Q9Y5P4 (C43BP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	COL4A3BP
Synonyms:	CERT, STARD11

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	624 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Lipid transport Transport
Cellular component	Cytoplasm Endoplasmic reticulum Golgi apparatus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER to Golgi ceramide transport Inferred from mutant phenotype Ref.16. Source: UniProtKB cell morphogenesis Inferred from electronic annotation. Source: Compara cell proliferation Inferred from electronic annotation. Source: Compara ceramide metabolic process Inferred from electronic annotation. Source: Compara endoplasmic reticulum organization Inferred from electronic annotation. Source: Compara heart morphogenesis Inferred from electronic annotation. Source: Compara immune response Non-traceable author statement Ref.2. Source: UniProtKB in utero embryonic development Inferred from electronic annotation. Source: Compara lipid homeostasis Inferred from electronic annotation. Source: Compara mitochondrion morphogenesis Inferred from electronic annotation. Source: Compara muscle contraction Inferred from electronic annotation. Source: Compara response to endoplasmic reticulum stress Inferred from electronic annotation. Source: Compara signal transduction Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome sphingolipid biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	Golgi 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: Compara nucleus Inferred from direct assay. Source: HPA
Molecular_function	ceramide 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 624

624

Collagen type IV alpha-3-binding protein

PRO_0000220665

Regions

Domain

23 – 117

95

PH

Domain

389 – 618

230

START

Coiled coil

263 – 303

41

Potential

Motif

321 – 327

7

FFAT

Sites

Binding site

472

1

Ceramide

Binding site

493

1

Ceramide

Binding site

530

1

Ceramide

Binding site

579

1

Ceramide

Amino acid modifications

Modified residue

132

1

Phosphoserine; by PKD Ref.11

Modified residue

315

1

Phosphoserine Ref.9

Modified residue

377

1

Phosphoserine Ref.12

Modified residue

380

1

Phosphoserine By similarity

Modified residue

611

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1

1

M → MQHSCIPTPPSPFSAPPAFL PVVTRESRRGLSSGGSAGRN AGVTATAAAADGWKGRLPSP LVLLPRSARCQARRRRGGRT SSLLLLPPTPERALFASPSP DPSPRGLGASSGAAEGAGAG LLLGCRASM in isoform 3.

VSP_041022

Alternative sequence

371 – 396

26

Missing in isoform 2.

VSP_006276

Natural variant

599

1

K → R.
Corresponds to variant rs55882089 [ dbSNP | Ensembl ].

VAR_061815

Experimental info

Mutagenesis

132

1

S → A: Abolishes the phosphorylation. Strongly reduces the interaction with phosphatidylinositol 4-phosphate. Increases the ceramide transfer activity. Ref.11

Mutagenesis

324

1

D → A: Impairs the endoplasmic reticulum-to-Golgi ceramide trafficking and abolishes the interaction with VAPA. Ref.10

Mutagenesis

472

1

E → A: Reduces ceramide transfer. Ref.16

Mutagenesis

493

1

Q → A: No effect on ceramide transfer activity. Ref.16

Mutagenesis

499

1

W → A: Reduces affinity for membranes. Abolishes ceramide transfer; when associated with A-588. Ref.17

Mutagenesis

530

1

N → A: Reduces ceramide transfer. Ref.16

Mutagenesis

588

1

W → A: Abolishes ceramide transfer; when associated with A-499.

Secondary structure

1

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624

Helix Strand Turn

Details...

