Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9H267 (VP33B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vacuolar protein sorting-associated protein 33B

Short name=hVPS33B
Gene names
Name:VPS33B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length617 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. Mediates phagolysosomal fusion in macrophages. Ref.6

Subunit structure

Interacts with RAB11A and VIPAS39. Interacts with M.tuberculosis PtpA. Ref.6 Ref.8

Subcellular location

Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. Lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Note: Cytoplasmic, peripheral membrane protein associated with late endosomes/lysosomes. Colocalizes with M.tuberculosis PtpA in the cytosol of tuberculosis-infected macrophages and associates with phagosomes. Colocalizes in clusters with VIPAS39 at cytoplasmic organelles. Ref.6 Ref.8 Ref.10

Tissue specificity

Ubiquitous; highly expressed in testis and low expression in the lung.

Post-translational modification

Phosphorylated on tyrosine residues. Dephosphorylation by M.tuberculosis PtpA is necessary to induce the reduction of host phagolysosome fusion in M.tuberculosis-infected macrophages. Ref.6

Involvement in disease

Arthrogryposis, renal dysfunction and cholestasis syndrome 1 (ARCS1) [MIM:208085]: A multisystem disorder, characterized by neurogenic arthrogryposis multiplex congenita, renal tubular dysfunction and neonatal cholestasis with bile duct hypoplasia and low gamma glutamyl transpeptidase activity. Platelet dysfunction is common.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.10 Ref.11

Sequence similarities

Belongs to the STXBP/unc-18/SEC1 family.

Caution

According to Ref.6, it is autophosphorylated. However, it is not related with protein kinases, suggesting it is phosphorylated by another protein.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VIPAS39Q9H9C120EBI-749072,EBI-749080

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 617616Vacuolar protein sorting-associated protein 33B
PRO_0000206305

Amino acid modifications

Modified residue21N-acetylalanine Ref.7

Natural variations

Natural variant301L → P in ARCS1; interacts with VIPAS39 but does not colocalize with VIPAS39 at cytoplasmic organelles. Ref.8 Ref.10
VAR_018983
Natural variant2431S → F in ARCS1. Ref.11
VAR_057901
Natural variant5131F → S.
Corresponds to variant rs3177428 [ dbSNP | Ensembl ].
VAR_057330
Natural variant5141G → S. Ref.1 Ref.3 Ref.5
Corresponds to variant rs11073964 [ dbSNP | Ensembl ].
VAR_013828

Experimental info

Mutagenesis1331Y → E: Reduces phosphorylation activity, but does not impair phagolysosomal fusion in M.tuberculosis-infected macrophages; when associated with E-382; E-511 and E-517. Ref.6
Mutagenesis3821Y → E: Reduces phosphorylation activity, but does not impair phagolysosomal fusion in M.tuberculosis-infected macrophages; when associated with E-133; E-511 and E-517. Ref.6
Mutagenesis5111Y → E: Reduces phosphorylation activity, but does not impair phagolysosomal fusion in M.tuberculosis-infected macrophages; when associated with E-133; E-382 and E-517. Ref.6
Mutagenesis5171Y → E: Reduces phosphorylation activity, but does not impair phagolysosomal fusion in M.tuberculosis-infected macrophages; when associated with E-133; E-382 and E-511. Ref.6
Sequence conflict2931H → Y in BAB55345. Ref.3
Sequence conflict4661K → E in BAB55345. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9H267 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: BD7DB97E1FEB1D32

FASTA61770,585
        10         20         30         40         50         60 
MAFPHRPDAP ELPDFSMLKR LARDQLIYLL EQLPGKKDLF IEADLMSPLD RIANVSILKQ 

        70         80         90        100        110        120 
HEVDKLYKVE NKPALSSNEQ LCFLVRPRIK NMRYIASLVN ADKLAGRTRK YKVIFSPQKF 

       130        140        150        160        170        180 
YACEMVLEEE GIYGDVSCDE WAFSLLPLDV DLLSMELPEF FRDYFLEGDQ RWINTVAQAL 

       190        200        210        220        230        240 
HLLSTLYGPF PNCYGIGRCA KMAYELWRNL EEEEDGETKG RRPEIGHIFL LDRDVDFVTA 

       250        260        270        280        290        300 
LCSQVVYEGL VDDTFRIKCG SVDFGPEVTS SDKSLKVLLN AEDKVFNEIR NEHFSNVFGF 

       310        320        330        340        350        360 
LSQKARNLQA QYDRRRGMDI KQMKNFVSQE LKGLKQEHRL LSLHIGACES IMKKKTKQDF 

       370        380        390        400        410        420 
QELIKTEHAL LEGFNIREST SYIEEHIDRQ VSPIESLRLM CLLSITENGL IPKDYRSLKT 

       430        440        450        460        470        480 
QYLQSYGPEH LLTFSNLRRA GLLTEQAPGD TLTAVESKVS KLVTDKAAGK ITDAFSSLAK 

       490        500        510        520        530        540 
RSNFRAISKK LNLIPRVDGE YDLKVPRDMA YVFGGAYVPL SCRIIEQVLE RRSWQGLDEV 

       550        560        570        580        590        600 
VRLLNCSDFA FTDMTKEDKA SSESLRLILV VFLGGCTFSE ISALRFLGRE KGYRFIFLTT 

