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Q9Y5P4

- C43BP_HUMAN

UniProt

Q9Y5P4 - C43BP_HUMAN

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Protein
Collagen type IV alpha-3-binding protein
Gene
COL4A3BP, CERT, STARD11
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei472 – 4721Ceramide
Binding sitei493 – 4931Ceramide
Binding sitei530 – 5301Ceramide
Binding sitei579 – 5791Ceramide

GO - Molecular functioni

  1. ceramide binding Source: UniProtKB
  2. ceramide transporter activity Source: UniProtKB
  3. phosphatidylinositol-4-phosphate binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein kinase activity Source: ProtInc

GO - Biological processi

  1. ER to Golgi ceramide transport Source: UniProtKB
  2. cell morphogenesis Source: Ensembl
  3. cell proliferation Source: Ensembl
  4. ceramide metabolic process Source: Ensembl
  5. endoplasmic reticulum organization Source: Ensembl
  6. heart morphogenesis Source: Ensembl
  7. immune response Source: UniProtKB
  8. in utero embryonic development Source: Ensembl
  9. lipid homeostasis Source: Ensembl
  10. mitochondrion morphogenesis Source: Ensembl
  11. muscle contraction Source: Ensembl
  12. protein phosphorylation Source: ProtInc
  13. response to endoplasmic reticulum stress Source: Ensembl
  14. signal transduction Source: Ensembl
  15. small molecule metabolic process Source: Reactome
  16. sphingolipid biosynthetic process Source: Reactome
  17. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BRENDAi2.7.11.9. 2681.
ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Synonyms:CERT, STARD11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:2205. COL4A3BP.

Subcellular locationi

Cytoplasm. Golgi apparatus. Endoplasmic reticulum
Note: Preferentially localized to the Golgi apparatus.3 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. cytosol Source: Reactome
  3. endoplasmic reticulum membrane Source: Reactome
  4. mitochondrion Source: Ensembl
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321S → A: Abolishes the phosphorylation. Strongly reduces the interaction with phosphatidylinositol 4-phosphate. Increases the ceramide transfer activity. 1 Publication
Mutagenesisi324 – 3241D → A: Impairs the endoplasmic reticulum-to-Golgi ceramide trafficking and abolishes the interaction with VAPA. 1 Publication
Mutagenesisi472 – 4721E → A: Reduces ceramide transfer. 1 Publication
Mutagenesisi493 – 4931Q → A: No effect on ceramide transfer activity. 1 Publication
Mutagenesisi499 – 4991W → A: Reduces affinity for membranes. Abolishes ceramide transfer; when associated with A-588. 1 Publication
Mutagenesisi530 – 5301N → A: Reduces ceramide transfer. 1 Publication
Mutagenesisi588 – 5881W → A: Abolishes ceramide transfer; when associated with A-499.

Organism-specific databases

PharmGKBiPA26720.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 624624Collagen type IV alpha-3-binding protein
PRO_0000220665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei132 – 1321Phosphoserine; by PKD1 Publication
Modified residuei315 – 3151Phosphoserine1 Publication
Modified residuei377 – 3771Phosphoserine1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y5P4.
PaxDbiQ9Y5P4.
PRIDEiQ9Y5P4.

PTM databases

PhosphoSiteiQ9Y5P4.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

ArrayExpressiQ9Y5P4.
BgeeiQ9Y5P4.
CleanExiHS_COL4A3BP.
GenevestigatoriQ9Y5P4.

Organism-specific databases

HPAiHPA035645.

Interactioni

Subunit structurei

Interacts with COL4A3. Interacts with VAPA and VAPB. Interaction with VAPB is less efficient than with VAPA.1 Publication

Protein-protein interaction databases

BioGridi115396. 15 interactions.
IntActiQ9Y5P4. 13 interactions.
MINTiMINT-1441568.
STRINGi9606.ENSP00000369862.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 338
Turni36 – 383
Beta strandi40 – 489
Beta strandi51 – 566
Beta strandi58 – 625
Beta strandi64 – 718
Beta strandi75 – 784
Beta strandi85 – 906
Beta strandi93 – 986
Helixi102 – 11918
Helixi397 – 40711
Beta strandi413 – 4153
Beta strandi418 – 4247
Beta strandi427 – 4326
Beta strandi444 – 4518
Helixi455 – 4639
Helixi465 – 4673
Helixi468 – 4714
Beta strandi474 – 48512
Beta strandi488 – 4958
Beta strandi499 – 5024
Beta strandi504 – 51512
Beta strandi518 – 5225
Beta strandi525 – 5328
Beta strandi542 – 5465
Beta strandi548 – 55912
Beta strandi563 – 5653
Helixi570 – 5723
Beta strandi573 – 58412
Helixi591 – 61727
Beta strandi618 – 6203

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9Y5P4.
SMRiQ9Y5P4. Positions 20-121, 391-624.

