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O14514 (BAI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Brain-specific angiogenesis inhibitor 1
Gene names
Name:BAI1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1584 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Likely to be a potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53 signal in suppression of glioblastoma. May function in cell adhesion and signal transduction in the brain. Ref.6

Subunit structure

Interacts with ELMO1 and DOCK1. When bound to ELMO1 and DOCK1, it may act as a module to promote the engulfment By similarity. Interacts with MAGI1, MAGI3, BAIAP2 and PHYHIP. Ref.3 Ref.4 Ref.5

Subcellular location

Cell membrane; Multi-pass membrane protein. Note: Likely to be concentrated at cell-cell adhesion sites. Ref.7

Tissue specificity

Specifically expressed in brain. Reduced or no expression is observed in some glioblastoma cell lines and cancer tissues. No expression in astrocytes. Ref.6 Ref.7 Ref.8

Induction

By p53/TP53.

Domain

The TSP1 repeats inhibit in vivo angiogenesis in rat cornea induced by BFGF.

Post-translational modification

The endogenous protein is proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. Ref.9

Sequence similarities

Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily.

Contains 1 GPS domain.

Contains 5 TSP type-1 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 15841554Brain-specific angiogenesis inhibitor 1
PRO_0000012863

Regions

Topological domain31 – 948918Extracellular Potential
Transmembrane949 – 96921Helical; Name=1; Potential
Topological domain970 – 98011Cytoplasmic Potential
Transmembrane981 – 100121Helical; Name=2; Potential
Topological domain1002 – 10087Extracellular Potential
Transmembrane1009 – 102921Helical; Name=3; Potential
Topological domain1030 – 105223Cytoplasmic Potential
Transmembrane1053 – 107321Helical; Name=4; Potential
Topological domain1074 – 109320Extracellular Potential
Transmembrane1094 – 111421Helical; Name=5; Potential
Topological domain1115 – 113622Cytoplasmic Potential
Transmembrane1137 – 115721Helical; Name=6; Potential
Topological domain1158 – 11669Extracellular Potential
Transmembrane1167 – 118721Helical; Name=7; Potential
Topological domain1188 – 1584397Cytoplasmic Potential
Domain261 – 31555TSP type-1 1
Domain354 – 40754TSP type-1 2
Domain409 – 46254TSP type-1 3
Domain467 – 52054TSP type-1 4
Domain522 – 57554TSP type-1 5
Domain881 – 93858GPS
Region1365 – 1584220Necessary for interaction with MAGI1
Region1581 – 15844Indispensable for interaction with MAGI1
Motif231 – 2333Cell attachment site Potential
Compositional bias1411 – 142212Poly-Pro
Compositional bias1425 – 14306Poly-Pro

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation6071N-linked (GlcNAc...) Potential
Glycosylation6921N-linked (GlcNAc...) Potential
Glycosylation8441N-linked (GlcNAc...) Potential
Glycosylation8771N-linked (GlcNAc...) Potential
Glycosylation8811N-linked (GlcNAc...) Potential
Disulfide bond273 ↔ 309 By similarity
Disulfide bond277 ↔ 314 By similarity
Disulfide bond288 ↔ 299 By similarity
Disulfide bond366 ↔ 400 By similarity
Disulfide bond370 ↔ 406 By similarity
Disulfide bond381 ↔ 390 By similarity
Disulfide bond421 ↔ 456 By similarity
Disulfide bond425 ↔ 461 By similarity
Disulfide bond436 ↔ 446 By similarity
Disulfide bond479 ↔ 514 By similarity
Disulfide bond483 ↔ 519 By similarity
Disulfide bond494 ↔ 504 By similarity
Disulfide bond534 ↔ 569 By similarity
Disulfide bond538 ↔ 574 By similarity
Disulfide bond549 ↔ 559 By similarity
Disulfide bond581 ↔ 616 By similarity
Disulfide bond604 ↔ 634 By similarity
Disulfide bond884 ↔ 921 By similarity
Disulfide bond909 ↔ 923 By similarity

Experimental info

Sequence conflict10101V → M in BAA23647. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O14514 [UniParc].

