Full text data of LSP1
LSP1
(WP34)
[Confidence: low (only semi-automatic identification from reviews)]
Lymphocyte-specific protein 1 (47 kDa actin-binding protein; 52 kDa phosphoprotein; pp52; Lymphocyte-specific antigen WP34)
Lymphocyte-specific protein 1 (47 kDa actin-binding protein; 52 kDa phosphoprotein; pp52; Lymphocyte-specific antigen WP34)
UniProt
P33241
ID LSP1_HUMAN Reviewed; 339 AA.
AC P33241; B3KPP1; B3KRR6; E9PBV6; E9PFP3; Q16096; Q53H48; Q6FHM3;
read moreAC Q9BUY8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Lymphocyte-specific protein 1;
DE AltName: Full=47 kDa actin-binding protein;
DE AltName: Full=52 kDa phosphoprotein;
DE Short=pp52;
DE AltName: Full=Lymphocyte-specific antigen WP34;
GN Name=LSP1; Synonyms=WP34;
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 [MRNA] (ISOFORM 1).
RX PubMed=2295815;
RA Jongstra-Bilen J., Young A.J., Chong R., Jongstra J.;
RT "Human and mouse LSP1 genes code for highly conserved
RT phosphoproteins.";
RL J. Immunol. 144:1104-1110(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lymphocyte;
RX PubMed=2174784; DOI=10.1002/eji.1830201109;
RA Kadiyala R.K., McIntyre B.W., Krensky A.M.;
RT "Molecular cloning and characterization of WP34, a phosphorylated
RT human lymphocyte differentiation and activation antigen.";
RL Eur. J. Immunol. 20:2417-2423(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8274738;
RA Howard T., Li Y., Torres M., Guerrero A., Coates T.;
RT "The 47-kD protein increased in neutrophil actin dysfunction with 47-
RT and 89-kD protein abnormalities is lymphocyte-specific protein.";
RL Blood 83:231-241(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP THR-100.
RC TISSUE=Esophagus, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP THR-100.
RC TISSUE=Dermoid cancer;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP THR-100.
RC TISSUE=Lymph;
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 [9]
RP PHOSPHORYLATION AT SER-252 BY MAPKAPK2.
RX PubMed=17481585; DOI=10.1016/j.bbrc.2007.04.104;
RA Wu Y., Zhan L., Ai Y., Hannigan M., Gaestel M., Huang C.-K.,
RA Madri J.A.;
RT "MAPKAPK2-mediated LSP1 phosphorylation and FMLP-induced neutrophil
RT polarization.";
RL Biochem. Biophys. Res. Commun. 358:170-175(2007).
RN [10]
RP PHOSPHORYLATION AT SER-252, AND MASS SPECTROMETRY.
RA Carrascal M., Abian J.;
RL Submitted (JUN-2007) to UniProtKB.
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May play a role in mediating neutrophil activation and
CC chemotaxis (By similarity).
CC -!- SUBUNIT: Binds actin.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P33241-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33241-2; Sequence=VSP_045655;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P33241-3; Sequence=VSP_045983;
CC Note=No experimental confirmation available. Ref.5 (BAG52478)
CC sequence is in conflict in position: 31:G->Q;
CC -!- TISSUE SPECIFICITY: Activated T-lymphocytes.
CC -!- PTM: Phosphorylated by casein kinase II, protein kinase C and
CC MAPKAPK2. Phosphorylation by PKC induces translocation from
CC membrane to cytoplasm. Phosphorylation by MAPKAPK2 may regulate
CC neutrophil chemotaxis (By similarity).
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DR EMBL; M33552; AAA59534.1; -; mRNA.
DR EMBL; X55188; CAA38971.1; -; mRNA.
DR EMBL; S67783; AAB29545.1; -; mRNA.
DR EMBL; CR541728; CAG46529.1; -; mRNA.
DR EMBL; CR541754; CAG46554.1; -; mRNA.
DR EMBL; AK056576; BAG51753.1; -; mRNA.
DR EMBL; AK092071; BAG52478.1; -; mRNA.
