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Protein

Lipopolysaccharide-responsive and beige-like anchor protein

Gene

LRBA

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

Functioni

May be involved in coupling signal transduction and vesicle trafficking to enable polarized secretion and/or membrane deposition of immune effector molecules.By similarity

Enzyme and pathway databases

SignaLinkiP50851.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipopolysaccharide-responsive and beige-like anchor protein
Alternative name(s):
Beige-like protein
CDC4-like protein
Gene namesi
Name:LRBA
Synonyms:BGL, CDC4L, LBA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:1742. LRBA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1531 – 154818HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB-SubCell
  • Golgi apparatus Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • lysosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Golgi apparatus, Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency, common variable, 8, with autoimmunity (CVID8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive immunologic disorder associated with defective B-cell differentiation and decreased or absent antibody production. Affected individuals have early-childhood onset of recurrent infections, particularly respiratory infections, and also develop variable autoimmune disorders, including idiopathic thrombocytopenic purpura, autoimmune hemolytic anemia, and inflammatory bowel disease.
See also OMIM:614700
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2657 – 26571I → S in CVID8. 1 Publication
Corresponds to variant rs199469663 [ dbSNP | Ensembl ].
VAR_068690

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiLRBA.
MIMi614700. phenotype.
Orphaneti1572. Common variable immunodeficiency.
PharmGKBiPA30444.

Polymorphism and mutation databases

BioMutaiLRBA.
DMDMi259016388.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 28632862Lipopolysaccharide-responsive and beige-like anchor proteinPRO_0000051068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei10 – 101PhosphoserineCombined sources
Modified residuei979 – 9791PhosphoserineCombined sources
Modified residuei1003 – 10031PhosphoserineBy similarity
Modified residuei1100 – 11001PhosphoserineCombined sources
Modified residuei1135 – 11351PhosphoserineCombined sources
Modified residuei1139 – 11391PhosphoserineCombined sources
Modified residuei1233 – 12331PhosphoserineBy similarity
Modified residuei1247 – 12471PhosphoserineCombined sources
Modified residuei1261 – 12611PhosphoserineCombined sources
Modified residuei1488 – 14881PhosphoserineCombined sources
Modified residuei1498 – 14981PhosphoserineCombined sources
Modified residuei1605 – 16051PhosphoserineCombined sources
Modified residuei1767 – 17671PhosphoserineBy similarity
Modified residuei1770 – 17701PhosphoserineBy similarity
Modified residuei2064 – 20641PhosphoserineCombined sources
Modified residuei2496 – 24961PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP50851.
MaxQBiP50851.
PaxDbiP50851.
PeptideAtlasiP50851.
PRIDEiP50851.

PTM databases

iPTMnetiP50851.
PhosphoSiteiP50851.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

By bacterial lipopolysaccharides (LPS).

Gene expression databases

BgeeiP50851.
CleanExiHS_LRBA.
ExpressionAtlasiP50851. baseline and differential.
GenevisibleiP50851. HS.

Organism-specific databases

HPAiHPA019366.
HPA023597.

Interactioni

Protein-protein interaction databases

BioGridi107423. 25 interactions.
DIPiDIP-50531N.
IntActiP50851. 6 interactions.
STRINGi9606.ENSP00000349629.

