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Protein

Brain-specific angiogenesis inhibitor 1

Gene

Bai1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: InterPro

GO - Biological processi

  1. negative regulation of angiogenesis Source: MGI
  2. neuropeptide signaling pathway Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Brain-specific angiogenesis inhibitor 1
Gene namesi
Name:Bai1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1933736. Bai1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 948915ExtracellularSequence 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 – 1582395CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 15821549Brain-specific angiogenesis inhibitor 1PRO_0000245046Add
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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ3UHD1.
PaxDbiQ3UHD1.
PRIDEiQ3UHD1.

PTM databases

PhosphoSiteiQ3UHD1.

Expressioni

Tissue specificityi

Specifically expressed in brain.1 Publication

Developmental stagei

Observed only on embryonic brain not in other tissues.1 Publication

Gene expression databases

BgeeiQ3UHD1.
CleanExiMM_BAI1.
ExpressionAtlasiQ3UHD1. baseline and differential.
GenevestigatoriQ3UHD1.

Interactioni

Subunit structurei

Interacts with MAGI1, MAGI3, BAIAP2 and PHYHIP (By similarity). Interacts with ELMO1 and DOCK1. When bound to ELMO1 and DOCK1, it may act as a module to promote the engulfment.By similarity2 Publications

Protein-protein interaction databases

BioGridi223612. 2 interactions.
DIPiDIP-37711N.
IntActiQ3UHD1. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ3UHD1.
SMRiQ3UHD1. Positions 262-401, 410-934, 946-1187.
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

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1382 – 144968Pro-richAdd
BLAST

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.
InParanoidiQ3UHD1.
KOiK04596.
OMAiSWRGCRT.
OrthoDBiEOG7KDF90.
PhylomeDBiQ3UHD1.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q3UHD1-1) [UniParc]FASTAAdd to Basket

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
MRGQAAAPGP IWILAPLLLL LLLLGRWARA ASGADIGPGT EQCTTLVQGK
60 70 80 90 100
FFGYFSAAAV FPANASRCSW TLRNPDPRRY TLYMKVAKAP APCSGPGRVR
110 120 130 140 150
TYQFDSFLES TRTYLGVESF DEVLRLCDSS APLAFLQASK QFLQMQRQQP
160 170 180 190 200
PQDGDLGPQG EFPSSSDDFS VEYLVVGNRN PSHAACQMLC RWLDACLAGS
210 220 230 240 250
RSSHPCGIMQ TPCACLGGDV GDPASSPLVP RGDVCLRDGV AGGPENCLTS
260 270 280 290 300
LTQDRGGHGS AGGWKLWSLW GECTRDCGGG LQTRTRTCLP TLGVEGGGCE
310 320 330 340 350
GVLEEGRLCN RKACGPTGRS SSRSQSLRST DARRREEFGD ELQQFGFPSP
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 NEWSSWSTCS ASCSQGRQQR TRECNGPSYG
510 520 530 540 550
GAECQGHWVE TRDCFLQQCP VDGKWQAWAS WGSCSVTCGG GSQRRERVCS
560 570 580 590 600
GPFFGGAACQ GPQDEYRQCG AQRCPEPHEI CDEDNFGAVV WKETPAGEVA
610 620 630 640 650
AVRCPRNATG LILRRCELDE EGIAFWEPPT YIRCVSIDYR NIQMMTREHL
660 670 680 690 700
AKAQRGLPGE GVSEVIQTLL EISQDGTSYS GDLLSTIDVL RNMTEIFRRA
710 720 730 740 750
YYSPTPGDVQ NFVQIISNLL AEENRDKWEE AQLMGPNAKE LFRLVEDFVD
760 770 780 790 800
VIGFRMKDLR DAYQVTDNLV LSIHKLPASG ATDISFPMKG WRATGDWAKV
810 820 830 840 850
PEDRVTVSKS VFSTGLAEAD DSSVFVVGTV LYRNLGSFLA LQRNTTVLNS
860 870 880 890 900
KVISVTVKPP PRSLLTPLEI EFAHMYNGTT NQTCILWDET DGPSSSAPPQ
910 920 930 940 950
LGPWSWRGCR TVPLDALRTR CLCDRLSTFA ILAQLSADAT MDKVTVPSVT
960 970 980 990 1000
LIVGCGVSSL TLLMLVIIYV SVWRYIRSER SVILINFCLS IISSNALILI
1010 1020 1030 1040 1050
GQTQTRNKVV CTLVAAFLHF FFLSSFCWVL TEAWQSYMAV TGRLRSRLVR
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
GTFKRPSLPE EEKMKLAKGP PPTFNSLPAN VSKLHLHGSP RYPGGPLPDF
1310 1320 1330 1340 1350
PNHSLTLKKD KAPKSSFIGD GDIFKKLDSE LSRAQEKALD TSYVILPTAT
1360 1370 1380 1390 1400
ATLRPKPKEE PKYSINIDQM PQTRLIHLSM APDASFPTRS PPAREPPGGA
1410 1420 1430 1440 1450
PPEVPPVQPP PPPPPPPPPP QQPIPPPPTL EPAPPSLGDT GEPAAHPGPS
1460 1470 1480 1490 1500
SGAGAKNENV ATLSVSSLER RKSRYAELDF EKIMHTRKRH QDMFQDLNRK
1510 1520 1530 1540 1550
LQHAAEKEKE VPGADSKPEK QQTPNKRAWE SLRKPHGTPA WVKKELEPLP
1560 1570 1580
PSPLELRSVE WEKAGATIPL VGQDIIDLQT EV
Length:1,582
Mass (Da):173,297
Last modified:October 11, 2005 - v1
Checksum:i6D1AA6D46E2E223B
GO
Isoform 2 (identifier: Q3UHD1-2)

