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Q9Y5P4 (C43BP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen type IV alpha-3-binding protein
Alternative name(s):
Ceramide transfer protein
Short name=hCERT
Goodpasture antigen-binding protein
Short name=GPBP
START domain-containing protein 11
Short name=StARD11
StAR-related lipid transfer protein 11
Gene names
Name:COL4A3BP
Synonyms:CERT, STARD11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length624 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. Ref.3 Ref.11 Ref.16 Ref.17

Subunit structure

Interacts with COL4A3. Interacts with VAPA and VAPB. Interaction with VAPB is less efficient than with VAPA. Ref.10

Subcellular location

Cytoplasm. Golgi apparatus. Endoplasmic reticulum. Note: Preferentially localized to the Golgi apparatus. Ref.3 Ref.10 Ref.16

Tissue specificity

Widely expressed.

Domain

The START domain recognizes ceramides and diacylglycerol lipids, interacts with membranes, and mediates the intermembrane transfer of ceramides and diacylglycerol lipids. Ref.3

The PH domain targets the Golgi apparatus. Ref.3

The FFAT motif is required for interaction with VAPA and VAPB. Ref.3

Post-translational modification

Phosphorylation on Ser-132 decreases the affinity toward phosphatidylinositol 4-phosphate at Golgi membranes and reduces ceramide transfer activity. Inactivated by hyperphosphorylation of serine residues by CSNK1G2/CK1 that triggers dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis.

Sequence similarities

Contains 1 PH domain.

Contains 1 START domain.

Caution

Was originally (Ref.1) reported to have a protein kinase activity and to phosphorylate on Ser and Thr residues the Goodpasture autoantigen (in vitro).

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentCytoplasm
Endoplasmic reticulum
Golgi apparatus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER to Golgi ceramide transport

Inferred from mutant phenotype Ref.16. Source: UniProtKB

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

ceramide metabolic process

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum organization

Inferred from electronic annotation. Source: Ensembl

heart morphogenesis

Inferred from electronic annotation. Source: Ensembl

immune response

Non-traceable author statement Ref.2. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

lipid homeostasis

Inferred from electronic annotation. Source: Ensembl

mitochondrion morphogenesis

Inferred from electronic annotation. Source: Ensembl

muscle contraction

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

response to endoplasmic reticulum stress

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid biosynthetic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.16. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionceramide binding

Inferred from direct assay Ref.3Ref.16. Source: UniProtKB

ceramide transporter activity

Inferred from direct assay Ref.16. Source: UniProtKB

phosphatidylinositol-4-phosphate binding

Inferred from direct assay Ref.3. Source: UniProtKB

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5P4-1)

Also known as: CERTL;

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.
Isoform 2 (identifier: Q9Y5P4-2)

Also known as: Delta26; GPBPD26;

The sequence of this isoform differs from the canonical sequence as follows:
     371-396: Missing.
Isoform 3 (identifier: Q9Y5P4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQHSCIPTPP...GLLLGCRASM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 624624Collagen type IV alpha-3-binding protein
PRO_0000220665

Regions

Domain23 – 11795PH
Domain389 – 618230START
Coiled coil263 – 30341 Potential
Motif321 – 3277FFAT

Sites

Binding site4721Ceramide
Binding site4931Ceramide
Binding site5301Ceramide
Binding site5791Ceramide

Amino acid modifications

Modified residue1321Phosphoserine; by PKD Ref.11
Modified residue3151Phosphoserine Ref.9
Modified residue3771Phosphoserine Ref.12

Natural variations

Alternative sequence11M → MQHSCIPTPPSPFSAPPAFL PVVTRESRRGLSSGGSAGRN AGVTATAAAADGWKGRLPSP LVLLPRSARCQARRRRGGRT SSLLLLPPTPERALFASPSP DPSPRGLGASSGAAEGAGAG LLLGCRASM in isoform 3.
VSP_041022
Alternative sequence371 – 39626Missing in isoform 2.
VSP_006276
Natural variant1381S → C Found in a patient with mental retardation. Ref.18
VAR_069403
Natural variant5991K → R.
Corresponds to variant rs55882089 [ dbSNP | Ensembl ].
VAR_061815

Experimental info

Mutagenesis1321S → A: Abolishes the phosphorylation. Strongly reduces the interaction with phosphatidylinositol 4-phosphate. Increases the ceramide transfer activity. Ref.11
Mutagenesis3241D → A: Impairs the endoplasmic reticulum-to-Golgi ceramide trafficking and abolishes the interaction with VAPA. Ref.10
Mutagenesis4721E → A: Reduces ceramide transfer. Ref.16
Mutagenesis4931Q → A: No effect on ceramide transfer activity. Ref.16
Mutagenesis4991W → A: Reduces affinity for membranes. Abolishes ceramide transfer; when associated with A-588. Ref.17
Mutagenesis5301N → A: Reduces ceramide transfer. Ref.16
Mutagenesis5881W → A: Abolishes ceramide transfer; when associated with A-499.