DR EMBL; AK222733; BAD96453.1; -; mRNA.
DR EMBL; AC051649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001785; AAH01785.1; -; mRNA.
DR PIR; A43542; A43542.
DR RefSeq; NP_001013271.1; NM_001013253.1.
DR RefSeq; NP_001013272.1; NM_001013254.1.
DR RefSeq; NP_001013273.1; NM_001013255.1.
DR RefSeq; NP_001229861.1; NM_001242932.1.
DR RefSeq; NP_002330.1; NM_002339.2.
DR RefSeq; XP_005252982.1; XM_005252925.1.
DR RefSeq; XP_005252983.1; XM_005252926.1.
DR RefSeq; XP_005252984.1; XM_005252927.1.
DR UniGene; Hs.56729; -.
DR PDB; 3BH8; X-ray; 1.65 A; C=249-258.
DR PDBsum; 3BH8; -.
DR ProteinModelPortal; P33241; -.
DR STRING; 9606.ENSP00000308383; -.
DR PhosphoSite; P33241; -.
DR DMDM; 462553; -.
DR SWISS-2DPAGE; P33241; -.
DR PaxDb; P33241; -.
DR PeptideAtlas; P33241; -.
DR PRIDE; P33241; -.
DR DNASU; 4046; -.
DR Ensembl; ENST00000311604; ENSP00000308383; ENSG00000130592.
DR Ensembl; ENST00000381775; ENSP00000371194; ENSG00000130592.
DR Ensembl; ENST00000405957; ENSP00000383932; ENSG00000130592.
DR Ensembl; ENST00000406638; ENSP00000384022; ENSG00000130592.
DR GeneID; 4046; -.
DR KEGG; hsa:4046; -.
DR UCSC; uc001lui.3; human.
DR CTD; 4046; -.
DR GeneCards; GC11P001874; -.
DR HGNC; HGNC:6707; LSP1.
DR HPA; CAB017781; -.
DR HPA; HPA019693; -.
DR MIM; 153432; gene.
DR neXtProt; NX_P33241; -.
DR PharmGKB; PA30472; -.
DR eggNOG; NOG302084; -.
DR HOGENOM; HOG000231050; -.
DR HOVERGEN; HBG001610; -.
DR KO; K14957; -.
DR OMA; SDWSQKP; -.
DR OrthoDB; EOG7FNC7W; -.
DR PhylomeDB; P33241; -.
DR SignaLink; P33241; -.
DR ChiTaRS; LSP1; human.
DR EvolutionaryTrace; P33241; -.
DR GeneWiki; LSP1; -.
DR GenomeRNAi; 4046; -.
DR NextBio; 15838; -.
DR PRO; PR:P33241; -.
DR ArrayExpress; P33241; -.
DR Bgee; P33241; -.
DR CleanEx; HS_LSP1; -.
DR Genevestigator; P33241; -.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR GO; GO:0006928; P:cellular component movement; TAS:ProtInc.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR InterPro; IPR006018; Caldesmon_LSP.
DR InterPro; IPR002211; Lymphspecific.
DR PANTHER; PTHR12060; PTHR12060; 1.
DR Pfam; PF02029; Caldesmon; 1.
DR PRINTS; PR01083; LYMPHSPCIFIC.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Complete proteome; Direct protein sequencing; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 339 Lymphocyte-specific protein 1.
FT /FTId=PRO_0000084503.
FT MOD_RES 175 175 Phosphothreonine (By similarity).
FT MOD_RES 177 177 Phosphoserine (By similarity).
FT MOD_RES 189 189 Phosphoserine.
FT MOD_RES 252 252 Phosphoserine; by MAPKAPK2.
FT MOD_RES 327 327 N6-acetyllysine.
FT VAR_SEQ 1 62 Missing (in isoform 2).
FT /FTId=VSP_045655.
