RBCC

Full text data of LPIN2

LPIN2 (KIAA0249) [Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Phosphatidate phosphatase LPIN2; 3.1.3.4 (Lipin-2)

UniProt Q92539
ID LPIN2_HUMAN Reviewed; 896 AA.
AC Q92539; A7MD25; D3DUH3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1997, sequence version 1.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Phosphatidate phosphatase LPIN2;
DE EC=3.1.3.4;
DE AltName: Full=Lipin-2;
GN Name=LPIN2; Synonyms=KIAA0249;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI.
RT The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
RT analysis of cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17158099; DOI=10.1074/jbc.M610745200;
RA Donkor J., Sariahmetoglu M., Dewald J., Brindley D.N., Reue K.;
RT "Three mammalian lipins act as phosphatidate phosphatases with
RT distinct tissue expression patterns.";
RL J. Biol. Chem. 282:3450-3457(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP VARIANT MAJEEDS LEU-734, AND TISSUE SPECIFICITY.
RX PubMed=15994876; DOI=10.1136/jmg.2005.030759;
RA Ferguson P.J., Chen S., Tayeh M.K., Ochoa L., Leal S.M., Pelet A.,
RA Munnich A., Lyonnet S., Majeed H.A., El-Shanti H.;
RT "Homozygous mutations in LPIN2 are responsible for the syndrome of
RT chronic recurrent multifocal osteomyelitis and congenital
RT dyserythropoietic anaemia (Majeed syndrome).";
RL J. Med. Genet. 42:551-557(2005).
CC -!- FUNCTION: Plays important roles in controlling the metabolism of
CC fatty acids at differents levels. Acts as a magnesium-dependent
CC phosphatidate phosphatase enzyme which catalyzes the conversion of
CC phosphatidic acid to diacylglycerol during triglyceride,
CC phosphatidylcholine and phosphatidylethanolamine biosynthesis in
CC the reticulum endoplasmic membrane. Acts also as a nuclear
CC transcriptional coactivator for PPARGC1A to modulate lipid
CC metabolism (By similarity).
CC -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC 1,2-diacyl-sn-glycerol + phosphate.
CC -!- COFACTOR: Mg(2+) (By similarity).
CC -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm, cytosol
CC (By similarity). Endoplasmic reticulum membrane (By similarity).
CC Note=Translocates to endoplasmic reticulum membrane with
CC increasing levels of oleate (By similarity).
CC -!- TISSUE SPECIFICITY: Expressed in liver, lung, kidney, placenta,
CC spleen, thymus, lymph node, prostate, testes, small intestine, and
CC colon.
CC -!- DOMAIN: Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic
CC motif known to be essential for phosphatidate phosphatase activity
CC (By similarity).
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, a motif
CC known to be a transcriptional binding motif (By similarity).
CC -!- DISEASE: Majeed syndrome (MAJEEDS) [MIM:609628]: An autosomal
CC recessive syndrome characterized by chronic recurrent multifocal
CC osteomyelitis that is of early onset with a lifelong course,
CC congenital dyserythropoietic anemia that presents as hypochromic,
CC microcytic anemia during the first year of life and ranges from
CC mild to transfusion-dependent, and transient inflammatory
CC dermatosis, often manifesting as Sweet syndrome (neutrophilic skin
CC infiltration). Note=The disease is caused by mutations affecting
CC the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the lipin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13380.2; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=INFEVERS; Note=Repertory of FMF and hereditary
CC autoinflammatory disorders mutations;