Structurei

Secondary structure

1
2863
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2079 – 20879Combined sources
Beta strandi2092 – 20998Combined sources
Beta strandi2101 – 21088Combined sources
Helixi2113 – 21175Combined sources
Helixi2120 – 21256Combined sources
Beta strandi2132 – 21343Combined sources
Helixi2135 – 21373Combined sources
Beta strandi2138 – 21469Combined sources
Beta strandi2149 – 21579Combined sources
Beta strandi2162 – 21665Combined sources
Helixi2170 – 217910Combined sources
Turni2195 – 21995Combined sources
Helixi2202 – 22087Combined sources
Helixi2211 – 22166Combined sources
Helixi2222 – 223312Combined sources
Helixi2240 – 22423Combined sources
Beta strandi2254 – 22574Combined sources
Helixi2263 – 22653Combined sources
Helixi2273 – 22764Combined sources
Helixi2278 – 229013Combined sources
Beta strandi2294 – 22963Combined sources
Beta strandi2300 – 23034Combined sources
Helixi2308 – 23158Combined sources
Helixi2321 – 23299Combined sources
Turni2336 – 23383Combined sources
Helixi2343 – 235210Combined sources
Helixi2362 – 23654Combined sources
Helixi2368 – 23714Combined sources
Helixi2400 – 241213Combined sources
Helixi2414 – 24174Combined sources
Helixi2420 – 24278Combined sources
Helixi2434 – 24407Combined sources
Helixi2446 – 24483Combined sources
Helixi2455 – 24573Combined sources
Helixi2461 – 247414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T77X-ray2.40A/B/C/D2076-2489[»]
ProteinModelPortaliP50851.
SMRiP50851. Positions 2076-2489, 2600-2812.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50851.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1301 – 134343WD 1Add
BLAST
Domaini2073 – 2181109BEACH-type PHPROSITE-ProRule annotationAdd
BLAST
Domaini2200 – 2489290BEACHPROSITE-ProRule annotationAdd
BLAST
Repeati2591 – 263343WD 2Add
BLAST
Repeati2636 – 267944WD 3Add
BLAST
Repeati2695 – 273541WD 4Add
BLAST
Repeati2777 – 281640WD 5Add
BLAST
Repeati2819 – 285840WD 6Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1006 – 105348Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1990 – 19945Poly-Arg

Sequence similaritiesi

Contains 1 BEACH domain.PROSITE-ProRule annotation
Contains 1 BEACH-type PH domain.PROSITE-ProRule annotation
Contains 6 WD repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, Transmembrane, Transmembrane helix, WD repeat

Phylogenomic databases

eggNOGiKOG1786. Eukaryota.
ENOG410XNQC. LUCA.
GeneTreeiENSGT00760000119083.
HOGENOMiHOG000082375.
HOVERGENiHBG012582.
InParanoidiP50851.
OMAiEEIGPCS.
OrthoDBiEOG7HTHG2.
PhylomeDBiP50851.
TreeFamiTF313490.

Family and domain databases

Gene3Di1.10.1540.10. 1 hit.
2.130.10.10. 1 hit.
2.30.29.40. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000409. BEACH_dom.
IPR013320. ConA-like_dom.
IPR010508. DUF1088.
IPR031570. DUF4704.
IPR023362. PH-BEACH_dom.
IPR011993. PH_dom-like.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF02138. Beach. 1 hit.
PF06469. DUF1088. 1 hit.
PF15787. DUF4704. 1 hit.
PF14844. PH_BEACH. 1 hit.
[Graphical view]
SMARTiSM01026. Beach. 1 hit.
SM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF50978. SSF50978. 1 hit.
SSF81837. SSF81837. 1 hit.
PROSITEiPS50197. BEACH. 1 hit.
PS51783. PH_BEACH. 1 hit.
[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. AlignAdd to basket