FT VAR_SEQ 1 18 MAEASSDPGAEEREELLG -> MAPIWSPPGRVSGCHLSSG
FT PAPGSAVGPWLGTPHPSLPLPLAPHKPPPPGLPGSAGQTSL
FT PAQRECVFPGDAAVHQELCGLGFEECLGSIPQAHQCYLTNG
FT PKRRKCSPRRRGRAPAWLCGGSPPCHQGLGHEHPSSGPSTN
FT CSPR (in isoform 3).
FT /FTId=VSP_045983.
FT VARIANT 100 100 A -> T (in dbSNP:rs621679).
FT /FTId=VAR_011867.
FT VARIANT 108 108 Q -> L (in dbSNP:rs11545725).
FT /FTId=VAR_061680.
FT VARIANT 229 229 Q -> K (in dbSNP:rs1803928).
FT /FTId=VAR_011868.
FT CONFLICT 15 15 Missing (in Ref. 3; AAB29545).
FT CONFLICT 24 24 S -> T (in Ref. 2; CAA38971).
FT CONFLICT 100 101 Missing (in Ref. 3; AAB29545).
FT CONFLICT 148 148 E -> D (in Ref. 5; BAG52478).
SQ SEQUENCE 339 AA; 37192 MW; F2A18533500611D9 CRC64;
MAEASSDPGA EEREELLGPT AQWSVEDEEE AVHEQCQHER DRQLQAQDEE GGGHVPERPK
QEMLLSLKPS EAPELDEDEG FGDWSQRPEQ RQQHEGAQGA LDSGEPPQCR SPEGEQEDRP
GLHAYEKEDS DEVHLEELSL SKEGPGPEDT VQDNLGAAGA EEEQEEHQKC QQPRTPSPLV
LEGTIEQSSP PLSPTTKLID RTESLNRSIE KSNSVKKSQP DLPISKIDQW LEQYTQAIET
AGRTPKLARQ ASIELPSMAV ASTKSRWETG EVQAQSAAKT PSCKDIVAGD MSKKSLWEQK
GGSKTSSTIK STPSGKRYKF VATGHGKYEK VLVEGGPAP
//
ID LSP1_HUMAN Reviewed; 339 AA.
AC P33241; B3KPP1; B3KRR6; E9PBV6; E9PFP3; Q16096; Q53H48; Q6FHM3;
read moreAC Q9BUY8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Lymphocyte-specific protein 1;
DE AltName: Full=47 kDa actin-binding protein;
DE AltName: Full=52 kDa phosphoprotein;
DE Short=pp52;
DE AltName: Full=Lymphocyte-specific antigen WP34;
GN Name=LSP1; Synonyms=WP34;
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 [MRNA] (ISOFORM 1).
RX PubMed=2295815;
RA Jongstra-Bilen J., Young A.J., Chong R., Jongstra J.;
RT "Human and mouse LSP1 genes code for highly conserved
RT phosphoproteins.";
RL J. Immunol. 144:1104-1110(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lymphocyte;
RX PubMed=2174784; DOI=10.1002/eji.1830201109;
RA Kadiyala R.K., McIntyre B.W., Krensky A.M.;
RT "Molecular cloning and characterization of WP34, a phosphorylated
RT human lymphocyte differentiation and activation antigen.";
RL Eur. J. Immunol. 20:2417-2423(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8274738;
RA Howard T., Li Y., Torres M., Guerrero A., Coates T.;
RT "The 47-kD protein increased in neutrophil actin dysfunction with 47-
RT and 89-kD protein abnormalities is lymphocyte-specific protein.";
RL Blood 83:231-241(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP THR-100.
RC TISSUE=Esophagus, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP THR-100.
RC TISSUE=Dermoid cancer;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP THR-100.
RC TISSUE=Lymph;
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 [9]
RP PHOSPHORYLATION AT SER-252 BY MAPKAPK2.
RX PubMed=17481585; DOI=10.1016/j.bbrc.2007.04.104;
RA Wu Y., Zhan L., Ai Y., Hannigan M., Gaestel M., Huang C.-K.,
RA Madri J.A.;
RT "MAPKAPK2-mediated LSP1 phosphorylation and FMLP-induced neutrophil
RT polarization.";
RL Biochem. Biophys. Res. Commun. 358:170-175(2007).