CC URL="http://fmf.igh.cnrs.fr/ISSAID/infevers/search.php?n=7";
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DR EMBL; D87436; BAA13380.2; ALT_INIT; mRNA.
DR EMBL; CH471113; EAX01686.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01687.1; -; Genomic_DNA.
DR EMBL; BC152448; AAI52449.1; -; mRNA.
DR RefSeq; NP_055461.1; NM_014646.2.
DR RefSeq; XP_005258235.1; XM_005258178.1.
DR RefSeq; XP_005258236.1; XM_005258179.1.
DR UniGene; Hs.132342; -.
DR ProteinModelPortal; Q92539; -.
DR IntAct; Q92539; 2.
DR STRING; 9606.ENSP00000261596; -.
DR PhosphoSite; Q92539; -.
DR DMDM; 2495724; -.
DR PaxDb; Q92539; -.
DR PRIDE; Q92539; -.
DR DNASU; 9663; -.
DR Ensembl; ENST00000261596; ENSP00000261596; ENSG00000101577.
DR GeneID; 9663; -.
DR KEGG; hsa:9663; -.
DR UCSC; uc002klo.3; human.
DR CTD; 9663; -.
DR GeneCards; GC18M002906; -.
DR HGNC; HGNC:14450; LPIN2.
DR HPA; CAB015223; -.
DR HPA; HPA017857; -.
DR MIM; 605519; gene.
DR MIM; 609628; phenotype.
DR neXtProt; NX_Q92539; -.
DR Orphanet; 77297; Majeed syndrome.
DR PharmGKB; PA30437; -.
DR eggNOG; COG5083; -.
DR HOGENOM; HOG000230954; -.
DR HOVERGEN; HBG052338; -.
DR InParanoid; Q92539; -.
DR KO; K15728; -.
DR OMA; EDTVCTI; -.
DR OrthoDB; EOG7QZG8X; -.
DR PhylomeDB; Q92539; -.
DR Reactome; REACT_111217; Metabolism.
DR GenomeRNAi; 9663; -.
DR NextBio; 36287; -.
DR PRO; PR:Q92539; -.
DR ArrayExpress; Q92539; -.
DR Bgee; Q92539; -.
DR CleanEx; HS_LPIN2; -.
DR Genevestigator; Q92539; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; TAS:Reactome.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR007651; Lipin_N.
DR InterPro; IPR013209; LNS2.
DR InterPro; IPR026744; LPIN2.
DR PANTHER; PTHR12181:SF11; PTHR12181:SF11; 1.
DR Pfam; PF04571; Lipin_N; 1.
DR Pfam; PF08235; LNS2; 1.
DR SMART; SM00775; LNS2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Congenital dyserythropoietic anemia; Cytoplasm;
KW Disease mutation; Endoplasmic reticulum; Fatty acid metabolism;
KW Hereditary hemolytic anemia; Hydrolase; Lipid metabolism; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1 896 Phosphatidate phosphatase LPIN2.
FT /FTId=PRO_0000209881.
FT REGION 1 108 N-LIP.
FT REGION 635 837 C-LIP.
FT MOTIF 153 158 Nuclear localization signal (Potential).
FT MOTIF 689 693 DXDXT motif.
FT MOTIF 700 704 LXXIL motif.
FT MOD_RES 106 106 Phosphoserine (By similarity).
FT MOD_RES 186 186 Phosphoserine (By similarity).
FT MOD_RES 187 187 Phosphoserine (By similarity).
FT VARIANT 734 734 S -> L (in MAJEEDS).
FT /FTId=VAR_023817.
SQ SEQUENCE 896 AA; 99399 MW; 080113FCCA533272 CRC64;
MNYVGQLAGQ VIVTVKELYK GINQATLSGC IDVIVVQQQD GSYQCSPFHV RFGKLGVLRS
KEKVIDIEIN GSAVDLHMKL GDNGEAFFVE ETEEEYEKLP AYLATSPIPT EDQFFKDIDT
PLVKSGGDET PSQSSDISHV LETETIFTPS SVKKKKRRRK KYKQDSKKEE QAASAAAEDT
CDVGVSSDDD KGAQAARGSS NASLKEEECK EPLLFHSGDH YPLSDGDWSP LETTYPQTAC
PKSDSELEVK PAESLLRSES HMEWTWGGFP ESTKVSKRER SDHHPRTATI TPSENTHFRV
IPSEDNLISE VEKDASMEDT VCTIVKPKPR ALGTQMSDPT SVAELLEPPL ESTQISSMLD
ADHLPNAALA EAPSESKPAA KVDSPSKKKG VHKRSQHQGP DDIYLDDLKG LEPEVAALYF
PKSESEPGSR QWPESDTLSG SQSPQSVGSA AADSGTECLS DSAMDLPDVT LSLCGGLSEN
GEISKEKFME HIITYHEFAE NPGLIDNPNL VIRIYNRYYN WALAAPMILS LQVFQKSLPK
ATVESWVKDK MPKKSGRWWF WRKRESMTKQ LPESKEGKSE APPASDLPSS SKEPAGARPA
ENDSSSDEGS QELEESITVD PIPTEPLSHG STTSYKKSLR LSSDQIAKLK LHDGPNDVVF
SITTQYQGTC RCAGTIYLWN WNDKIIISDI DGTITKSDAL GQILPQLGKD WTHQGIAKLY
HSINENGYKF LYCSARAIGM ADMTRGYLHW VNDKGTILPR GPLMLSPSSL FSAFHREVIE
KKPEKFKIEC LNDIKNLFAP SKQPFYAAFG NRPNDVYAYT QVGVPDCRIF TVNPKGELIQ
ERTKGNKSSY HRLSELVEHV FPLLSKEQNS AFPCPEFSSF CYWRDPIPEV DLDDLS
//

