SAAL1_HUMAN
ID SAAL1_HUMAN Reviewed; 474 AA.
AC Q96ER3; A6NH05;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein SAAL1;
DE AltName: Full=Synoviocyte proliferation-associated in collagen-induced arthritis protein 1 {ECO:0000303|PubMed:22127701};
DE Short=SPACIA1;
GN Name=SAAL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
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., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-387, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22127701; DOI=10.1002/art.30617;
RA Sato T., Fujii R., Konomi K., Yagishita N., Aratani S., Araya N., Aono H.,
RA Yudoh K., Suzuki N., Beppu M., Yamano Y., Nishioka K., Nakajima T.;
RT "Overexpression of SPACIA1/SAAL1, a newly identified gene that is involved
RT in synoviocyte proliferation, accelerates the progression of synovitis in
RT mice and humans.";
RL Arthritis Rheum. 63:3833-3842(2011).
RN [8]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Plays a role in promoting the proliferation of synovial
CC fibroblasts in response to pro-inflammatory stimuli.
CC {ECO:0000269|PubMed:22127701}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22127701}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and ovary, and to a
CC lesser extent in the lung, spleen and the heart (at protein level).
CC {ECO:0000269|PubMed:22127701}.
CC -!- SIMILARITY: Belongs to the SAAL1 family. {ECO:0000305}.
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DR EMBL; AC090099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68419.1; -; Genomic_DNA.
DR EMBL; BC012010; AAH12010.1; -; mRNA.
DR CCDS; CCDS31439.1; -.
DR RefSeq; NP_612430.2; NM_138421.2.
DR AlphaFoldDB; Q96ER3; -.
DR SMR; Q96ER3; -.
DR BioGRID; 125228; 207.
DR IntAct; Q96ER3; 34.
DR MINT; Q96ER3; -.
DR STRING; 9606.ENSP00000432487; -.
DR GlyGen; Q96ER3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96ER3; -.
DR PhosphoSitePlus; Q96ER3; -.
DR BioMuta; SAAL1; -.
DR DMDM; 209572677; -.
DR EPD; Q96ER3; -.
DR jPOST; Q96ER3; -.
DR MassIVE; Q96ER3; -.
DR MaxQB; Q96ER3; -.
DR PaxDb; Q96ER3; -.
DR PeptideAtlas; Q96ER3; -.
DR PRIDE; Q96ER3; -.
DR ProteomicsDB; 76442; -.
DR Antibodypedia; 42486; 123 antibodies from 23 providers.
DR CPTC; Q96ER3; 1 antibody.
DR DNASU; 113174; -.
DR Ensembl; ENST00000524803.6; ENSP00000432487.1; ENSG00000166788.10.
DR GeneID; 113174; -.
DR KEGG; hsa:113174; -.
DR MANE-Select; ENST00000524803.6; ENSP00000432487.1; NM_138421.3; NP_612430.2.
DR UCSC; uc001mnq.4; human.
DR CTD; 113174; -.
DR DisGeNET; 113174; -.
DR GeneCards; SAAL1; -.
DR HGNC; HGNC:25158; SAAL1.
DR HPA; ENSG00000166788; Low tissue specificity.
DR neXtProt; NX_Q96ER3; -.
DR OpenTargets; ENSG00000166788; -.
DR PharmGKB; PA142670959; -.
DR VEuPathDB; HostDB:ENSG00000166788; -.
DR eggNOG; ENOG502QS5W; Eukaryota.
DR GeneTree; ENSGT00390000004737; -.
DR InParanoid; Q96ER3; -.
DR OMA; CDVVCED; -.
DR OrthoDB; 1032139at2759; -.
DR PhylomeDB; Q96ER3; -.
DR TreeFam; TF323873; -.
DR PathwayCommons; Q96ER3; -.
DR SignaLink; Q96ER3; -.
DR SIGNOR; Q96ER3; -.
DR BioGRID-ORCS; 113174; 13 hits in 1087 CRISPR screens.
DR ChiTaRS; SAAL1; human.
DR GenomeRNAi; 113174; -.
DR Pharos; Q96ER3; Tdark.
DR PRO; PR:Q96ER3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96ER3; protein.
DR Bgee; ENSG00000166788; Expressed in ganglionic eminence and 131 other tissues.
DR ExpressionAtlas; Q96ER3; baseline and differential.
DR Genevisible; Q96ER3; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:1901647; P:positive regulation of synoviocyte proliferation; IMP:FlyBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..474
FT /note="Protein SAAL1"
FT /id="PRO_0000279540"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2C2"
FT MOD_RES 387
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VARIANT 315
FT /note="I -> V (in dbSNP:rs35525096)"
FT /id="VAR_053846"
FT VARIANT 426
FT /note="S -> G (in dbSNP:rs28930681)"
FT /id="VAR_053847"
FT CONFLICT 10
FT /note="P -> PP (in Ref. 3; AAH12010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 53558 MW; C206C80827F49681 CRC64;
MDRNPSPPPP GRDKEEEEEV AGGDCIGSTV YSKHWLFGVL SGLIQIVSPE NTKSSSDDEE
QLTELDEEME NEICRVWDMS MDEDVALFLQ EFNAPDIFMG VLAKSKCPRL REICVGILGN
MACFQEICVS ISSDKNLGQV LLHCLYDSDP PTLLETSRLL LTCLSQAEVA SVWVERIQEH
PAIYDSICFI MSSSTNVDLL VKVGEVVDKL FDLDEKLMLE WVRNGAAQPL DQPQEESEEQ
PVFRLVPCIL EAAKQVRSEN PEWLDVYMHI LQLLTTVDDG IQAIVHCPDT GKDIWNLLFD
LVCHEFCQSD DPPIILQEQK TVLASVFSVL SAIYASQTEQ EYLKIEKVDL PLIDSLIRVL
QNMEQCQKKP ENSAESNTEE TKRTDLTQDD FHLKILKDIL CEFLSNIFQA LTKETVAQGV
KEGQLSKQKC SSAFQNLLPF YSPVVEDFIK ILREVDKALA DDLEKNFPSL KVQT