RN [10]
RP PHOSPHORYLATION AT SER-252, AND MASS SPECTROMETRY.
RA Carrascal M., Abian J.;
RL Submitted (JUN-2007) to UniProtKB.
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May play a role in mediating neutrophil activation and
CC chemotaxis (By similarity).
CC -!- SUBUNIT: Binds actin.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P33241-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33241-2; Sequence=VSP_045655;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P33241-3; Sequence=VSP_045983;
CC Note=No experimental confirmation available. Ref.5 (BAG52478)
CC sequence is in conflict in position: 31:G->Q;
CC -!- TISSUE SPECIFICITY: Activated T-lymphocytes.
CC -!- PTM: Phosphorylated by casein kinase II, protein kinase C and
CC MAPKAPK2. Phosphorylation by PKC induces translocation from
CC membrane to cytoplasm. Phosphorylation by MAPKAPK2 may regulate
CC neutrophil chemotaxis (By similarity).
CC -----------------------------------------------------------------------
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DR EMBL; M33552; AAA59534.1; -; mRNA.
DR EMBL; X55188; CAA38971.1; -; mRNA.
DR EMBL; S67783; AAB29545.1; -; mRNA.
DR EMBL; CR541728; CAG46529.1; -; mRNA.
DR EMBL; CR541754; CAG46554.1; -; mRNA.
DR EMBL; AK056576; BAG51753.1; -; mRNA.
DR EMBL; AK092071; BAG52478.1; -; mRNA.
DR EMBL; AK222733; BAD96453.1; -; mRNA.
DR EMBL; AC051649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001785; AAH01785.1; -; mRNA.
DR PIR; A43542; A43542.
DR RefSeq; NP_001013271.1; NM_001013253.1.
DR RefSeq; NP_001013272.1; NM_001013254.1.
DR RefSeq; NP_001013273.1; NM_001013255.1.
DR RefSeq; NP_001229861.1; NM_001242932.1.
DR RefSeq; NP_002330.1; NM_002339.2.
DR RefSeq; XP_005252982.1; XM_005252925.1.
DR RefSeq; XP_005252983.1; XM_005252926.1.
DR RefSeq; XP_005252984.1; XM_005252927.1.
DR UniGene; Hs.56729; -.
DR PDB; 3BH8; X-ray; 1.65 A; C=249-258.
DR PDBsum; 3BH8; -.
DR ProteinModelPortal; P33241; -.
DR STRING; 9606.ENSP00000308383; -.
DR PhosphoSite; P33241; -.
DR DMDM; 462553; -.
DR SWISS-2DPAGE; P33241; -.
DR PaxDb; P33241; -.
DR PeptideAtlas; P33241; -.
DR PRIDE; P33241; -.
DR DNASU; 4046; -.
DR Ensembl; ENST00000311604; ENSP00000308383; ENSG00000130592.
DR Ensembl; ENST00000381775; ENSP00000371194; ENSG00000130592.
DR Ensembl; ENST00000405957; ENSP00000383932; ENSG00000130592.
DR Ensembl; ENST00000406638; ENSP00000384022; ENSG00000130592.
DR GeneID; 4046; -.
DR KEGG; hsa:4046; -.
DR UCSC; uc001lui.3; human.
DR CTD; 4046; -.
DR GeneCards; GC11P001874; -.
DR HGNC; HGNC:6707; LSP1.
DR HPA; CAB017781; -.
DR HPA; HPA019693; -.
DR MIM; 153432; gene.
DR neXtProt; NX_P33241; -.
DR PharmGKB; PA30472; -.
DR eggNOG; NOG302084; -.
DR HOGENOM; HOG000231050; -.
DR HOVERGEN; HBG001610; -.
DR KO; K14957; -.
DR OMA; SDWSQKP; -.
DR OrthoDB; EOG7FNC7W; -.
DR PhylomeDB; P33241; -.
DR SignaLink; P33241; -.
DR ChiTaRS; LSP1; human.