MIM 605519
*RECORD*
*FIELD* NO
605519
*FIELD* TI
*605519 LIPIN 2; LPIN2
*FIELD* TX

CLONING

Mice carrying mutations in the fatty liver dystrophy (fld) gene have
read morefeatures of human lipodystrophy (Reue et al., 2000). In the human,
lipodystrophy is a heterogeneous group of disorders characterized by
loss of body fat, fatty liver, hypertriglyceridemia, and insulin
resistance. Through positional cloning, Peterfy et al. (2001) isolated
the gene responsible for fatty liver dystrophy in mice and characterized
2 independent mutant alleles of the fld gene. They designated the gene
Lpin1 and named the novel nuclear protein which it encodes lipin.
Through database searches, Peterfy et al. (2001) identified several
mouse and human EST and genomic sequences with similarities to Lpin1.
These included 2 Lpin1-related mouse genes (Lpin2 and Lpin3) and 3 human
homologs (LPIN1 (605518), LPIN2, and LPIN3 (605520)). LPIN2 is identical
to the KIAA0249 gene identified by Nagase et al. (1996).

By PCR and Northern blot analysis, Ferguson et al. (2005) detected a
6-kb LPIN2 transcript in multiple human tissues including liver, lung,
kidney, and placenta.

GENE STRUCTURE

Ferguson et al. (2005) noted that the LPIN2 gene contains 20 exons
spanning 95 kb.

MAPPING

Using sequence databases, Peterfy et al. (2001) mapped the human LPIN2
gene to 18p. They mapped the mouse gene to chromosome 17.

MOLECULAR GENETICS

In 2 consanguineous Arab families with Majeed syndrome (609628),
previously reported by Majeed et al. (1989, 2000, 2001), Ferguson et al.
(2005) identified homozygosity for a missense mutation (S734L;
605519.0001) and a 2-bp deletion (605519.0002) in the LPIN2 gene,
respectively.

*FIELD* AV
.0001
MAJEED SYNDROME
LPIN2, SER734LEU

In 4 affected members of 2 consanguineous sibships of a Jordanian Arab
family with Majeed syndrome (609628), previously reported by Majeed et
al. (1989, 2000), Ferguson et al. (2005) identified homozygosity for a
2201C-T transition in exon 17 of the LPIN2 gene, resulting in a
ser734-to-leu (S734L) substitution. The mutation was not found in 2,300
unrelated (CEPH) chromosomes, but it had a frequency of 0.005 (4
heterozygotes in 734 chromosomes) in 367 unrelated, ethnically matched
Jordanian controls.

.0002
MAJEED SYNDROME
LPIN2, 2-BP DEL, 540AT

In 2 affected sibs of a consanguineous Jordanian Arab family with Majeed
syndrome (609628), previously reported by Majeed et al. (2001), Ferguson
et al. (2005) identified homozygosity for a 2-bp deletion (540delAT) in
exon 4 of the LPIN2 gene, resulting in a stop codon at position 181. The
mutation was not found in 2,300 unrelated (CEPH) chromosomes, or in 367
unrelated, ethnically matched Jordanian controls.

