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Protein

Collagen type IV alpha-3-binding protein

Gene

COL4A3BP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • ceramide binding Source: UniProtKB
  • ceramide transporter activity Source: UniProtKB
  • phosphatidylinositol-4-phosphate binding Source: UniProtKB
  • protein kinase activity Source: ProtInc

GO - Biological processi

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
Name:COL4A3BP
Synonyms:CERT, STARD11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:2205. COL4A3BP.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • Golgi apparatus Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleoplasm 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.

Polymorphism and mutation databases

BioMutaiCOL4A3BP.
DMDMi20978413.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 624624Collagen type IV alpha-3-binding proteinPRO_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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y5P4.
PaxDbiQ9Y5P4.
PRIDEiQ9Y5P4.

PTM databases

PhosphoSiteiQ9Y5P4.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiQ9Y5P4.
CleanExiHS_COL4A3BP.
ExpressionAtlasiQ9Y5P4. baseline and differential.
GenevisibleiQ9Y5P4. HS.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTL8Q9H5683EBI-739994,EBI-10306917
ARL6IP1Q150413EBI-739994,EBI-714543
CSNK1G2P783684EBI-739994,EBI-748380
ITGB3BPQ133524EBI-739994,EBI-712105

Protein-protein interaction databases

BioGridi115396. 22 interactions.
IntActiQ9Y5P4. 15 interactions.
MINTiMINT-1441568.
STRINGi9606.ENSP00000369862.

Structurei

Secondary structure

1
624
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 338Combined sources
Turni36 – 383Combined sources
Beta strandi40 – 489Combined sources
Beta strandi51 – 566Combined sources
Beta strandi58 – 625Combined sources
Beta strandi64 – 718Combined sources
Beta strandi75 – 784Combined sources
Beta strandi85 – 906Combined sources
Beta strandi93 – 986Combined sources
Helixi102 – 11918Combined sources
Helixi397 – 40711Combined sources
Beta strandi413 – 4153Combined sources
Beta strandi418 – 4247Combined sources
Beta strandi427 – 4326Combined sources
Beta strandi444 – 4518Combined sources
Helixi455 – 4639Combined sources
Helixi465 – 4673Combined sources
Helixi468 – 4714Combined sources
Beta strandi474 – 48512Combined sources
Beta strandi488 – 4958Combined sources
Beta strandi499 – 5024Combined sources
Beta strandi504 – 51512Combined sources
Beta strandi518 – 5225Combined sources
Beta strandi525 – 5328Combined sources
Beta strandi542 – 5465Combined sources
Beta strandi548 – 55912Combined sources
Beta strandi563 – 5653Combined sources
Helixi570 – 5723Combined sources
Beta strandi573 – 58412Combined sources
Helixi591 – 61727Combined sources
Beta strandi618 – 6203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y5P4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 11795PHPROSITE-ProRule annotationAdd
BLAST
Domaini389 – 618230STARTPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili263 – 30341Sequence AnalysisAdd
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.PROSITE-ProRule annotation
Contains 1 START domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG238964.
GeneTreeiENSGT00650000093230.
HOVERGENiHBG050753.
InParanoidiQ9Y5P4.
KOiK08283.
OMAiWPTSMPS.
OrthoDBiEOG7G7KNJ.
PhylomeDBiQ9Y5P4.
TreeFamiTF106160.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.530.20. 1 hit.
InterProiIPR011993. PH-like_dom.
IPR001849. PH_domain.
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. AlignAdd to basket

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

        10         20         30         40         50
MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN
60 70 80 90 100
ALSYYKSEDE TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ
110 120 130 140 150
DPDHRQQWID AIEQHKTESG YGSESSLRRH GSMVSLVSGA SGYSATSTSS
160 170 180 190 200
FKKGHSLREK LAEMETFRDI LCRQVDTLQK YFDACADAVS KDELQRDKVV
210 220 230 240 250
EDDEDDFPTT RSDGDFLHST NGNKEKLFPH VTPKGINGID FKGEAITFKA
260 270 280 290 300
TTAGILATLS HCIELMVKRE DSWQKRLDKE TEKKRRTEEA YKNAMTELKK
310 320 330 340 350
KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP
360 370 380 390 400
TSLPSGDAFS SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM
410 420 430 440 450
VQNHMTYSLQ DVGGDANWQL VVEEGEMKVY RREVEENGIV LDPLKATHAV
460 470 480 490 500
KGVTGHEVCN YFWNVDVRND WETTIENFHV VETLADNAII IYQTHKRVWP
510 520 530 540 550
ASQRDVLYLS VIRKIPALTE NDPETWIVCN FSVDHDSAPL NNRCVRAKIN
560 570 580 590 600
VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR
610 620
EYPKFLKRFT SYVQEKTAGK PILF
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. 1 PublicationVSP_041022
Alternative sequencei371 – 39626Missing in isoform 2. 4 PublicationsVSP_006276Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000380494; ENSP00000369862; ENSG00000113163. [Q9Y5P4-3]
ENST00000405807; ENSP00000383996; ENSG00000113163.
GeneIDi10087.
KEGGihsa:10087.
UCSCiuc003kds.3. human. [Q9Y5P4-2]
uc003kdt.3. human. [Q9Y5P4-3]
uc003kdu.2. human. [Q9Y5P4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115396. 22 interactions.
IntActiQ9Y5P4. 15 interactions.
MINTiMINT-1441568.
STRINGi9606.ENSP00000369862.

PTM databases

PhosphoSiteiQ9Y5P4.

Polymorphism and mutation databases

BioMutaiCOL4A3BP.
DMDMi20978413.

Proteomic databases

MaxQBiQ9Y5P4.
PaxDbiQ9Y5P4.
PRIDEiQ9Y5P4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380494; ENSP00000369862; ENSG00000113163. [Q9Y5P4-3]
ENST00000405807; ENSP00000383996; ENSG00000113163.
GeneIDi10087.
KEGGihsa:10087.
UCSCiuc003kds.3. human. [Q9Y5P4-2]
uc003kdt.3. human. [Q9Y5P4-3]
uc003kdu.2. human. [Q9Y5P4-1]

Organism-specific databases

CTDi10087.
GeneCardsiGC05M074664.
HGNCiHGNC:2205. COL4A3BP.
HPAiHPA035645.
MIMi604677. gene.
neXtProtiNX_Q9Y5P4.
PharmGKBiPA26720.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG238964.
GeneTreeiENSGT00650000093230.
HOVERGENiHBG050753.
InParanoidiQ9Y5P4.
KOiK08283.
OMAiWPTSMPS.
OrthoDBiEOG7G7KNJ.
PhylomeDBiQ9Y5P4.
TreeFamiTF106160.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9Y5P4.
GeneWikiiCOL4A3BP.
GenomeRNAii10087.
NextBioi38145.
PROiQ9Y5P4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5P4.
CleanExiHS_COL4A3BP.
ExpressionAtlasiQ9Y5P4. baseline and differential.
GenevisibleiQ9Y5P4. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.530.20. 1 hit.
InterProiIPR011993. PH-like_dom.
IPR001849. PH_domain.
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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "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.
  18. "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.
  19. 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: July 22, 2015
This is version 137 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 reported to have a protein kinase activity and to phosphorylate on Ser and Thr residues the Goodpasture autoantigen (in vitro).1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.