DR EvolutionaryTrace; P33241; -.
DR GeneWiki; LSP1; -.
DR GenomeRNAi; 4046; -.
DR NextBio; 15838; -.
DR PRO; PR:P33241; -.
DR ArrayExpress; P33241; -.
DR Bgee; P33241; -.
DR CleanEx; HS_LSP1; -.
DR Genevestigator; P33241; -.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR GO; GO:0006928; P:cellular component movement; TAS:ProtInc.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR InterPro; IPR006018; Caldesmon_LSP.
DR InterPro; IPR002211; Lymphspecific.
DR PANTHER; PTHR12060; PTHR12060; 1.
DR Pfam; PF02029; Caldesmon; 1.
DR PRINTS; PR01083; LYMPHSPCIFIC.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Complete proteome; Direct protein sequencing; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 339 Lymphocyte-specific protein 1.
FT /FTId=PRO_0000084503.
FT MOD_RES 175 175 Phosphothreonine (By similarity).
FT MOD_RES 177 177 Phosphoserine (By similarity).
FT MOD_RES 189 189 Phosphoserine.
FT MOD_RES 252 252 Phosphoserine; by MAPKAPK2.
FT MOD_RES 327 327 N6-acetyllysine.
FT VAR_SEQ 1 62 Missing (in isoform 2).
FT /FTId=VSP_045655.
FT VAR_SEQ 1 18 MAEASSDPGAEEREELLG -> MAPIWSPPGRVSGCHLSSG
FT PAPGSAVGPWLGTPHPSLPLPLAPHKPPPPGLPGSAGQTSL
FT PAQRECVFPGDAAVHQELCGLGFEECLGSIPQAHQCYLTNG
FT PKRRKCSPRRRGRAPAWLCGGSPPCHQGLGHEHPSSGPSTN
FT CSPR (in isoform 3).
FT /FTId=VSP_045983.
FT VARIANT 100 100 A -> T (in dbSNP:rs621679).
FT /FTId=VAR_011867.
FT VARIANT 108 108 Q -> L (in dbSNP:rs11545725).
FT /FTId=VAR_061680.
FT VARIANT 229 229 Q -> K (in dbSNP:rs1803928).
FT /FTId=VAR_011868.
FT CONFLICT 15 15 Missing (in Ref. 3; AAB29545).
FT CONFLICT 24 24 S -> T (in Ref. 2; CAA38971).
FT CONFLICT 100 101 Missing (in Ref. 3; AAB29545).
FT CONFLICT 148 148 E -> D (in Ref. 5; BAG52478).
SQ SEQUENCE 339 AA; 37192 MW; F2A18533500611D9 CRC64;
MAEASSDPGA EEREELLGPT AQWSVEDEEE AVHEQCQHER DRQLQAQDEE GGGHVPERPK
QEMLLSLKPS EAPELDEDEG FGDWSQRPEQ RQQHEGAQGA LDSGEPPQCR SPEGEQEDRP
GLHAYEKEDS DEVHLEELSL SKEGPGPEDT VQDNLGAAGA EEEQEEHQKC QQPRTPSPLV
LEGTIEQSSP PLSPTTKLID RTESLNRSIE KSNSVKKSQP DLPISKIDQW LEQYTQAIET
AGRTPKLARQ ASIELPSMAV ASTKSRWETG EVQAQSAAKT PSCKDIVAGD MSKKSLWEQK
GGSKTSSTIK STPSGKRYKF VATGHGKYEK VLVEGGPAP
//
MIM
153432
*RECORD*
*FIELD* NO
153432
*FIELD* TI
*153432 LYMPHOCYTE-SPECIFIC PROTEIN; LSP1
;;pp52
*FIELD* TX
CLONING
Signal transduction in B lymphocytes following antigen binding to a
read moremembrane-associated immunoglobulin complex initiates a diverse array of
intracellular events. To define genes participating in these events, May
et al. (1993) and others used various cDNA cloning strategies to
identify genes preferentially expressed in B lymphocytes. One gene,
variously named LSP1 and pp52, exhibited a number of properties
supporting a possible role in B-cell signaling pathways. The gene codes
for a 52-kD phosphoprotein expressed only in transformed and
untransformed B cells, thymocytes, and untransformed T-cell lines.
