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Protein

Brain-specific angiogenesis inhibitor 1

Gene

BAI1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: GDB

GO - Biological processi

  1. axonogenesis Source: ProtInc
  2. cell adhesion Source: ProtInc
  3. G-protein coupled receptor signaling pathway Source: GDB
  4. negative regulation of angiogenesis Source: InterPro
  5. negative regulation of cell proliferation Source: ProtInc
  6. peripheral nervous system development Source: ProtInc
  7. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

SignaLinkiO14514.

Names & Taxonomyi

Protein namesi
Recommended name:
Brain-specific angiogenesis inhibitor 1
Gene namesi
Name:BAI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:943. BAI1.

Subcellular locationi

  1. Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

  2. Note: Likely to be concentrated at cell-cell adhesion sites.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 948918ExtracellularSequence AnalysisAdd
BLAST
Transmembranei949 – 96921Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini970 – 98011CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei981 – 100121Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini1002 – 10087ExtracellularSequence Analysis
Transmembranei1009 – 102921Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini1030 – 105223CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1053 – 107321Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini1074 – 109320ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1094 – 111421Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini1115 – 113622CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1137 – 115721Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini1158 – 11669ExtracellularSequence Analysis
Transmembranei1167 – 118721Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini1188 – 1584397CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell-cell junction Source: ProtInc
  2. integral component of membrane Source: GDB
  3. integral component of plasma membrane Source: ProtInc
  4. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25247.

Polymorphism and mutation databases

BioMutaiBAI1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 15841554Brain-specific angiogenesis inhibitor 1PRO_0000012863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi273 ↔ 309PROSITE-ProRule annotation
Disulfide bondi277 ↔ 314PROSITE-ProRule annotation
Disulfide bondi288 ↔ 299PROSITE-ProRule annotation
Disulfide bondi366 ↔ 400PROSITE-ProRule annotation
Disulfide bondi370 ↔ 406PROSITE-ProRule annotation
Disulfide bondi381 ↔ 390PROSITE-ProRule annotation
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi421 ↔ 456PROSITE-ProRule annotation
Disulfide bondi425 ↔ 461PROSITE-ProRule annotation
Disulfide bondi436 ↔ 446PROSITE-ProRule annotation
Disulfide bondi479 ↔ 514PROSITE-ProRule annotation
Disulfide bondi483 ↔ 519PROSITE-ProRule annotation
Disulfide bondi494 ↔ 504PROSITE-ProRule annotation
Disulfide bondi534 ↔ 569PROSITE-ProRule annotation
Disulfide bondi538 ↔ 574PROSITE-ProRule annotation
Disulfide bondi549 ↔ 559PROSITE-ProRule annotation
Disulfide bondi581 ↔ 616PROSITE-ProRule annotation
Disulfide bondi604 ↔ 634PROSITE-ProRule annotation
Glycosylationi607 – 6071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi692 – 6921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi844 – 8441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi877 – 8771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi881 – 8811N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi884 ↔ 921PROSITE-ProRule annotation
Disulfide bondi909 ↔ 923PROSITE-ProRule annotation

Post-translational modificationi

The endogenous protein is proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit.1 Publication

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO14514.
PRIDEiO14514.

PTM databases

PhosphoSiteiO14514.

Expressioni

Tissue specificityi

Specifically expressed in brain. Reduced or no expression is observed in some glioblastoma cell lines and cancer tissues. No expression in astrocytes.3 Publications

Inductioni

By p53/TP53.

Gene expression databases

BgeeiO14514.
CleanExiHS_BAI1.
ExpressionAtlasiO14514. baseline.
GenevestigatoriO14514.

Organism-specific databases

HPAiHPA038785.

Interactioni

Subunit structurei

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.By similarity3 Publications

Protein-protein interaction databases

BioGridi107051. 18 interactions.
DIPiDIP-40884N.
IntActiO14514. 3 interactions.
MINTiMINT-93782.
STRINGi9606.ENSP00000313046.