Miscellaneous databases

EvolutionaryTraceiQ9Y5P4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 11795PH
Add
BLAST
Domaini389 – 618230START
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili263 – 30341 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi321 – 3277FFAT

Domaini

The START domain recognizes ceramides and diacylglycerol lipids, interacts with membranes, and mediates the intermembrane transfer of ceramides and diacylglycerol lipids.1 Publication
The PH domain targets the Golgi apparatus.1 Publication
The FFAT motif is required for interaction with VAPA and VAPB.1 Publication

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 START domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG238964.
HOVERGENiHBG050753.
InParanoidiQ9Y5P4.
KOiK08283.
OMAiWPTSMPS.
OrthoDBiEOG7G7KNJ.
PhylomeDBiQ9Y5P4.
TreeFamiTF106160.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.530.20. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50848. START. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y5P4-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN    50
ALSYYKSEDE TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ 100
DPDHRQQWID AIEQHKTESG YGSESSLRRH GSMVSLVSGA SGYSATSTSS 150
FKKGHSLREK LAEMETFRDI LCRQVDTLQK YFDACADAVS KDELQRDKVV 200
EDDEDDFPTT RSDGDFLHST NGNKEKLFPH VTPKGINGID FKGEAITFKA 250
TTAGILATLS HCIELMVKRE DSWQKRLDKE TEKKRRTEEA YKNAMTELKK 300
KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP 350
TSLPSGDAFS SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM 400
VQNHMTYSLQ DVGGDANWQL VVEEGEMKVY RREVEENGIV LDPLKATHAV 450
KGVTGHEVCN YFWNVDVRND WETTIENFHV VETLADNAII IYQTHKRVWP 500
ASQRDVLYLS VIRKIPALTE NDPETWIVCN FSVDHDSAPL NNRCVRAKIN 550
VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR 600
EYPKFLKRFT SYVQEKTAGK PILF 624
Length:624
Mass (Da):70,835
Last modified:November 1, 1999 - v1
Checksum:iA125162492AC5A0E
GO
Isoform 2 (identifier: Q9Y5P4-2) [UniParc]FASTAAdd to Basket

Also known as: Delta26, GPBPD26

The sequence of this isoform differs from the canonical sequence as follows:
     371-396: Missing.

Show »
Length:598
Mass (Da):68,007
Checksum:iFC52E241DE7C5D85
GO
Isoform 3 (identifier: Q9Y5P4-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:752
Mass (Da):83,708
Checksum:i277A14A581D94EDF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381S → C Found in a patient with mental retardation. 1 Publication
VAR_069403
Natural varianti599 – 5991K → R.
Corresponds to variant rs55882089 [ dbSNP | Ensembl ].
VAR_061815

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MQHSCIPTPPSPFSAPPAFL PVVTRESRRGLSSGGSAGRN AGVTATAAAADGWKGRLPSP LVLLPRSARCQARRRRGGRT SSLLLLPPTPERALFASPSP DPSPRGLGASSGAAEGAGAG LLLGCRASM in isoform 3.
VSP_041022
Alternative sequencei371 – 39626Missing in isoform 2.
VSP_006276Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4028.1. [Q9Y5P4-1]
CCDS4029.1. [Q9Y5P4-2]
CCDS47235.1. [Q9Y5P4-3]
RefSeqiNP_001123577.1. NM_001130105.1. [Q9Y5P4-3]
NP_005704.1. NM_005713.2. [Q9Y5P4-1]
NP_112729.1. NM_031361.2. [Q9Y5P4-2]
XP_006714576.1. XM_006714513.1. [Q9Y5P4-1]
UniGeneiHs.270437.