Thompson et al. (1996) showed that tissue-specific alternative splicing
produced 2 different Lsp1 transcripts in mouse. In lymphocytes, exon 1L
is used, while exon 1S is used in stromal cells. Both the 5-prime
untranslated regions and amino acid sequences of the alternative exons
are distinct and are, apparently, transcribed using different
tissue-specific promoters.
MAPPING
May et al. (1993) mapped the LSP1 gene to 11p15.5 by fluorescence in
situ hybridization. They unexpectedly found that the human pp52 gene is
1 of 4 closely related loci. Two of the 4 loci harbored dysfunctional
frameshift mutations or premature translation stop sites. These
hybridized to 1q12 and 2p11.2. They were unable to map the fourth gene.
May et al. (1993) pointed out that 11p15.5 is a location associated with
karyotypic abnormalities in certain B-cell malignancies.
MOLECULAR GENETICS
Easton et al. (2007) identified a T/C SNP (dbSNP rs3817198) in the LSP1
gene that was significantly (p = 3 x 10(-9)) associated with familial
breast cancer (114480) in a 3-stage genomewide association study of
22,848 cases from 22 studies. Easton et al. (2007) found that the allele
was common in the U.K. population and thus unlikely to confer increased
disease risk individually. However, in combination with other
susceptibility alleles, the SNP may become clinically significant.
In a study of 9,442 BRCA1 (113705) and 5,665 BRCA2 (600185) mutation
carriers from 33 study centers, Antoniou et al. (2009) found that the
minor allele (C) of the SNP dbSNP rs3817198 in LSP1 on chromosome
11p15.5 was associated with increased breast cancer risk only for BRCA2
mutation carriers (P trend = 2.8 x 10(-4)).
ANIMAL MODEL
Liu et al. (2005) noted that LSP1 is an intracellular Ca(2+)- and
F-actin (see 102610)-binding protein and a major substrate of MAPKAPK2
(602006) in the p38 MAPK (MAPK14; 600289) pathway. Using intravital
microscopy, they demonstrated that Lsp1 -/- mice had impaired neutrophil
extravasation in response to Tnf (191160), Il1b (147720), and Cxcl1
(155730), but no deficit in neutrophil rolling or adhesion.
Transplantation experiments showed that wildtype leukocytes had a
migration defect in Lsp1 -/- mice, whereas Lsp1 -/- neutrophils
extravasated normally in wildtype mice. Vascular permeability to
histamine was also reduced in Lsp1 -/- mice. Immunofluorescence
microscopy and Western blot analysis showed that Lsp1 was present in
wildtype but not Lsp1 -/- microvascular endothelial cells, and cultured
human endothelial cells also expressed LSP1. Liu et al. (2005) proposed
that LSP1 expressed in endothelium regulates neutrophil transendothelial
migration.
*FIELD* RF
1. Antoniou, A. C.; Sinilnikova, O. M.; McGuffog, L.; Healey, S.;
Nevanlinna, H.; Heikkinen, T.; Simard, J.; Spurdle, A. B.; Beesley,
J.; Chen, X.; Kathleen Cuningham Foundation Consortium for Research
into Familial Breast Cancer; Neuhausen, S. L.; and 131 others:
Common variants in LSP1, 2q35 and 8q24 and breast cancer risk for
BRCA1 and BRCA2 mutation carriers. Hum. Molec. Genet. 18: 4442-4456,
2009.
2. Easton, D. F.; Pooley, K. A.; Dunning, A. M.; Pharoah, P. D. P.;
Thompson, D.; Ballinger, D. G.; Struewing, J. P.; Morrison, J.; Field,
H.; Luben, R.; Wareham, N.; Ahmed, S.; and 93 others: Genome-wide
association study identifies novel breast cancer susceptibility loci. Nature 447:
1087-1093, 2007.