*FIELD* RF
1. Ferguson, P. J.; Chen, S.; Tayeh, M. K.; Ochoa, L.; Leal, S. M.;
Pelet, A.; Munnich, A.; Lyonnet, S.; Majeed, H. A.; El-Shanti, H.
: Homozygous mutations in LPIN2 are responsible for the syndrome of
chronic recurrent multifocal osteomyelitis and congenital dyserythropoietic
anaemia (Majeed syndrome). J. Med. Genet. 42: 551-557, 2005.

2. Majeed, H. A.; Al-Tarawna, M.; El-Shanti, H.; Kamel, B.; Al-Khalaileh,
F.: The syndrome of chronic recurrent multifocal osteomyelitis and
congenital dyserythropoietic anaemia: report of a new family and a
review. Europ. J. Pediat. 160: 705-710, 2001.

3. Majeed, H. A.; El-Shanti, H.; Al-Rimawa, H.; Al-Masri, N.: On
mice and men: an autosomal recessive syndrome of chronic recurrent
multifocal osteomyelitis and congenital dyserythropoietic anemia.
(Letter) J. Pediat. 137: 441-442, 2000.

4. Majeed, H. A.; Kalaawi, M.; Mohanty, D.; Teebi, A. S.; Tunjekar,
M. F.; Al-Gharbawy, F.; Majeed, S. A.; Al-Gazzar, A. H.: Congenital
dyserythropoietic anemia and chronic recurrent multifocal osteomyelitis
in three related children and the association with Sweet syndrome
in two siblings. J. Pediat. 115: 730-734, 1989.

5. Nagase, T.; Seki, N.; Ishikawa, K.; Ohira, M.; Kawarabayasi, Y.;
Ohara, O.; Tanaka, A.; Kotani, H.; Miyajima, N.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. VI. The coding
sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis
of cDNA clones from cell line KG-1 and brain. DNA Res. 3: 321-329,
1996.

6. Peterfy, M.; Phan, J.; Xu, P.; Reue, K.: Lipodystrophy in the
fld mouse results from mutation of a new gene encoding a nuclear protein,
lipin. Nature Genet. 27: 121-124, 2001.

7. Reue, K.; Xu, P.; Wang, X.-P.; Slavin, B. G.: Adipose tissue deficiency,
glucose intolerance, and increased atherosclerosis result from mutation
in the mouse fatty liver dystrophy (fld) gene. J. Lipid Res. 41:
1067-1076, 2000.

*FIELD* CN
Marla J. F. O'Neill - updated: 9/19/2005

*FIELD* CD
Victor A. McKusick: 1/2/2001

*FIELD* ED
wwang: 10/05/2005
terry: 9/19/2005
mgross: 1/23/2001
mgross: 1/2/2001

MIM 609628
*RECORD*
*FIELD* NO
609628
*FIELD* TI
#609628 MAJEED SYNDROME
;;CHRONIC RECURRENT MULTIFOCAL OSTEOMYELITIS, CONGENITAL DYSERYTHROPOIETIC
read moreANEMIA, AND NEUTROPHILIC DERMATOSIS
*FIELD* TX
A number sign (#) is used with this entry because of evidence that
Majeed syndrome can be caused by mutation in the LPIN2 gene (605519).

CLINICAL FEATURES

Majeed et al. (1989) reported 2 brothers and a female cousin who had
chronic recurrent multifocal osteomyelitis (CRMO; 259680) and congenital
dyserythropoietic anemia (CDA); the brothers also had neutrophilic
dermatosis or Sweet syndrome (608068). The clinical course of all 3
children was similar; the unaffected parents in both families were
consanguineous.