Isoform 1 (identifier: P50851-1) [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
MASEDNRVPS PPPTGDDGGG GGREETPTEG GALSLKPGLP IRGIRMKFAV
60 70 80 90 100
LTGLVEVGEV SNRDIVETVF NLLVGGQFDL EMNFIIQEGE SINCMVDLLE
110 120 130 140 150
KCDITCQAEV WSMFTAILKK SIRNLQVCTE VGLVEKVLGK IEKVDNMIAD
160 170 180 190 200
LLVDMLGVLA SYNLTVRELK LFFSKLQGDK GRWPPHAGKL LSVLKHMPQK
210 220 230 240 250
YGPDAFFNFP GKSAAAIALP PIAKWPYQNG FTFHTWLRMD PVNNINVDKD
260 270 280 290 300
KPYLYCFRTS KGLGYSAHFV GGCLIVTSIK SKGKGFQHCV KFDFKPQKWY
310 320 330 340 350
MVTIVHIYNR WKNSELRCYV NGELASYGEI TWFVNTSDTF DKCFLGSSET
360 370 380 390 400
ADANRVFCGQ MTAVYLFSEA LNAAQIFAIY QLGLGYKGTF KFKAESDLFL
410 420 430 440 450
AEHHKLLLYD GKLSSAIAFT YNPRATDAQL CLESSPKDNP SIFVHSPHAL
460 470 480 490 500
MLQDVKAVLT HSIQSAMHSI GGVQVLFPLF AQLDYRQYLS DEIDLTICST
510 520 530 540 550
LLAFIMELLK NSIAMQEQML ACKGFLVIGY SLEKSSKSHV SRAVLELCLA
560 570 580 590 600
FSKYLSNLQN GMPLLKQLCD HVLLNPAIWI HTPAKVQLML YTYLSTEFIG
610 620 630 640 650
TVNIYNTIRR VGTVLLIMHT LKYYYWAVNP QDRSGITPKG LDGPRPNQKE
660 670 680 690 700
MLSLRAFLLM FIKQLVMKDS GVKEDELQAI LNYLLTMHED DNLMDVLQLL
710 720 730 740 750
VALMSEHPNS MIPAFDQRNG LRVIYKLLAS KSEGIRVQAL KAMGYFLKHL
760 770 780 790 800
APKRKAEVML GHGLFSLLAE RLMLQTNLIT MTTYNVLFEI LIEQIGTQVI
810 820 830 840 850
HKQHPDPDSS VKIQNPQILK VIATLLRNSP QCPESMEVRR AFLSDMIKLF
860 870 880 890 900
NNSRENRRSL LQCSVWQEWM LSLCYFNPKN SDEQKITEMV YAIFRILLYH
910 920 930 940 950
AVKYEWGGWR VWVDTLSITH SKVTFEIHKE NLANIFREQQ GKVDEEIGLC
960 970 980 990 1000
SSTSVQAASG IRRDINVSVG SQQPDTKDSP VCPHFTTNGN ENSSIEKTSS
1010 1020 1030 1040 1050
LESASNIELQ TTNTSYEEMK AEQENQELPD EGTLEETLTN ETRNADDLEV
1060 1070 1080 1090 1100
SSDIIEAVAI SSNSFITTGK DSMTVSEVTA SISSPSEEDA SEMPEFLDKS
1110 1120 1130 1140 1150
IVEEEEDDDY VELKVEGSPT EEANLPTELQ DNSLSPAASE AGEKLDMFGN
1160 1170 1180 1190 1200
DDKLIFQEGK PVTEKQTDTE TQDSKDSGIQ TMTASGSSAM SPETTVSQIA
1210 1220 1230 1240 1250
VESDLGQMLE EGKKATNLTR ETKLINDCHG SVSEASSEQK IAKLDVSNVA
1260 1270 1280 1290 1300
TDTERLELKA SPNVEAPQPH RHVLEISRQH EQPGQGIAPD AVNGQRRDSR
1310 1320 1330 1340 1350
STVFRIPEFN WSQMHQRLLT DLLFSIETDI QMWRSHSTKT VMDFVNSSDN
1360 1370 1380 1390 1400
VIFVHNTIHL ISQVMDNMVM ACGGILPLLS AATSATHELE NIEPTQGLSI
1410 1420 1430 1440 1450
EASVTFLQRL ISLVDVLIFA SSLGFTEIEA EKSMSSGGIL RQCLRLVCAV
1460 1470 1480 1490 1500
AVRNCLECQQ HSQLKTRGDK ALKPMHSLIP LGKSAAKSPV DIVTGGISPV
1510 1520 1530 1540 1550