3. Liu, L.; Cara, D. C.; Kaur, J.; Raharjo, E.; Mullaly, S. C.; Jongstra-Bilen,
J.; Jongstra, J.; Kubes, P.: LSP1 is an endothelial gatekeeper of
leukocyte transendothelial migration. J. Exp. Med. 201: 409-418,
2005.
4. May, W.; Korenberg, J. R.; Chen, X. N.; Lunsford, L.; Wood, W.
J.; Thompson, A.; Wall, R.; Denny, C. T.: Human lymphocyte-specific
pp52 gene is a member of a highly conserved dispersed family. Genomics 15:
515-520, 1993.
5. Thompson, A. A.; Omori, S. A.; Gilly, M. J.; May, W.; Gordon, M.
S.; Wood, W. J., Jr.; Miyoshi, E.; Malone, C. S.; Gimble, J.; Denny,
C. T.; Wall, R.: Alternatively spliced exons encode the tissue-specific
5-prime termini of leukocyte pp52 and stromal cell S37 mRNA isoforms. Genomics 32:
352-357, 1996.
*FIELD* CN
George E. Tiller - updated: 10/4/2010
Cassandra L. Kniffin - updated: 7/17/2007
Paul J. Converse - updated: 10/27/2006
Alan F. Scott - updated: 4/12/1996
*FIELD* CD
Victor A. McKusick: 3/19/1993
*FIELD* ED
alopez: 10/26/2010
terry: 10/4/2010
carol: 8/17/2007
ckniffin: 7/17/2007
carol: 6/20/2007
mgross: 10/27/2006
dkim: 9/11/1998
mark: 4/12/1996
terry: 4/12/1996
terry: 4/11/1996
mark: 4/10/1996
carol: 4/30/1993
carol: 3/19/1993
*RECORD*
*FIELD* NO
153432
*FIELD* TI
*153432 LYMPHOCYTE-SPECIFIC PROTEIN; LSP1
;;pp52
*FIELD* TX
CLONING
Signal transduction in B lymphocytes following antigen binding to a
read moremembrane-associated immunoglobulin complex initiates a diverse array of
intracellular events. To define genes participating in these events, May
et al. (1993) and others used various cDNA cloning strategies to
identify genes preferentially expressed in B lymphocytes. One gene,
variously named LSP1 and pp52, exhibited a number of properties
supporting a possible role in B-cell signaling pathways. The gene codes
for a 52-kD phosphoprotein expressed only in transformed and
untransformed B cells, thymocytes, and untransformed T-cell lines.
Thompson et al. (1996) showed that tissue-specific alternative splicing
produced 2 different Lsp1 transcripts in mouse. In lymphocytes, exon 1L
is used, while exon 1S is used in stromal cells. Both the 5-prime
untranslated regions and amino acid sequences of the alternative exons
are distinct and are, apparently, transcribed using different
tissue-specific promoters.
MAPPING
May et al. (1993) mapped the LSP1 gene to 11p15.5 by fluorescence in
situ hybridization. They unexpectedly found that the human pp52 gene is
1 of 4 closely related loci. Two of the 4 loci harbored dysfunctional
frameshift mutations or premature translation stop sites. These
hybridized to 1q12 and 2p11.2. They were unable to map the fourth gene.
May et al. (1993) pointed out that 11p15.5 is a location associated with
karyotypic abnormalities in certain B-cell malignancies.
MOLECULAR GENETICS
Easton et al. (2007) identified a T/C SNP (dbSNP rs3817198) in the LSP1
gene that was significantly (p = 3 x 10(-9)) associated with familial
breast cancer (114480) in a 3-stage genomewide association study of
22,848 cases from 22 studies. Easton et al. (2007) found that the allele
was common in the U.K. population and thus unlikely to confer increased
disease risk individually. However, in combination with other
susceptibility alleles, the SNP may become clinically significant.
In a study of 9,442 BRCA1 (113705) and 5,665 BRCA2 (600185) mutation
carriers from 33 study centers, Antoniou et al. (2009) found that the
minor allele (C) of the SNP dbSNP rs3817198 in LSP1 on chromosome
11p15.5 was associated with increased breast cancer risk only for BRCA2
mutation carriers (P trend = 2.8 x 10(-4)).