Genome annotation databases

EnsembliENST00000261415; ENSP00000261415; ENSG00000113163. [Q9Y5P4-2]
ENST00000380494; ENSP00000369862; ENSG00000113163. [Q9Y5P4-3]
ENST00000405807; ENSP00000383996; ENSG00000113163. [Q9Y5P4-1]
GeneIDi10087.
KEGGihsa:10087.
UCSCiuc003kds.3. human. [Q9Y5P4-2]
uc003kdt.3. human. [Q9Y5P4-3]
uc003kdu.2. human. [Q9Y5P4-1]

Polymorphism databases

DMDMi20978413.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4028.1. [Q9Y5P4-1 ]
CCDS4029.1. [Q9Y5P4-2 ]
CCDS47235.1. [Q9Y5P4-3 ]
RefSeqi NP_001123577.1. NM_001130105.1. [Q9Y5P4-3 ]
NP_005704.1. NM_005713.2. [Q9Y5P4-1 ]
NP_112729.1. NM_031361.2. [Q9Y5P4-2 ]
XP_006714576.1. XM_006714513.1. [Q9Y5P4-1 ]
UniGenei Hs.270437.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E3M X-ray 2.20 A 347-624 [» ]
2E3N X-ray 1.40 A 347-624 [» ]
2E3O X-ray 1.55 A 347-624 [» ]
2E3P X-ray 1.40 A/B 347-624 [» ]
2E3Q X-ray 2.08 A 347-624 [» ]
2E3R X-ray 1.65 A/B 347-624 [» ]
2E3S X-ray 1.94 A 347-624 [» ]
2RSG NMR - A 24-117 [» ]
2Z9Y X-ray 1.80 A 347-624 [» ]
2Z9Z X-ray 1.74 A 347-624 [» ]
3H3Q X-ray 2.00 A/B 347-624 [» ]
3H3R X-ray 1.85 A/B 347-624 [» ]
3H3S X-ray 1.66 A/B 347-624 [» ]
3H3T X-ray 2.40 A/B 347-624 [» ]
4HHV X-ray 1.75 A/B 20-121 [» ]
ProteinModelPortali Q9Y5P4.
SMRi Q9Y5P4. Positions 20-121, 391-624.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115396. 15 interactions.
IntActi Q9Y5P4. 13 interactions.
MINTi MINT-1441568.
STRINGi 9606.ENSP00000369862.

PTM databases

PhosphoSitei Q9Y5P4.

Polymorphism databases

DMDMi 20978413.

Proteomic databases

MaxQBi Q9Y5P4.
PaxDbi Q9Y5P4.
PRIDEi Q9Y5P4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261415 ; ENSP00000261415 ; ENSG00000113163 . [Q9Y5P4-2 ]
ENST00000380494 ; ENSP00000369862 ; ENSG00000113163 . [Q9Y5P4-3 ]
ENST00000405807 ; ENSP00000383996 ; ENSG00000113163 . [Q9Y5P4-1 ]
GeneIDi 10087.
KEGGi hsa:10087.
UCSCi uc003kds.3. human. [Q9Y5P4-2 ]
uc003kdt.3. human. [Q9Y5P4-3 ]
uc003kdu.2. human. [Q9Y5P4-1 ]

Organism-specific databases

CTDi 10087.
GeneCardsi GC05M074664.
HGNCi HGNC:2205. COL4A3BP.
HPAi HPA035645.
MIMi 604677. gene.
neXtProti NX_Q9Y5P4.
PharmGKBi PA26720.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG238964.
HOVERGENi HBG050753.
InParanoidi Q9Y5P4.
KOi K08283.
OMAi WPTSMPS.
OrthoDBi EOG7G7KNJ.
PhylomeDBi Q9Y5P4.
TreeFami TF106160.

Enzyme and pathway databases

BRENDAi 2.7.11.9. 2681.
Reactomei REACT_115810. Sphingolipid de novo biosynthesis.

Miscellaneous databases

EvolutionaryTracei Q9Y5P4.
GeneWikii COL4A3BP.
GenomeRNAii 10087.
NextBioi 38145.
PROi Q9Y5P4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y5P4.
Bgeei Q9Y5P4.
CleanExi HS_COL4A3BP.
Genevestigatori Q9Y5P4.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.530.20. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF01852. START. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00234. START. 1 hit.
[Graphical view ]
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS50848. START. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. Cited for: VARIANT CYS-138.

Entry informationi

Entry nameiC43BP_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5P4
Secondary accession number(s): A8K7S2
, B3KUB7, Q53YV1, Q53YV2, Q96Q85, Q96Q88, Q9H2S7, Q9H2S8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 127 of the entry and version 1 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

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

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