RDLDRLLQDM DINRLRAVVF RDIEDSKQAQ FLALAVVYFI SVLMVSKYRD
1560 1570 1580 1590 1600
ILEPQNERHS QSCTETGSEN ENVSLSEITP AAFSTLTTAS VEESESTSSA
1610 1620 1630 1640 1650
RRRDSGIGEE TATGLGSHVE VTPHTAPPGV SAGPDAISEV LSTLSLEVNK
1660 1670 1680 1690 1700
SPETKNDRGN DLDTKATPSV SVSKNVNVKD ILRSLVNIPA DGVTVDPALL
1710 1720 1730 1740 1750
PPACLGALGD LSVEQPVQFR SFDRSVIVAA KKSAVSPSTF NTSIPTNAVS
1760 1770 1780 1790 1800
VVSSVDSAQA SDMGGESPGS RSSNAKLPSV PTVDSVSQDP VSNMSITERL
1810 1820 1830 1840 1850
EHALEKAAPL LREIFVDFAP FLSRTLLGSH GQELLIEGTS LVCMKSSSSV
1860 1870 1880 1890 1900
VELVMLLCSQ EWQNSIQKNA GLAFIELVNE GRLLSQTMKD HLVRVANEAE
1910 1920 1930 1940 1950
FILSRQRAED IHRHAEFESL CAQYSADKRE DEKMCDHLIR AAKYRDHVTA
1960 1970 1980 1990 2000
TQLIQKIINI LTDKHGAWGN SAVSRPLEFW RLDYWEDDLR RRRRFVRNPL
2010 2020 2030 2040 2050
GSTHPEATLK TAVEHVCIFK LRENSKATDE DILAKGKQSI RSQALGNQNS
2060 2070 2080 2090 2100
ENEILLEGDD DTLSSVDEKD LENLAGPVSL STPAQLVAPS VVVKGTLSVT
2110 2120 2130 2140 2150
SSELYFEVDE EDPNFKKIDP KILAYTEGLH GKWLFTEIRS IFSRRYLLQN
2160 2170 2180 2190 2200
TALEIFMANR VAVMFNFPDP ATVKKVVNYL PRVGVGTSFG LPQTRRISLA
2210 2220 2230 2240 2250
SPRQLFKASN MTQRWQHREI SNFEYLMFLN TIAGRSYNDL NQYPVFPWVI
2260 2270 2280 2290 2300
TNYESEELDL TLPTNFRDLS KPIGALNPKR AAFFAERYES WEDDQVPKFH
2310 2320 2330 2340 2350
YGTHYSTASF VLAWLLRIEP FTTYFLNLQG GKFDHADRTF SSISRAWRNS
2360 2370 2380 2390 2400
QRDTSDIKEL IPEFYYLPEM FVNFNNYNLG VMDDGTVVSD VELPPWAKTS
2410 2420 2430 2440 2450
EEFVHINRLA LESEFVSCQL HQWIDLIFGY KQQGPEAVRA LNVFYYLTYE
2460 2470 2480 2490 2500
GAVNLNSITD PVLREAVEAQ IRSFGQTPSQ LLIEPHPPRG SAMQVSPLMF
2510 2520 2530 2540 2550
TDKAQQDVIM VLKFPSNSPV THVAANTQPG LATPAVITVT ANRLFAVNKW
2560 2570 2580 2590 2600
HNLPAHQGAV QDQPYQLPVE IDPLIASNTG MHRRQITDLL DQSIQVHSQC
2610 2620 2630 2640 2650
FVITSDNRYI LVCGFWDKSF RVYSTDTGRL IQVVFGHWDV VTCLARSESY
2660 2670 2680 2690 2700
IGGNCYILSG SRDATLLLWY WNGKCSGIGD NPGSETAAPR AILTGHDYEV
2710 2720 2730 2740 2750
TCAAVCAELG LVLSGSQEGP CLIHSMNGDL LRTLEGPENC LKPKLIQASR
2760 2770 2780 2790 2800
EGHCVIFYEN GLFCTFSVNG KLQATMETDD NIRAIQLSRD GQYLLTGGDR
2810 2820 2830 2840 2850
GVVVVRQVSD LKQLFAYPGC DAGIRAMALS YDQRCIISGM ASGSIVLFYN
2860
DFNRWHHEYQ TRY
Length:2,863
Mass (Da):319,108
Last modified:September 22, 2009 - v4
Checksum:i58CD1F4314F685EE
GO
Isoform 2 (identifier: P50851-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2016-2026: Missing.
     2684-2684: Missing.