Secondary structure

............................................................ 624
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CERTL) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A125162492AC5A0E

FASTA62470,835
        10         20         30         40         50         60 
MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN ALSYYKSEDE 

        70         80         90        100        110        120 
TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ DPDHRQQWID AIEQHKTESG 

       130        140        150        160        170        180 
YGSESSLRRH GSMVSLVSGA SGYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK 

       190        200        210        220        230        240 
YFDACADAVS KDELQRDKVV EDDEDDFPTT RSDGDFLHST NGNKEKLFPH VTPKGINGID 

       250        260        270        280        290        300 
FKGEAITFKA TTAGILATLS HCIELMVKRE DSWQKRLDKE TEKKRRTEEA YKNAMTELKK 

       310        320        330        340        350        360 
KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP TSLPSGDAFS 

       370        380        390        400        410        420 
SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM VQNHMTYSLQ DVGGDANWQL 

       430        440        450        460        470        480 
VVEEGEMKVY RREVEENGIV LDPLKATHAV KGVTGHEVCN YFWNVDVRND WETTIENFHV 

       490        500        510        520        530        540 
VETLADNAII IYQTHKRVWP ASQRDVLYLS VIRKIPALTE NDPETWIVCN FSVDHDSAPL 

       550        560        570        580        590        600 
NNRCVRAKIN VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR 

       610        620 
EYPKFLKRFT SYVQEKTAGK PILF 

« Hide

Isoform 2 (Delta26) (GPBPD26) [UniParc].

Checksum: FC52E241DE7C5D85
Show »

FASTA59868,007
Isoform 3 [UniParc].

Checksum: 277A14A581D94EDF
Show »