Last modified October 31, 2012. Version 2.
Checksum: A604E634DDD741F7

FASTA1,584173,501
        10         20         30         40         50         60 
MRGQAAAPGP VWILAPLLLL LLLLGRRARA AAGADAGPGP EPCATLVQGK FFGYFSAAAV 

        70         80         90        100        110        120 
FPANASRCSW TLRNPDPRRY TLYMKVAKAP VPCSGPGRVR TYQFDSFLES TRTYLGVESF 

       130        140        150        160        170        180 
DEVLRLCDPS APLAFLQASK QFLQMRRQQP PQHDGLRPRA GPPGPTDDFS VEYLVVGNRN 

       190        200        210        220        230        240 
PSRAACQMLC RWLDACLAGS RSSHPCGIMQ TPCACLGGEA GGPAAGPLAP RGDVCLRDAV 

       250        260        270        280        290        300 
AGGPENCLTS LTQDRGGHGA TGGWKLWSLW GECTRDCGGG LQTRTRTCLP APGVEGGGCE 

       310        320        330        340        350        360 
GVLEEGRQCN REACGPAGRT SSRSQSLRST DARRREELGD ELQQFGFPAP QTGDPAAEEW 

       370        380        390        400        410        420 
SPWSVCSSTC GEGWQTRTRF CVSSSYSTQC SGPLREQRLC NNSAVCPVHG AWDEWSPWSL 

       430        440        450        460        470        480 
CSSTCGRGFR DRTRTCRPPQ FGGNPCEGPE KQTKFCNIAL CPGRAVDGNW NEWSSWSACS 

       490        500        510        520        530        540 
ASCSQGRQQR TRECNGPSYG GAECQGHWVE TRDCFLQQCP VDGKWQAWAS WGSCSVTCGA 

       550        560        570        580        590        600 
GSQRRERVCS GPFFGGAACQ GPQDEYRQCG TQRCPEPHEI CDEDNFGAVI WKETPAGEVA 

       610        620        630        640        650        660 
AVRCPRNATG LILRRCELDE EGIAYWEPPT YIRCVSIDYR NIQMMTREHL AKAQRGLPGE 

       670        680        690        700        710        720 
GVSEVIQTLV EISQDGTSYS GDLLSTIDVL RNMTEIFRRA YYSPTPGDVQ NFVQILSNLL 

       730        740        750        760        770        780 
AEENRDKWEE AQLAGPNAKE LFRLVEDFVD VIGFRMKDLR DAYQVTDNLV LSIHKLPASG 

       790        800        810        820        830        840 
ATDISFPMKG WRATGDWAKV PEDRVTVSKS VFSTGLTEAD EASVFVVGTV LYRNLGSFLA 

       850        860        870        880        890        900 
LQRNTTVLNS KVISVTVKPP PRSLRTPLEI EFAHMYNGTT NQTCILWDET DVPSSSAPPQ 

       910        920        930        940        950        960 
LGPWSWRGCR TVPLDALRTR CLCDRLSTFA ILAQLSADAN MEKATLPSVT LIVGCGVSSL 

       970        980        990       1000       1010       1020 
TLLMLVIIYV SVWRYIRSER SVILINFCLS IISSNALILI GQTQTRNKVV CTLVAAFLHF 

      1030       1040       1050       1060       1070       1080 
FFLSSFCWVL TEAWQSYMAV TGHLRNRLIR KRFLCLGWGL PALVVAISVG FTKAKGYSTM 

      1090       1100       1110       1120       1130       1140 
NYCWLSLEGG LLYAFVGPAA AVVLVNMVIG ILVFNKLVSK DGITDKKLKE RAGASLWSSC 

      1150       1160       1170       1180       1190       1200 
VVLPLLALTW MSAVLAVTDR RSALFQILFA VFDSLEGFVI VMVHCILRRE VQDAVKCRVV 

      1210       1220       1230       1240       1250       1260 
DRQEEGNGDS GGSFQNGHAQ LMTDFEKDVD LACRSVLNKD IAACRTATIT GTLKRPSLPE 

      1270       1280       1290       1300       1310       1320 
EEKLKLAHAK GPPTNFNSLP ANVSKLHLHG SPRYPGGPLP DFPNHSLTLK RDKAPKSSFV 

      1330       1340       1350       1360       1370       1380 
GDGDIFKKLD SELSRAQEKA LDTSYVILPT ATATLRPKPK EEPKYSIHID QMPQTRLIHL 

      1390       1400       1410       1420       1430       1440 
STAPEASLPA RSPPSRQPPS GGPPEAPPAQ PPPPPPPPPP PPQQPLPPPP NLEPAPPSLG 

      1450       1460       1470       1480       1490       1500 
DPGEPAAHPG PSTGPSTKNE NVATLSVSSL ERRKSRYAEL DFEKIMHTRK RHQDMFQDLN 

      1510       1520       1530       1540       1550       1560 
RKLQHAAEKD KEVLGPDSKP EKQQTPNKRP WESLRKAHGT PTWVKKELEP LQPSPLELRS 