Show »
Length:2,851
Mass (Da):317,702
Checksum:iDA708A4D40A9889E
GO

Sequence cautioni

The sequence AAB09603.1 differs from that shown. Reason: Frameshift at positions 2674, 2851 and 2858. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti377 – 3771F → L in AAM53530 (PubMed:12160729).Curated
Sequence conflicti750 – 7512LA → RP in AAG48558 (PubMed:11254716).Curated
Sequence conflicti2179 – 21791Y → F in AAG48558 (PubMed:11254716).Curated
Sequence conflicti2179 – 21791Y → F in AAB09603 (PubMed:15815621).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1090 – 10901A → G.1 Publication
Corresponds to variant rs1782360 [ dbSNP | Ensembl ].
VAR_057605
Natural varianti1230 – 12301G → D.
Corresponds to variant rs34708681 [ dbSNP | Ensembl ].
VAR_057606
Natural varianti1677 – 16771N → S.
Corresponds to variant rs17027133 [ dbSNP | Ensembl ].
VAR_057607
Natural varianti1997 – 19971R → C.
Corresponds to variant rs35879351 [ dbSNP | Ensembl ].
VAR_057608
Natural varianti2038 – 20381Q → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_035883
Natural varianti2274 – 22741G → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_035884
Natural varianti2657 – 26571I → S in CVID8. 1 Publication
Corresponds to variant rs199469663 [ dbSNP | Ensembl ].
VAR_068690
Natural varianti2701 – 27011T → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_035885
Natural varianti2704 – 27041A → T.
Corresponds to variant rs3749574 [ dbSNP | Ensembl ].
VAR_057609
Natural varianti2713 – 27131L → F.
Corresponds to variant rs34662958 [ dbSNP | Ensembl ].
VAR_057610
Natural varianti2809 – 28091S → L.
Corresponds to variant rs2290846 [ dbSNP | Ensembl ].
VAR_022028

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2016 – 202611Missing in isoform 2. 1 PublicationVSP_038225Add
BLAST
Alternative sequencei2684 – 26841Missing in isoform 2. 1 PublicationVSP_038226

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216648 mRNA. Translation: AAG48558.2.
AF217149 mRNA. Translation: AAG48559.1.
AF467287 mRNA. Translation: AAM53530.1.
AC092544 Genomic DNA. No translation available.
AC092612 Genomic DNA. No translation available.
AC093748 Genomic DNA. Translation: AAY40984.1.
AC097373 Genomic DNA. Translation: AAY40973.1.
AC104796 Genomic DNA. No translation available.
AC110813 Genomic DNA. No translation available.
M83822 mRNA. Translation: AAB09603.1. Frameshift.
CCDSiCCDS3773.1. [P50851-1]
CCDS58928.1. [P50851-2]
RefSeqiNP_001186211.2. NM_001199282.2. [P50851-2]
NP_006717.2. NM_006726.4. [P50851-1]
XP_011530736.1. XM_011532434.1. [P50851-1]
UniGeneiHs.480938.

Genome annotation databases

EnsembliENST00000357115; ENSP00000349629; ENSG00000198589. [P50851-1]
ENST00000510413; ENSP00000421552; ENSG00000198589. [P50851-2]
GeneIDi987.
KEGGihsa:987.
UCSCiuc003ilu.5. human. [P50851-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216648 mRNA. Translation: AAG48558.2.
AF217149 mRNA. Translation: AAG48559.1.
AF467287 mRNA. Translation: AAM53530.1.
AC092544 Genomic DNA. No translation available.
AC092612 Genomic DNA. No translation available.
AC093748 Genomic DNA. Translation: AAY40984.1.
AC097373 Genomic DNA. Translation: AAY40973.1.
AC104796 Genomic DNA. No translation available.
AC110813 Genomic DNA. No translation available.
M83822 mRNA. Translation: AAB09603.1. Frameshift.
CCDSiCCDS3773.1. [P50851-1]
CCDS58928.1. [P50851-2]
RefSeqiNP_001186211.2. NM_001199282.2. [P50851-2]
NP_006717.2. NM_006726.4. [P50851-1]
XP_011530736.1. XM_011532434.1. [P50851-1]
UniGeneiHs.480938.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T77X-ray2.40A/B/C/D2076-2489[»]
ProteinModelPortaliP50851.
SMRiP50851. Positions 2076-2489, 2600-2812.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107423. 25 interactions.
DIPiDIP-50531N.
IntActiP50851. 6 interactions.
STRINGi9606.ENSP00000349629.

PTM databases

iPTMnetiP50851.
PhosphoSiteiP50851.

Polymorphism and mutation databases

BioMutaiLRBA.
DMDMi259016388.

Proteomic databases

EPDiP50851.
MaxQBiP50851.
PaxDbiP50851.
PeptideAtlasiP50851.
PRIDEiP50851.