Beta strand

26 – 36

11

Beta strand

40 – 48

9

Beta strand

51 – 57

7

Helix

60 – 62

3

Beta strand

66 – 70

5

Beta strand

75 – 78

4

Beta strand

83 – 90

8

Beta strand

93 – 98

6

Helix

106 – 115

10

Helix

397 – 407

11

Beta strand

413 – 415

3

Beta strand

418 – 424

7

Beta strand

427 – 432

6

Beta strand

444 – 451

8

Helix

455 – 463

9

Helix

465 – 467

3

Helix

468 – 471

4

Beta strand

474 – 485

12

Beta strand

488 – 495

8

Beta strand

499 – 502

4

Beta strand

504 – 515

12

Beta strand

518 – 522

5

Beta strand

525 – 532

8

Beta strand

542 – 546

5

Beta strand

548 – 559

12

Beta strand

563 – 565

3

Helix

570 – 572

3

Beta strand

573 – 584

12

Helix

591 – 617

27

Beta strand

618 – 620

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CERTL) [UniParc]. Last modified November 1, 1999. Version 1. Checksum: A125162492AC5A0E	FASTA	624	70,835
	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
	Isoform 2 (Delta26) (GPBPD26) [UniParc]. Checksum: FC52E241DE7C5D85	FASTA	598	68,007
	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 VEEMVQNHMT YSLQDVGGDA NWQLVVEEGE MKVYRREVEE NGIVLDPLKA 430 440 450 460 470 480 THAVKGVTGH EVCNYFWNVD VRNDWETTIE NFHVVETLAD NAIIIYQTHK RVWPASQRDV 490 500 510 520 530 540 LYLSVIRKIP ALTENDPETW IVCNFSVDHD SAPLNNRCVR AKINVAMICQ TLVSPPEGNQ 550 560 570 580 590 EISRDNILCK ITYVANVNPG GWAPASVLRA VAKREYPKFL KRFTSYVQEK TAGKPILF
	Isoform 3 [UniParc]. Checksum: 277A14A581D94EDF	FASTA	752	83,708
	10 20 30 40 50 60 MQHSCIPTPP SPFSAPPAFL PVVTRESRRG LSSGGSAGRN AGVTATAAAA DGWKGRLPSP 70 80 90 100 110 120 LVLLPRSARC QARRRRGGRT SSLLLLPPTP ERALFASPSP DPSPRGLGAS SGAAEGAGAG 130 140 150 160 170 180 LLLGCRASMS DNQSWNSSGS EEDPETESGP PVERCGVLSK WTNYIHGWQD RWVVLKNNAL 190 200 210 220 230 240 SYYKSEDETE YGCRGSICLS KAVITPHDFD ECRFDISVND SVWYLRAQDP DHRQQWIDAI 250 260 270 280 290 300 EQHKTESGYG SESSLRRHGS MVSLVSGASG YSATSTSSFK KGHSLREKLA EMETFRDILC 310 320 330 340 350 360 RQVDTLQKYF DACADAVSKD ELQRDKVVED DEDDFPTTRS DGDFLHSTNG NKEKLFPHVT 370 380 390 400 410 420 PKGINGIDFK GEAITFKATT AGILATLSHC IELMVKREDS WQKRLDKETE KKRRTEEAYK 430 440 450 460 470 480 NAMTELKKKS HFGGPDYEEG PNSLINEEEF FDAVEAALDR QDKIEEQSQS EKVRLHWPTS 490 500 510 520 530 540 LPSGDAFSSV GTHRFVQKPY SRSSSMSSID LVSASDDVHR FSSQVEEMVQ NHMTYSLQDV 550 560 570 580 590 600 GGDANWQLVV EEGEMKVYRR EVEENGIVLD PLKATHAVKG VTGHEVCNYF WNVDVRNDWE 610 620 630 640 650 660 TTIENFHVVE TLADNAIIIY QTHKRVWPAS QRDVLYLSVI RKIPALTEND PETWIVCNFS 670 680 690 700 710 720 VDHDSAPLNN RCVRAKINVA MICQTLVSPP EGNQEISRDN ILCKITYVAN VNPGGWAPAS 730 740 750 VLRAVAKREY PKFLKRFTSY VQEKTAGKPI LF

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
+	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.

IPI

IPI00024701.
IPI00182914.
IPI00657692.

RefSeq

NP_001123577.1. NM_001130105.1.
NP_005704.1. NM_005713.2.
NP_112729.1. NM_031361.2.

UniGene

Hs.270437.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9Y5P4.

ModBase

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Protein-protein interaction databases

IntAct

Q9Y5P4. 12 interactions.

MINT

MINT-1441568.

STRING

9606.ENSP00000369862.

PTM databases

PhosphoSite

Q9Y5P4.

Polymorphism databases

DMDM

20978413.

Proteomic databases

PaxDb

Q9Y5P4.

PRIDE

Q9Y5P4.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000261415; ENSP00000261415; ENSG00000113163.
ENST00000380494; ENSP00000369862; ENSG00000113163.
ENST00000405807; ENSP00000383996; ENSG00000113163.

GeneID

10087.

KEGG

hsa:10087.

UCSC

uc003kds.3. human.
uc003kdt.3. human.
uc003kdu.2. human.

Organism-specific databases

CTD

10087.

GeneCards

GC05M074664.

HGNC

HGNC:2205. COL4A3BP.

HPA

HPA035645.

MIM

604677. gene.

neXtProt

NX_Q9Y5P4.

PharmGKB

PA26720.

GenAtlas

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Phylogenomic databases

eggNOG

NOG238964.

HOVERGEN

HBG050753.

InParanoid

Q9Y5P4.

KO

K08283.

OMA

FFDACAD.

OrthoDB

EOG46Q6S7.

PhylomeDB

Q9Y5P4.

Enzyme and pathway databases

BRENDA

2.7.11.9. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

Q9Y5P4.

CleanEx

HS_COL4A3BP.

Genevestigator

Q9Y5P4.

GermOnline

ENSG00000113163. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.
3.30.530.20. 1 hit.

InterPro

IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]

Pfam

PF00169. PH. 1 hit.
PF01852. START. 1 hit.
[Graphical view]

SMART

SM00233. PH. 1 hit.
SM00234. START. 1 hit.
[Graphical view]

PROSITE

PS50003. PH_DOMAIN. 1 hit.
PS50848. START. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q9Y5P4.

GenomeRNAi

10087.

NextBio

38145.

SOURCE

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Entry information

Entry name

C43BP_HUMAN

Accession

Primary (citable) accession number: Q9Y5P4
Secondary accession number(s): A8K7S2 , 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:	May 29, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.