ANIMAL MODEL
Liu et al. (2005) noted that LSP1 is an intracellular Ca(2+)- and
F-actin (see 102610)-binding protein and a major substrate of MAPKAPK2
(602006) in the p38 MAPK (MAPK14; 600289) pathway. Using intravital
microscopy, they demonstrated that Lsp1 -/- mice had impaired neutrophil
extravasation in response to Tnf (191160), Il1b (147720), and Cxcl1
(155730), but no deficit in neutrophil rolling or adhesion.
Transplantation experiments showed that wildtype leukocytes had a
migration defect in Lsp1 -/- mice, whereas Lsp1 -/- neutrophils
extravasated normally in wildtype mice. Vascular permeability to
histamine was also reduced in Lsp1 -/- mice. Immunofluorescence
microscopy and Western blot analysis showed that Lsp1 was present in
wildtype but not Lsp1 -/- microvascular endothelial cells, and cultured
human endothelial cells also expressed LSP1. Liu et al. (2005) proposed
that LSP1 expressed in endothelium regulates neutrophil transendothelial
migration.
*FIELD* RF
1. Antoniou, A. C.; Sinilnikova, O. M.; McGuffog, L.; Healey, S.;
Nevanlinna, H.; Heikkinen, T.; Simard, J.; Spurdle, A. B.; Beesley,
J.; Chen, X.; Kathleen Cuningham Foundation Consortium for Research
into Familial Breast Cancer; Neuhausen, S. L.; and 131 others:
Common variants in LSP1, 2q35 and 8q24 and breast cancer risk for
BRCA1 and BRCA2 mutation carriers. Hum. Molec. Genet. 18: 4442-4456,
2009.
2. Easton, D. F.; Pooley, K. A.; Dunning, A. M.; Pharoah, P. D. P.;
Thompson, D.; Ballinger, D. G.; Struewing, J. P.; Morrison, J.; Field,
H.; Luben, R.; Wareham, N.; Ahmed, S.; and 93 others: Genome-wide
association study identifies novel breast cancer susceptibility loci. Nature 447:
1087-1093, 2007.
3. Liu, L.; Cara, D. C.; Kaur, J.; Raharjo, E.; Mullaly, S. C.; Jongstra-Bilen,
J.; Jongstra, J.; Kubes, P.: LSP1 is an endothelial gatekeeper of
leukocyte transendothelial migration. J. Exp. Med. 201: 409-418,
2005.
4. May, W.; Korenberg, J. R.; Chen, X. N.; Lunsford, L.; Wood, W.
J.; Thompson, A.; Wall, R.; Denny, C. T.: Human lymphocyte-specific
pp52 gene is a member of a highly conserved dispersed family. Genomics 15:
515-520, 1993.
5. Thompson, A. A.; Omori, S. A.; Gilly, M. J.; May, W.; Gordon, M.
S.; Wood, W. J., Jr.; Miyoshi, E.; Malone, C. S.; Gimble, J.; Denny,
C. T.; Wall, R.: Alternatively spliced exons encode the tissue-specific
5-prime termini of leukocyte pp52 and stromal cell S37 mRNA isoforms. Genomics 32:
352-357, 1996.
*FIELD* CN
George E. Tiller - updated: 10/4/2010
Cassandra L. Kniffin - updated: 7/17/2007
Paul J. Converse - updated: 10/27/2006
Alan F. Scott - updated: 4/12/1996
*FIELD* CD
Victor A. McKusick: 3/19/1993
*FIELD* ED
alopez: 10/26/2010
terry: 10/4/2010
carol: 8/17/2007
ckniffin: 7/17/2007
carol: 6/20/2007
mgross: 10/27/2006
dkim: 9/11/1998
mark: 4/12/1996
terry: 4/12/1996
terry: 4/11/1996
mark: 4/10/1996
carol: 4/30/1993
carol: 3/19/1993