Protocols and materials databases

DNASUi987.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357115; ENSP00000349629; ENSG00000198589. [P50851-1]
ENST00000510413; ENSP00000421552; ENSG00000198589. [P50851-2]
GeneIDi987.
KEGGihsa:987.
UCSCiuc003ilu.5. human. [P50851-1]

Organism-specific databases

CTDi987.
GeneCardsiLRBA.
HGNCiHGNC:1742. LRBA.
HPAiHPA019366.
HPA023597.
MalaCardsiLRBA.
MIMi606453. gene.
614700. phenotype.
neXtProtiNX_P50851.
Orphaneti1572. Common variable immunodeficiency.
PharmGKBiPA30444.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1786. Eukaryota.
ENOG410XNQC. LUCA.
GeneTreeiENSGT00760000119083.
HOGENOMiHOG000082375.
HOVERGENiHBG012582.
InParanoidiP50851.
OMAiEEIGPCS.
OrthoDBiEOG7HTHG2.
PhylomeDBiP50851.
TreeFamiTF313490.

Enzyme and pathway databases

SignaLinkiP50851.

Miscellaneous databases

ChiTaRSiLRBA. human.
EvolutionaryTraceiP50851.
GeneWikiiLRBA.
GenomeRNAii987.
PROiP50851.
SOURCEiSearch...

Gene expression databases

BgeeiP50851.
CleanExiHS_LRBA.
ExpressionAtlasiP50851. baseline and differential.
GenevisibleiP50851. HS.

Family and domain databases

Gene3Di1.10.1540.10. 1 hit.
2.130.10.10. 1 hit.
2.30.29.40. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000409. BEACH_dom.
IPR013320. ConA-like_dom.
IPR010508. DUF1088.
IPR031570. DUF4704.
IPR023362. PH-BEACH_dom.
IPR011993. PH_dom-like.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF02138. Beach. 1 hit.
PF06469. DUF1088. 1 hit.
PF15787. DUF4704. 1 hit.
PF14844. PH_BEACH. 1 hit.
[Graphical view]
SMARTiSM01026. Beach. 1 hit.
SM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF50978. SSF50978. 1 hit.
SSF81837. SSF81837. 1 hit.
PROSITEiPS50197. BEACH. 1 hit.
PS51783. PH_BEACH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel lipopolysaccharide-inducible gene with key features of both A kinase anchor proteins and chs1/beige proteins."
    Wang J.-W., Howson J., Haller E., Kerr W.G.
    J. Immunol. 166:4586-4595(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "BCL8 is a novel, evolutionarily conserved human gene family encoding proteins with presumptive protein kinase A anchoring function."
    Dyomin V.G., Chaganti S.R., Dyomina K., Palanisamy N., Murty V.V.V.S., Dalla-Favera R., Chaganti R.S.K.
    Genomics 80:158-165(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, VARIANT GLY-1090.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Mager D.L.
    Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 775-2863 (ISOFORM 1).
  5. "Strategy for detecting cellular transcripts promoted by human endogenous long terminal repeats: identification of a novel gene (CDC4L) with homology to yeast CDC4."
    Feuchter A.E., Freeman J.D., Mager D.L.
    Genomics 13:1237-1246(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2179-2863 (ISOFORM 1).
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-1100 AND SER-1139, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-1135; SER-1247; SER-1261; SER-1488; SER-1498; SER-2064 AND SER-2496, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1261 AND SER-1605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Crystal structure of the PH-BEACH domains of human LRBA/BGL."
    Gebauer D., Li J., Jogl G., Shen Y., Myszka D.G., Tong L.
    Biochemistry 43:14873-14880(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2076-2489.
  18. Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-2038; ARG-2274 AND LYS-2701.
  19. Cited for: VARIANT CVID8 SER-2657.

Entry informationi

Entry nameiLRBA_HUMAN
AccessioniPrimary (citable) accession number: P50851
Secondary accession number(s): Q4W5J4
, Q4W5L6, Q8NFQ0, Q9H2U3, Q9H2U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 22, 2009
Last modified: July 6, 2016
This is version 160 of the entry and version 4 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 said to be similar to yeast CDC4, but that similarity is very limited.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

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 one 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.