Structurei

3D structure databases

ProteinModelPortaliO14514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini261 – 31555TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini354 – 40754TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini409 – 46254TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini467 – 52054TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini522 – 57554TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini881 – 93858GPSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1365 – 1584220Necessary for interaction with MAGI1Add
BLAST
Regioni1581 – 15844Indispensable for interaction with MAGI1

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi231 – 2333Cell attachment siteSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1411 – 142212Poly-ProAdd
BLAST
Compositional biasi1425 – 14306Poly-Pro

Domaini

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

Sequence similaritiesi

Contains 1 GPS domain.PROSITE-ProRule annotation
Contains 5 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG285547.
GeneTreeiENSGT00780000121867.
HOGENOMiHOG000230916.
HOVERGENiHBG004813.
InParanoidiO14514.
KOiK04596.
OMAiSWRGCRT.
OrthoDBiEOG7KDF90.
PhylomeDBiO14514.
TreeFamiTF331634.

Family and domain databases

InterProiIPR022624. 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]
PfamiPF00002. 7tm_2. 1 hit.
PF12003. DUF3497. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01694. BAIPRECURSOR.
PR00249. GPCRSECRETIN.
SMARTiSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50227. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O14514-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGQAAAPGP VWILAPLLLL LLLLGRRARA AAGADAGPGP EPCATLVQGK
60 70 80 90 100
FFGYFSAAAV FPANASRCSW TLRNPDPRRY TLYMKVAKAP VPCSGPGRVR
110 120 130 140 150
TYQFDSFLES TRTYLGVESF DEVLRLCDPS APLAFLQASK QFLQMRRQQP
160 170 180 190 200
PQHDGLRPRA GPPGPTDDFS VEYLVVGNRN PSRAACQMLC RWLDACLAGS
210 220 230 240 250
RSSHPCGIMQ TPCACLGGEA GGPAAGPLAP RGDVCLRDAV AGGPENCLTS
260 270 280 290 300
LTQDRGGHGA TGGWKLWSLW GECTRDCGGG LQTRTRTCLP APGVEGGGCE
310 320 330 340 350
GVLEEGRQCN REACGPAGRT SSRSQSLRST DARRREELGD ELQQFGFPAP
360 370 380 390 400
QTGDPAAEEW SPWSVCSSTC GEGWQTRTRF CVSSSYSTQC SGPLREQRLC
410 420 430 440 450
NNSAVCPVHG AWDEWSPWSL CSSTCGRGFR DRTRTCRPPQ FGGNPCEGPE
460 470 480 490 500
KQTKFCNIAL CPGRAVDGNW NEWSSWSACS ASCSQGRQQR TRECNGPSYG
510 520 530 540 550
GAECQGHWVE TRDCFLQQCP VDGKWQAWAS WGSCSVTCGA GSQRRERVCS
560 570 580 590 600
GPFFGGAACQ GPQDEYRQCG TQRCPEPHEI CDEDNFGAVI WKETPAGEVA
610 620 630 640 650
AVRCPRNATG LILRRCELDE EGIAYWEPPT YIRCVSIDYR NIQMMTREHL
660 670 680 690 700
AKAQRGLPGE GVSEVIQTLV EISQDGTSYS GDLLSTIDVL RNMTEIFRRA
710 720 730 740 750
YYSPTPGDVQ NFVQILSNLL AEENRDKWEE AQLAGPNAKE LFRLVEDFVD
760 770 780 790 800
VIGFRMKDLR DAYQVTDNLV LSIHKLPASG ATDISFPMKG WRATGDWAKV
810 820 830 840 850
PEDRVTVSKS VFSTGLTEAD EASVFVVGTV LYRNLGSFLA LQRNTTVLNS
860 870 880 890 900
KVISVTVKPP PRSLRTPLEI EFAHMYNGTT NQTCILWDET DVPSSSAPPQ
910 920 930 940 950
LGPWSWRGCR TVPLDALRTR CLCDRLSTFA ILAQLSADAN MEKATLPSVT
960 970 980 990 1000
LIVGCGVSSL TLLMLVIIYV SVWRYIRSER SVILINFCLS IISSNALILI
1010 1020 1030 1040 1050
GQTQTRNKVV CTLVAAFLHF FFLSSFCWVL TEAWQSYMAV TGHLRNRLIR
1060 1070 1080 1090 1100
KRFLCLGWGL PALVVAISVG FTKAKGYSTM NYCWLSLEGG LLYAFVGPAA
1110 1120 1130 1140 1150
AVVLVNMVIG ILVFNKLVSK DGITDKKLKE RAGASLWSSC VVLPLLALTW
1160 1170 1180 1190 1200
MSAVLAVTDR RSALFQILFA VFDSLEGFVI VMVHCILRRE VQDAVKCRVV
1210 1220 1230 1240 1250
DRQEEGNGDS GGSFQNGHAQ LMTDFEKDVD LACRSVLNKD IAACRTATIT
1260 1270 1280 1290 1300
GTLKRPSLPE EEKLKLAHAK GPPTNFNSLP ANVSKLHLHG SPRYPGGPLP
1310 1320 1330 1340 1350
DFPNHSLTLK RDKAPKSSFV GDGDIFKKLD SELSRAQEKA LDTSYVILPT
1360 1370 1380 1390 1400
ATATLRPKPK EEPKYSIHID QMPQTRLIHL STAPEASLPA RSPPSRQPPS
1410 1420 1430 1440 1450
GGPPEAPPAQ PPPPPPPPPP PPQQPLPPPP NLEPAPPSLG DPGEPAAHPG
1460 1470 1480 1490 1500
PSTGPSTKNE NVATLSVSSL ERRKSRYAEL DFEKIMHTRK RHQDMFQDLN
1510 1520 1530 1540 1550
RKLQHAAEKD KEVLGPDSKP EKQQTPNKRP WESLRKAHGT PTWVKKELEP
1560 1570 1580
LQPSPLELRS VEWERSGATI PLVGQDIIDL QTEV
Length:1,584
Mass (Da):173,501
Last modified:October 31, 2012 - v2
Checksum:iA604E634DDD741F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1010 – 10101V → M in BAA23647 (PubMed:9393972).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005297 mRNA. Translation: BAA23647.1.
AC139676 Genomic DNA. No translation available.
CCDSiCCDS64985.1.
PIRiT00026.
RefSeqiNP_001693.2. NM_001702.2.
UniGeneiHs.194654.