       610 
AVTNSARLME AMSEVKA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, mapping and expression analysis of VPS33B, the human orthologue of rat Vps33b."
Carim-Todd L., Sumoy L., Andreu N., Estivill X., Escarceller M.
Cytogenet. Cell Genet. 89:92-95(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-514.
[2]"Molecular cloning and characterization of human VPS18, VPS11, VPS16, and VPS33."
Huizing M., Didier A., Walenta J., Anikster Y., Gahl W.A., Kraemer H.
Gene 264:241-247(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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], VARIANT SER-514.
Tissue: Placenta.
[4]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANT SER-514.
Tissue: Placenta.
[6]"Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B."
Bach H., Papavinasasundaram K.G., Wong D., Hmama Z., Av-Gay Y.
Cell Host Microbe 3:316-322(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEPHOSPHORYLATION, PHOSPHORYLATION, INTERACTION WITH MYCOBACTERIUM TUBERCULOSIS PTPA, MUTAGENESIS OF TYR-133; TYR-382; TYR-511 AND TYR-517, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"Mutations in VIPAR cause an arthrogryposis, renal dysfunction and cholestasis syndrome phenotype with defects in epithelial polarization."
Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y., Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B., Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P., Thomas S.G., Rappoport J.Z. expand/collapse author list , Arias I.M., Wolburg H., Knisely A.S., Kelly D.A., Muller F., Maher E.R., Gissen P.
Nat. Genet. 42:303-312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11A AND VIPAS39, CHARACTERIZATION OF VARIANT ARCS1 PRO-30, SUBCELLULAR LOCATION.
[9]"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].
[10]"Mutations in VPS33B, encoding a regulator of SNARE-dependent membrane fusion, cause arthrogryposis-renal dysfunction-cholestasis (ARC) syndrome."
Gissen P., Johnson C.A., Morgan N.V., Stapelbroek J.M., Forshew T., Cooper W.N., McKiernan P.J., Klomp L.W.J., Morris A.A.M., Wraith J.E., McClean P., Lynch S.A., Thompson R.J., Lo B., Quarrell O.W., Di Rocco M., Trembath R.C., Mandel H. expand/collapse author list , Wali S., Karet F.E., Knisely A.S., Houwen R.H.J., Kelly D.A., Maher E.R.
Nat. Genet. 36:400-404(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARCS1 PRO-30, SUBCELLULAR LOCATION.
[11]"Molecular investigations to improve diagnostic accuracy in patients with ARC syndrome."
Cullinane A.R., Straatman-Iwanowska A., Seo J.K., Ko J.S., Song K.S., Gizewska M., Gruszfeld D., Gliwicz D., Tuysuz B., Erdemir G., Sougrat R., Wakabayashi Y., Hinds R., Barnicoat A., Mandel H., Chitayat D., Fischler B., Garcia-Cazorla A. expand/collapse author list , Knisely A.S., Kelly D.A., Maher E.R., Gissen P.
Hum. Mutat. 30:E330-E337(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARCS1 PHE-243.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF201694 mRNA. Translation: AAF91174.1.
AL357472 mRNA. Translation: CAB93109.1.
AF308803 mRNA. Translation: AAG34680.1.
AK027754 mRNA. Translation: BAB55345.1.
AC068831 Genomic DNA. No translation available.
BC016445 mRNA. Translation: AAH16445.1.
RefSeqNP_061138.3. NM_018668.4.
UniGeneHs.745007.

3D structure databases

ProteinModelPortalQ9H267.
SMRQ9H267. Positions 14-614.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117659. 22 interactions.
IntActQ9H267. 8 interactions.
MINTMINT-1451069.
STRING9606.ENSP00000327650.

PTM databases

PhosphoSiteQ9H267.

Polymorphism databases

DMDM313104046.

Proteomic databases

PaxDbQ9H267.
PRIDEQ9H267.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333371; ENSP00000327650; ENSG00000184056.
GeneID26276.
KEGGhsa:26276.
UCSCuc002bqp.1. human.

Organism-specific databases

CTD26276.
GeneCardsGC15M091541.
H-InvDBHIX0202153.
HGNCHGNC:12712. VPS33B.
HPAHPA040415.
MIM208085. phenotype.
608552. gene.
neXtProtNX_Q9H267.
Orphanet2697. Arthrogryposis - renal dysfunction - cholestasis.
PharmGKBPA37327.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5158.
HOGENOMHOG000166771.
HOVERGENHBG106182.
InParanoidQ9H267.
OMAKGYRFIF.
OrthoDBEOG722J85.
PhylomeDBQ9H267.
TreeFamTF315126.

Gene expression databases

ArrayExpressQ9H267.
BgeeQ9H267.
CleanExHS_VPS33B.
GenevestigatorQ9H267.

Family and domain databases

Gene3D3.40.50.1910. 2 hits.
InterProIPR027482. Sec-1-like_dom2.
IPR001619. Sec1-like.
IPR027121. VPS33.
[Graphical view]
PANTHERPTHR11679. PTHR11679. 1 hit.
PTHR11679:SF1. PTHR11679:SF1. 1 hit.
PfamPF00995. Sec1. 1 hit.
[Graphical view]
SUPFAMSSF56815. SSF56815. 2 hits.
ProtoNetSearch...

Other

GeneWikiVPS33B.
GenomeRNAi26276.
NextBio48583.
PROQ9H267.
SOURCESearch...

Entry information

Entry nameVP33B_HUMAN
AccessionPrimary (citable) accession number: Q9H267
Secondary accession number(s): Q96K14, Q9NRP6, Q9NSF3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 119 of the entry and version 2 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

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 15

Human chromosome 15: entries, gene names and cross-references to MIM