Majeed et al. (2000) reported a fourth child with CRMO and CDA born into
the consanguineous Arab family previously reported by Majeed et al.
(1989), a brother of the female cousin. Over a period of 9 to 16 years
of follow-up, the course of CRMO in these patients was characterized by
early onset and 1 to 3 episodes per month, sometimes associated with
mild fever. The 4 children failed to thrive; height and weight were
below the 5th percentile with delayed bone age. All had significant
hepatosplenomegaly and had required blood transfusions on several
occasions. Their peripheral blood smears showed hypochromia and
microcytosis, in contrast to the normo- and macrocytosis reported in
other variants of CDA (see 224120). Majeed et al. (2000) concluded that
the combination of CRMO characterized by early onset, aggressive course,
and long duration with a new microcytic type of CDA represented a new
autosomal recessive syndrome.

Majeed et al. (2001) reported a brother and sister, born into a
consanguineous Arab family, who developed Majeed syndrome at 3 weeks and
2 months of age, respectively. The diagnosis of CRMO was confirmed by
radiography and technetium isotope bone scans; bone marrow studies
confirmed the diagnosis of CDA, which was hypochromic and microcytic on
peripheral blood smears. At age 21, the brother still had active CRMO
with frequent relapses; both patients' height and weight were below the
5th percentile. The first-cousin parents and 3 other sibs were
unaffected.

Ferguson et al. (2005) noted that although Sweet syndrome was
definitively diagnosed in only the 2 brothers reported by Majeed et al.
(1989), the 2 cousins reported by Majeed et al. (1989, 2000) in that
family had a history of rash that was consistent with Sweet syndrome.
Ferguson et al. (2005) stated that the 2 affected sibs from the second
family reported by Majeed et al. (2001) did not have Sweet syndrome, but
1 of them had a history of cutaneous pustulosis, and an obligate carrier
from that family had severe psoriasis.

MOLECULAR GENETICS

In 2 consanguineous Arab families with Majeed syndrome, previously
reported by Majeed et al. (1989, 2000, 2001), Ferguson et al. (2005)
identified homozygosity for a missense mutation (S734L; 605519.0001) and
a 2-bp deletion (605519.0002) in the LPIN2 gene, respectively.

*FIELD* RF
1. Ferguson, P. J.; Chen, S.; Tayeh, M. K.; Ochoa, L.; Leal, S. M.;
Pelet, A.; Munnich, A.; Lyonnet, S.; Majeed, H. A.; El-Shanti, H.
: Homozygous mutations in LPIN2 are responsible for the syndrome of
chronic recurrent multifocal osteomyelitis and congenital dyserythropoietic
anaemia (Majeed syndrome). J. Med. Genet. 42: 551-557, 2005.

2. Majeed, H. A.; Al-Tarawna, M.; El-Shanti, H.; Kamel, B.; Al-Khalaileh,
F.: The syndrome of chronic recurrent multifocal osteomyelitis and
congenital dyserythropoietic anaemia: report of a new family and a
review. Europ. J. Pediat. 160: 705-710, 2001.

3. Majeed, H. A.; El-Shanti, H.; Al-Rimawa, H.; Al-Masri, N.: On
mice and men: an autosomal recessive syndrome of chronic recurrent
multifocal osteomyelitis and congenital dyserythropoietic anemia.
(Letter) J. Pediat. 137: 441-442, 2000.

4. Majeed, H. A.; Kalaawi, M.; Mohanty, D.; Teebi, A. S.; Tunjekar,
M. F.; Al-Gharbawy, F.; Majeed, S. A.; Al-Gazzar, A. H.: Congenital
dyserythropoietic anemia and chronic recurrent multifocal osteomyelitis
in three related children and the association with Sweet syndrome
in two siblings. J. Pediat. 115: 730-734, 1989.

*FIELD* CD
Marla J. F. O'Neill: 10/4/2005

*FIELD* ED
carol: 07/06/2007
wwang: 10/25/2005
wwang: 10/24/2005
wwang: 10/21/2005
mgross: 10/18/2005
wwang: 10/17/2005
wwang: 10/14/2005
wwang: 10/12/2005
wwang: 10/5/2005

RBCC Red Blood Cell Collection

Full text data of LPIN2