protein 11 (ORP11) dimerizes with ORP9 and localizes at the Golgi-late endosome interface."
    Zhou Y., Li S., Mayranpaa M.I., Zhong W., Back N., Yan D., Olkkonen V.M.
    Exp. Cell Res. 316:3304-3316(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  14. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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.
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-184.

Entry informationi

Entry nameiOSB11_HUMAN
AccessioniPrimary (citable) accession number: Q9BXB4
Secondary accession number(s): A8K9I7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: February 11, 2002
Last modified: October 29, 2014
This is version 115 of the entry and version 2 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 3
    Human chromosome 3: 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