Sequence is not available

Note: Observed very weakly in the kidney, skeletal muscle, skin, stomach, thymus and brain from embryonic day 18. By neonatal day 1, the expression is targeted only to the brain.

Length:
Mass (Da):

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti264 – 2641W → L in AAN86966. (PubMed:11245925)Curated
Sequence conflicti275 – 28612RDCGG…QTRTR → AGLRGRPANSNP in AAN86966. (PubMed:11245925)CuratedAdd
BLAST
Sequence conflicti300 – 3001E → K in AAN86966. (PubMed:11245925)Curated
Sequence conflicti821 – 8211D → G in BAE28021. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY168408 mRNA. Translation: AAN86966.1.
AK147494 mRNA. Translation: BAE27949.1.
AK147456 mRNA. Translation: BAE27923.1.
AK147459 mRNA. Translation: BAE27926.1.
AK147607 mRNA. Translation: BAE28021.1.
CCDSiCCDS70635.1. [Q3UHD1-1]
RefSeqiNP_778156.2. NM_174991.3. [Q3UHD1-1]
UniGeneiMm.43133.

Genome annotation databases

EnsembliENSMUST00000042035; ENSMUSP00000046097; ENSMUSG00000034730. [Q3UHD1-1]
GeneIDi107831.
KEGGimmu:107831.
UCSCiuc007wco.1. mouse. [Q3UHD1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY168408 mRNA. Translation: AAN86966.1.
AK147494 mRNA. Translation: BAE27949.1.
AK147456 mRNA. Translation: BAE27923.1.
AK147459 mRNA. Translation: BAE27926.1.
AK147607 mRNA. Translation: BAE28021.1.
CCDSiCCDS70635.1. [Q3UHD1-1]
RefSeqiNP_778156.2. NM_174991.3. [Q3UHD1-1]
UniGeneiMm.43133.

3D structure databases

ProteinModelPortaliQ3UHD1.
SMRiQ3UHD1. Positions 262-401, 410-934, 946-1187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223612. 2 interactions.
DIPiDIP-37711N.
IntActiQ3UHD1. 1 interaction.

Chemistry

GuidetoPHARMACOLOGYi174.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiQ3UHD1.

Proteomic databases

MaxQBiQ3UHD1.
PaxDbiQ3UHD1.
PRIDEiQ3UHD1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042035; ENSMUSP00000046097; ENSMUSG00000034730. [Q3UHD1-1]
GeneIDi107831.
KEGGimmu:107831.
UCSCiuc007wco.1. mouse. [Q3UHD1-1]

Organism-specific databases

CTDi575.
MGIiMGI:1933736. Bai1.

Phylogenomic databases

eggNOGiNOG285547.
GeneTreeiENSGT00780000121867.
HOGENOMiHOG000230916.
HOVERGENiHBG004813.
InParanoidiQ3UHD1.
KOiK04596.
OMAiSWRGCRT.
OrthoDBiEOG7KDF90.
PhylomeDBiQ3UHD1.
TreeFamiTF331634.

Miscellaneous databases

NextBioi359547.
PROiQ3UHD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UHD1.
CleanExiMM_BAI1.
ExpressionAtlasiQ3UHD1. baseline and differential.
GenevestigatoriQ3UHD1.

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. "Characterization of mouse brain-specific angiogenesis inhibitor 1 (BAI1) and phytanoyl-CoA alpha-hydroxylase-associated protein 1, a novel BAI1-binding protein."
    Koh J.T., Lee Z.H., Ahn K.Y., Kim J.-K., Bae C.S., Kim H.-H., Kee H.J., Kim K.K.
    Brain Res. Mol. Brain Res. 87:223-237(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH PHYHIP.
    Strain: ICR.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1255-1268, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. "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.
  5. "BAI1 is an engulfment receptor for apoptotic cells upstream of the ELMO/Dock180/Rac module."
    Park D., Tosello-Trampont A.-C., Elliott M.R., Lu M., Haney L.B., Ma Z., Klibanov A.L., Mandell J.W., Ravichandran K.S.
    Nature 450:430-434(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ELMO1 AND DOCK1.

Entry informationi

Entry nameiBAI1_MOUSE
AccessioniPrimary (citable) accession number: Q3UHD1
Secondary accession number(s): Q3UH36, Q8CGM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 11, 2005
Last modified: February 4, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.