      1570       1580 
VEWERSGATI PLVGQDIIDL QTEV 

« Hide

References

« Hide 'large scale' references
[1]"A novel brain-specific p53-target gene, BAI1, containing thrombospondin type 1 repeats inhibits experimental angiogenesis."
Nishimori H., Shiratsuchi T., Urano T., Kimura Y., Kiyono K., Tatsumi K., Yoshida S., Ono M., Kuwano M., Nakamura Y., Tokino T.
Oncogene 15:2145-2150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[2]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Cloning and characterization of BAI-associated protein 1: a PDZ domain-containing protein that interacts with BAI1."
Shiratsuchi T., Futamura M., Oda K., Nishimori H., Nakamura Y., Tokino T.
Biochem. Biophys. Res. Commun. 247:597-604(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAGI1.
[4]"Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1."
Oda K., Shiratsuchi T., Nishimori H., Inazawa J., Yoshikawa H., Taketani Y., Nakamura Y., Tokino T.
Cytogenet. Cell Genet. 84:75-82(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAIAP2.
[5]"Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase."
Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A.
J. Biol. Chem. 275:21477-21485(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAGI3.
[6]"Overexpression of the p53-inducible brain-specific angiogenesis inhibitor 1 suppresses efficiently tumour angiogenesis."
Duda D.G., Sunamura M., Lozonschi L., Yokoyama T., Yatsuoka T., Motoi F., Horii A., Tani K., Asano S., Nakamura Y., Matsuno S.
Br. J. Cancer 86:490-496(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[7]"Brain-specific angiogenesis inhibitor 1 (BAI1) is expressed in human cerebral neuronal cells."
Mori K., Kanemura Y., Fujikawa H., Nakano A., Ikemoto H., Ozaki I., Matsumoto T., Tamura K., Yokota M., Arita N.
Neurosci. Res. 43:69-74(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[8]"Brain angiogenesis inhibitor 1 is differentially expressed in normal brain and glioblastoma independently of p53 expression."
Kaur B., Brat D.J., Calkins C.C., Van Meir E.G.
Am. J. Pathol. 162:19-27(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis."
Arac D., Boucard A.A., Bolliger M.F., Nguyen J., Soltis S.M., Sudhof T.C., Brunger A.T.
EMBO J. 31:1364-1378(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB005297 mRNA. Translation: BAA23647.1.
AC139676 Genomic DNA. No translation available.
PIRT00026.
RefSeqNP_001693.2. NM_001702.2.
UniGeneHs.194654.

3D structure databases

ProteinModelPortalO14514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107051. 18 interactions.
DIPDIP-40884N.
IntActO14514. 3 interactions.
MINTMINT-93782.
STRING9606.ENSP00000313046.

Chemistry

GuidetoPHARMACOLOGY174.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteO14514.

Proteomic databases

PaxDbO14514.
PRIDEO14514.

Protocols and materials databases

DNASU575.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323289; ENSP00000313046; ENSG00000181790.
ENST00000517894; ENSP00000430945; ENSG00000181790.
GeneID575.
KEGGhsa:575.
UCSCuc003ywm.3. human.

Organism-specific databases

CTD575.
GeneCardsGC08P143542.
H-InvDBHIX0025534.
HGNCHGNC:943. BAI1.
HPAHPA038785.
MIM602682. gene.
neXtProtNX_O14514.
PharmGKBPA25247.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG285547.
HOGENOMHOG000230916.
HOVERGENHBG004813.
InParanoidO14514.
KOK04596.
OMADSKPEKQ.
OrthoDBEOG7KDF90.
TreeFamTF331634.

Enzyme and pathway databases

SignaLinkO14514.

Gene expression databases

ArrayExpressO14514.
BgeeO14514.
CleanExHS_BAI1.
GenevestigatorO14514.

Family and domain databases

InterProIPR022624. DUF3497.
IPR017981. GPCR_2-like.
IPR008077. GPCR_2_brain-spec_angio_inhib.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR000203. GPS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF00002. 7tm_2. 1 hit.
PF12003. DUF3497. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSPR01694. BAIPRECURSOR.
PR00249. GPCRSECRETIN.
SMARTSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 5 hits.
PROSITEPS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS50092. TSP1. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBrain-specific_angiogenesis_inhibitor_1.
GenomeRNAi575.
NextBio2345.
PROO14514.
SOURCESearch...

Entry information

Entry nameBAI1_HUMAN
AccessionPrimary (citable) accession number: O14514
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 31, 2012
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries