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Germinal center-associated signaling and motility protein (Germinal center B-cell-expressed transcript 2 protein) (Germinal center-associated lymphoma protein) (hGAL)

 GCSAM_HUMAN             Reviewed;         178 AA.
Q8N6F7; C9JD17; C9JUG6;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
22-NOV-2017, entry version 108.
RecName: Full=Germinal center-associated signaling and motility protein;
AltName: Full=Germinal center B-cell-expressed transcript 2 protein;
AltName: Full=Germinal center-associated lymphoma protein;
Short=hGAL;
Name=GCSAM; Synonyms=GAL, GCET2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=12819018; DOI=10.1016/S0002-9440(10)63637-1;
Pan Z., Shen Y., Du C., Zhou G., Rosenwald A., Staudt L.M.,
Greiner T.C., McKeithan T.W., Chan W.C.;
"Two newly characterized germinal center B-cell-associated genes,
GCET1 and GCET2, have differential expression in normal and neoplastic
B cells.";
Am. J. Pathol. 163:135-144(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND TISSUE
SPECIFICITY.
PubMed=12509382; DOI=10.1182/blood-2002-06-1931;
Lossos I.S., Alizadeh A.A., Rajapaksa R., Tibshirani R., Levy R.;
"HGAL is a novel interleukin-4-inducible gene that strongly predicts
survival in diffuse large B-cell lymphoma.";
Blood 101:433-440(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lymphoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15677569; DOI=10.1182/blood-2004-08-3112;
Natkunam Y., Lossos I.S., Taidi B., Zhao S., Lu X., Ding F.,
Hammer A.S., Marafioti T., Byrne G.E. Jr., Levy S., Warnke R.A.,
Levy R.;
"Expression of the human germinal center-associated lymphoma (HGAL)
protein, a new marker of germinal center B-cell derivation.";
Blood 105:3979-3986(2005).
[6]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYH2 AND ACTB,
PHOSPHORYLATION BY LYN, AND MUTAGENESIS OF TYR-128 AND TYR-148.
PubMed=17823310; DOI=10.1182/blood-2007-04-087775;
Lu X., Chen J., Malumbres R., Cubedo Gil E., Helfman D.M.,
Lossos I.S.;
"HGAL, a lymphoma prognostic biomarker, interacts with the
cytoskeleton and mediates the effects of IL-6 on cell migration.";
Blood 110:4268-4277(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-148, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARHGEF11 AND
ARHGEF12.
PubMed=20844236; DOI=10.1182/blood-2010-04-281568;
Jiang X., Lu X., McNamara G., Liu X., Cubedo E., Sarosiek K.A.,
Sanchez-Garcia I., Helfman D.M., Lossos I.S.;
"HGAL, a germinal center specific protein, decreases lymphoma cell
motility by modulation of the RhoA signaling pathway.";
Blood 116:5217-5227(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
FUNCTION AS REGULATOR OF B-CELL RECEPTOR SIGNALING, INTERACTION WITH
SYK, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 106-TYR-TYR-107; TYR-128
AND TYR-148.
PubMed=23299888; DOI=10.1038/ncomms2334;
Romero-Camarero I., Jiang X., Natkunam Y., Lu X., Vicente-Duenas C.,
Gonzalez-Herrero I., Flores T., Garcia J.L., McNamara G., Kunder C.,
Zhao S., Segura V., Fontan L., Martinez-Climent J.A.,
Garcia-Criado F.J., Theis J.D., Dogan A., Campos-Sanchez E.,
Green M.R., Alizadeh A.A., Cobaleda C., Sanchez-Garcia I.,
Lossos I.S.;
"Germinal centre protein HGAL promotes lymphoid hyperplasia and
amyloidosis via BCR-mediated Syk activation.";
Nat. Commun. 4:1338-1338(2013).
-!- FUNCTION: Involved in the negative regulation of lymphocyte
motility. It mediates the migration-inhibitory effects of IL6.
Serves as a positive regulator of the RhoA signaling pathway.
Enhancement of RhoA activation results in inhibition of lymphocyte
and lymphoma cell motility by activation of its downstream
effector ROCK. Is a regulator of B-cell receptor signaling, that
acts through SYK kinase activation. {ECO:0000269|PubMed:17823310,
ECO:0000269|PubMed:20844236, ECO:0000269|PubMed:23299888}.
-!- SUBUNIT: Interacts with ACTB and MYH2; the interaction with MYH2
is increased by IL6-induced phosphorylation. Interacts (via C-
terminus) with ARHGEF11 (via DH domain). Interacts with ARHGEF12.
Interacts with SYK; the interaction increases after B-cell
receptor stimulation, resulting in enhanced SYK
autophosphorylation and activity. {ECO:0000269|PubMed:17823310,
ECO:0000269|PubMed:20844236, ECO:0000269|PubMed:23299888}.
-!- INTERACTION:
Q92624:APPBP2; NbExp=5; IntAct=EBI-10267082, EBI-743771;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=It
relocalizes from the cytoplasm to podosome-like structures upon
cell treatment with IL6.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8N6F7-1; Sequence=Displayed;
Name=2;
IsoId=Q8N6F7-2; Sequence=VSP_046085;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8N6F7-3; Sequence=VSP_046984;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Expressed in diffuse large B-cell lymphoma
(DLBCL) and several germinal center (GC)-like lymphoma cell lines
(at protein level). Highly expressed in normal GC lymphocytes and
GC-derived malignancies. Expressed in thymus and spleen.
{ECO:0000269|PubMed:12509382, ECO:0000269|PubMed:12819018,
ECO:0000269|PubMed:15677569}.
-!- INDUCTION: Up-regulated by IL4/interleukin-4.
{ECO:0000269|PubMed:12509382}.
-!- PTM: Phosphorylation on tyrosine residues can be induced by IL6.
Phosphorylation is mediated by LYN. {ECO:0000269|PubMed:17823310}.
-----------------------------------------------------------------------
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EMBL; AY212246; AAO22147.1; -; mRNA.
EMBL; AF521911; AAO21701.1; -; mRNA.
EMBL; AC128688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030506; AAH30506.1; -; mRNA.
EMBL; BM456595; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS2964.1; -. [Q8N6F7-1]
CCDS; CCDS54621.1; -. [Q8N6F7-3]
CCDS; CCDS54622.1; -. [Q8N6F7-2]
RefSeq; NP_001177188.1; NM_001190259.1. [Q8N6F7-2]
RefSeq; NP_001177189.1; NM_001190260.1. [Q8N6F7-3]
RefSeq; NP_689998.1; NM_152785.4. [Q8N6F7-1]
UniGene; Hs.49614; -.
ProteinModelPortal; Q8N6F7; -.
BioGrid; 129200; 1.
IntAct; Q8N6F7; 3.
STRING; 9606.ENSP00000419485; -.
iPTMnet; Q8N6F7; -.
PhosphoSitePlus; Q8N6F7; -.
SwissPalm; Q8N6F7; -.
BioMuta; GCSAM; -.
MaxQB; Q8N6F7; -.
PaxDb; Q8N6F7; -.
PeptideAtlas; Q8N6F7; -.
PRIDE; Q8N6F7; -.
DNASU; 257144; -.
Ensembl; ENST00000308910; ENSP00000309487; ENSG00000174500. [Q8N6F7-1]
Ensembl; ENST00000460387; ENSP00000420603; ENSG00000174500. [Q8N6F7-3]
Ensembl; ENST00000484193; ENSP00000419485; ENSG00000174500. [Q8N6F7-2]
GeneID; 257144; -.
KEGG; hsa:257144; -.
UCSC; uc003dys.2; human. [Q8N6F7-1]
CTD; 257144; -.
DisGeNET; 257144; -.
EuPathDB; HostDB:ENSG00000174500.12; -.
GeneCards; GCSAM; -.
HGNC; HGNC:20253; GCSAM.
HPA; HPA002473; -.
MIM; 607792; gene.
neXtProt; NX_Q8N6F7; -.
OpenTargets; ENSG00000174500; -.
PharmGKB; PA134980592; -.
eggNOG; ENOG410JBYS; Eukaryota.
eggNOG; ENOG41115IK; LUCA.
GeneTree; ENSGT00730000111441; -.
HOGENOM; HOG000293224; -.
HOVERGEN; HBG081549; -.
InParanoid; Q8N6F7; -.
OMA; EGCFCLP; -.
OrthoDB; EOG091G0O8J; -.
PhylomeDB; Q8N6F7; -.
TreeFam; TF338596; -.
GenomeRNAi; 257144; -.
PRO; PR:Q8N6F7; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000174500; -.
CleanEx; HS_GAL; -.
CleanEx; HS_GCET2; -.
ExpressionAtlas; Q8N6F7; baseline and differential.
Genevisible; Q8N6F7; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IPI:UniProtKB.
GO; GO:0045159; F:myosin II binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:2000402; P:negative regulation of lymphocyte migration; IMP:UniProtKB.
GO; GO:0050855; P:regulation of B cell receptor signaling pathway; IMP:UniProtKB.
InterPro; IPR031364; GC_assoc_lym.
PANTHER; PTHR35351; PTHR35351; 1.
Pfam; PF15666; HGAL; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Membrane; Phosphoprotein; Reference proteome.
CHAIN 1 178 Germinal center-associated signaling and
motility protein.
/FTId=PRO_0000256228.
MOD_RES 99 99 Phosphoserine.
{ECO:0000250|UniProtKB:Q6RFH4}.
MOD_RES 148 148 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
VAR_SEQ 9 9 N -> NSF (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046085.
VAR_SEQ 34 48 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_046984.
MUTAGEN 106 107 YY->AA: Does not affect the interaction
with SYK. {ECO:0000269|PubMed:23299888}.
MUTAGEN 128 128 Y->F: Does not affect IL6 induced
phosphorylation. Does not affect the
interaction with SYK.
{ECO:0000269|PubMed:17823310,
ECO:0000269|PubMed:23299888}.
MUTAGEN 148 148 Y->F: Prevents IL6 induced
phosphorylation. Does not affect the
interaction with SYK.
{ECO:0000269|PubMed:17823310,
ECO:0000269|PubMed:23299888}.
SEQUENCE 178 AA; 21005 MW; B7C91F3D4B78CD03 CRC64;
MGNSLLRENR RQQNTQEMPW NVRMQSPKQR TSRCWDHHIA EGCFCLPWKK ILIFEKRQDS
QNENERMSST PIQDNVDQTY SEELCYTLIN HRVLCTRPSG NSAEEYYENV PCKAERPRES
LGGTETEYSL LHMPSTDPRH ARSPEDEYEL LMPHRISSHF LQQPRPLMAP SETQFSHL


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