FASTA75283,708

References

« Hide 'large scale' references
[1]"Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen."
Raya A., Revert F., Navarro S., Saus J.
J. Biol. Chem. 274:12642-12649(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
[2]"Goodpasture antigen-binding protein, the kinase that phosphorylates the Goodpasture antigen, is an alternatively spliced variant implicated in autoimmune pathogenesis."
Raya A., Revert-Ros F., Martinez-Martinez P., Navarro S., Rosello E., Vieites B., Granero F., Forteza J., Saus J.
J. Biol. Chem. 275:40392-40399(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
[3]"Molecular machinery for non-vesicular trafficking of ceramide."
Hanada K., Kumagai K., Yasuda S., Miura Y., Kawano M., Fukasawa M., Nishijima M.
Nature 426:803-809(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, DOMAIN, SUBCELLULAR LOCATION.
[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 AND 3).
Tissue: Lung and Synovium.
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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: Placenta.
[8]"Homo sapiens genomic sequence, containing DINB1 and GPBP gene."
Ogi T., Yamamoto Y., Ohmori H.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
[9]"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-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT."
Kawano M., Kumagai K., Nishijima M., Hanada K.
J. Biol. Chem. 281:30279-30288(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VAPA AND VAPB, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-324.
[11]"Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein."
Fugmann T., Hausser A., Schoeffler P., Schmid S., Pfizenmaier K., Olayioye M.A.
J. Cell Biol. 178:15-22(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-132, FUNCTION, MUTAGENESIS OF SER-132.
[12]"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 SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelin."
Tomishige N., Kumagai K., Kusuda J., Nishijima M., Hanada K.
Mol. Biol. Cell 20:348-357(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CSNK1G2/CK1.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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].
[16]"Structural basis for specific lipid recognition by CERT responsible for nonvesicular trafficking of ceramide."
Kudo N., Kumagai K., Tomishige N., Yamaji T., Wakatsuki S., Nishijima M., Hanada K., Kato R.
Proc. Natl. Acad. Sci. U.S.A. 105:488-493(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 347-624 IN COMPLEXES WITH CERAMIDES AND DIACYLGLYCEROL, MUTAGENESIS OF GLU-472; GLN-493 AND ASN-530, FUNCTION, SUBCELLULAR LOCATION.
[17]"Crystal structures of the CERT START domain with inhibitors provide insights into the mechanism of ceramide transfer."
Kudo N., Kumagai K., Matsubara R., Kobayashi S., Hanada K., Wakatsuki S., Kato R.
J. Mol. Biol. 396:245-251(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 347-624 IN COMPLEXES WITH CERAMIDE AND INHIBITOR, MUTAGENESIS OF TRP-499, FUNCTION.
[18]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-138.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF136450 mRNA. Translation: AAD30288.1.
AF232930 mRNA. Translation: AAG42046.1.
AF232935 Genomic DNA. Translation: AAG42051.1.
AY453385 mRNA. Translation: AAR26717.1.
AY453386 mRNA. Translation: AAR26718.1.
AK091851 mRNA. Translation: BAC03762.1.
AK096854 mRNA. Translation: BAG53379.1.
AK292087 mRNA. Translation: BAF84776.1.
AC008897 Genomic DNA. No translation available.
AC112183 Genomic DNA. No translation available.
AC116341 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95757.1.
CH471084 Genomic DNA. Translation: EAW95760.1.
BC000102 mRNA. Translation: AAH00102.1.
AB036934 Genomic DNA. Translation: BAB58974.1.
AB036936 Genomic DNA. Translation: BAB58977.1.
RefSeqNP_001123577.1. NM_001130105.1.
NP_005704.1. NM_005713.2.
NP_112729.1. NM_031361.2.
UniGeneHs.270437.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E3MX-ray2.20A347-624[»]
2E3NX-ray1.40A347-624[»]
2E3OX-ray1.55A347-624[»]
2E3PX-ray1.40A/B347-624[»]
2E3QX-ray2.08A347-624[»]
2E3RX-ray1.65A/B347-624[»]
2E3SX-ray1.94A347-624[»]
2RSGNMR-A24-117[»]
2Z9YX-ray1.80A347-624[»]
2Z9ZX-ray1.74A347-624[»]
3H3QX-ray2.00A/B347-624[»]
3H3RX-ray1.85A/B347-624[»]
3H3SX-ray1.66A/B347-624[»]
3H3TX-ray2.40A/B347-624[»]
4HHVX-ray1.75A/B20-121[»]
ProteinModelPortalQ9Y5P4.
SMRQ9Y5P4. Positions 24-117, 391-624.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115396. 15 interactions.
IntActQ9Y5P4. 13 interactions.
MINTMINT-1441568.
STRING9606.ENSP00000369862.

PTM databases

PhosphoSiteQ9Y5P4.

Polymorphism databases

DMDM20978413.

Proteomic databases

PaxDbQ9Y5P4.
PRIDEQ9Y5P4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261415; ENSP00000261415; ENSG00000113163. [Q9Y5P4-2]
ENST00000380494; ENSP00000369862; ENSG00000113163. [Q9Y5P4-3]
ENST00000405807; ENSP00000383996; ENSG00000113163. [Q9Y5P4-1]
GeneID10087.
KEGGhsa:10087.
UCSCuc003kds.3. human. [Q9Y5P4-2]
uc003kdt.3. human. [Q9Y5P4-3]
uc003kdu.2. human. [Q9Y5P4-1]

Organism-specific databases

CTD10087.
GeneCardsGC05M074664.
HGNCHGNC:2205. COL4A3BP.
HPAHPA035645.
MIM604677. gene.
neXtProtNX_Q9Y5P4.
PharmGKBPA26720.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238964.
HOVERGENHBG050753.
InParanoidQ9Y5P4.
KOK08283.
OMAWPTSMPS.
OrthoDBEOG7G7KNJ.
PhylomeDBQ9Y5P4.
TreeFamTF106160.

Enzyme and pathway databases

BRENDA2.7.11.9. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9Y5P4.
BgeeQ9Y5P4.
CleanExHS_COL4A3BP.
GenevestigatorQ9Y5P4.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.530.20. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamPF00169. PH. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50848. START. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y5P4.
GeneWikiCOL4A3BP.
GenomeRNAi10087.
NextBio38145.
PROQ9Y5P4.
SOURCESearch...

Entry information

Entry nameC43BP_HUMAN
AccessionPrimary (citable) accession number: Q9Y5P4
Secondary accession number(s): A8K7S2 expand/collapse secondary AC list , B3KUB7, Q53YV1, Q53YV2, Q96Q85, Q96Q88, Q9H2S7, Q9H2S8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 123 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 5

Human chromosome 5: entries, gene names and cross-references to MIM