Genome annotation databases

EnsembliENST00000323289; ENSP00000313046; ENSG00000181790.
ENST00000517894; ENSP00000430945; ENSG00000181790.
GeneIDi575.
KEGGihsa:575.
UCSCiuc003ywm.3. human.

Polymorphism and mutation databases

BioMutaiBAI1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005297 mRNA. Translation: BAA23647.1.
AC139676 Genomic DNA. No translation available.
CCDSiCCDS64985.1.
PIRiT00026.
RefSeqiNP_001693.2. NM_001702.2.
UniGeneiHs.194654.

3D structure databases

ProteinModelPortaliO14514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107051. 18 interactions.
DIPiDIP-40884N.
IntActiO14514. 3 interactions.
MINTiMINT-93782.
STRINGi9606.ENSP00000313046.

Chemistry

GuidetoPHARMACOLOGYi174.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiO14514.

Polymorphism and mutation databases

BioMutaiBAI1.

Proteomic databases

PaxDbiO14514.
PRIDEiO14514.

Protocols and materials databases

DNASUi575.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323289; ENSP00000313046; ENSG00000181790.
ENST00000517894; ENSP00000430945; ENSG00000181790.
GeneIDi575.
KEGGihsa:575.
UCSCiuc003ywm.3. human.

Organism-specific databases

CTDi575.
GeneCardsiGC08P143542.
H-InvDBHIX0025534.
HGNCiHGNC:943. BAI1.
HPAiHPA038785.
MIMi602682. gene.
neXtProtiNX_O14514.
PharmGKBiPA25247.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG285547.
GeneTreeiENSGT00780000121867.
HOGENOMiHOG000230916.
HOVERGENiHBG004813.
InParanoidiO14514.
KOiK04596.
OMAiSWRGCRT.
OrthoDBiEOG7KDF90.
PhylomeDBiO14514.
TreeFamiTF331634.

Enzyme and pathway databases

SignaLinkiO14514.

Miscellaneous databases

GeneWikiiBrain-specific_angiogenesis_inhibitor_1.
GenomeRNAii575.
NextBioi2345.
PROiO14514.
SOURCEiSearch...

Gene expression databases

BgeeiO14514.
CleanExiHS_BAI1.
ExpressionAtlasiO14514. baseline.
GenevestigatoriO14514.

Family and domain databases

InterProiIPR022624. 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]
PfamiPF00002. 7tm_2. 1 hit.
PF12003. DUF3497. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01694. BAIPRECURSOR.
PR00249. GPCRSECRETIN.
SMARTiSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50227. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiBAI1_HUMAN
AccessioniPrimary (citable) accession number: O14514
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 31, 2012
Last modified: April 29, 2015
This is version 136 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. 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.