SOSSC_HUMAN
ID SOSSC_HUMAN Reviewed; 104 AA.
AC Q9NRY2; Q5VWJ7; Q96E04; Q9P090;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=SOSS complex subunit C;
DE AltName: Full=INTS3- and NABP-interacting protein;
DE AltName: Full=Sensor of single-strand DNA complex subunit C;
DE AltName: Full=Sensor of ssDNA subunit C;
DE Short=SOSS-C;
DE AltName: Full=Single-stranded DNA-binding protein-interacting protein 1;
DE Short=SSB-interacting protein 1;
DE Short=hSSBIP1;
GN Name=INIP; Synonyms=C9orf80, SSBIP1; ORFNames=HSPC043, HSPC291;
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 MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix, Lymph, and Uterus;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SOSS COMPLEX.
RX PubMed=19605351; DOI=10.1074/jbc.c109.039586;
RA Li Y., Bolderson E., Kumar R., Muniandy P.A., Xue Y., Richard D.J.,
RA Seidman M., Pandita T.K., Khanna K.K., Wang W.;
RT "hSSB1 and hSSB2 form similar multiprotein complexes that participate in
RT DNA damage response.";
RL J. Biol. Chem. 284:23525-23531(2009).
RN [6]
RP FUNCTION IN THE SOSS COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION IN THE
RP SOSS COMPLEX, AND INTERACTION WITH INTS3.
RX PubMed=19683501; DOI=10.1016/j.molcel.2009.06.011;
RA Huang J., Gong Z., Ghosal G., Chen J.;
RT "SOSS complexes participate in the maintenance of genomic stability.";
RL Mol. Cell 35:384-393(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP 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: Component of the SOSS complex, a multiprotein complex that
CC functions downstream of the MRN complex to promote DNA repair and G2/M
CC checkpoint. The SOSS complex associates with single-stranded DNA at DNA
CC lesions and influences diverse endpoints in the cellular DNA damage
CC response including cell-cycle checkpoint activation, recombinational
CC repair and maintenance of genomic stability. Required for efficient
CC homologous recombination-dependent repair of double-strand breaks
CC (DSBs) and ATM-dependent signaling pathways.
CC {ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.
CC -!- SUBUNIT: Component of the SOSS complex, composed of SOSS-B (SOSS-
CC B1/NABP2 or SOSS-B2/NABP1), SOSS-A/INTS3 and SOSS-C/INIP. SOSS
CC complexes containing SOSS-B1/NABP2 are more abundant than complexes
CC containing SOSS-B2/NABP1. Interacts with INTS3; the interaction is
CC direct. {ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.
CC -!- INTERACTION:
CC Q9NRY2; Q03989: ARID5A; NbExp=3; IntAct=EBI-2881520, EBI-948603;
CC Q9NRY2; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-2881520, EBI-953896;
CC Q9NRY2; Q14129: DGCR6; NbExp=5; IntAct=EBI-2881520, EBI-12206931;
CC Q9NRY2; Q9BY27: DGCR6L; NbExp=6; IntAct=EBI-2881520, EBI-742953;
CC Q9NRY2; Q68E01: INTS3; NbExp=6; IntAct=EBI-2881520, EBI-2680854;
CC Q9NRY2; O76011: KRT34; NbExp=3; IntAct=EBI-2881520, EBI-1047093;
CC Q9NRY2; Q93062: RBPMS; NbExp=4; IntAct=EBI-2881520, EBI-740322;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19605351,
CC ECO:0000269|PubMed:19683501}. Note=Localizes to nuclear foci following
CC DNA damage.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRY2-2; Sequence=VSP_023423, VSP_023424;
CC -!- SIMILARITY: Belongs to the SOSS-C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28969.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH13097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF161409; AAF28969.1; ALT_INIT; mRNA.
DR EMBL; AF161411; AAF28971.2; -; mRNA.
DR EMBL; AL390067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013097; AAH13097.1; ALT_INIT; mRNA.
DR EMBL; BC014881; AAH14881.1; -; mRNA.
DR EMBL; BC065210; AAH65210.1; -; mRNA.
DR CCDS; CCDS6785.1; -. [Q9NRY2-1]
DR RefSeq; NP_067041.1; NM_021218.2. [Q9NRY2-1]
DR PDB; 4OWT; X-ray; 2.00 A; C=1-104.
DR PDB; 4OWW; X-ray; 2.30 A; C=1-104.
DR PDBsum; 4OWT; -.
DR PDBsum; 4OWW; -.
DR AlphaFoldDB; Q9NRY2; -.
DR SMR; Q9NRY2; -.
DR BioGRID; 121823; 23.
DR ComplexPortal; CPX-482; SOSS1 complex.
DR ComplexPortal; CPX-614; SOSS2 complex.
DR IntAct; Q9NRY2; 17.
DR MINT; Q9NRY2; -.
DR STRING; 9606.ENSP00000363360; -.
DR iPTMnet; Q9NRY2; -.
DR PhosphoSitePlus; Q9NRY2; -.
DR BioMuta; INIP; -.
DR EPD; Q9NRY2; -.
DR jPOST; Q9NRY2; -.
DR MassIVE; Q9NRY2; -.
DR MaxQB; Q9NRY2; -.
DR PaxDb; Q9NRY2; -.
DR PeptideAtlas; Q9NRY2; -.
DR PRIDE; Q9NRY2; -.
DR ProteomicsDB; 82439; -. [Q9NRY2-1]
DR ProteomicsDB; 82440; -. [Q9NRY2-2]
DR Antibodypedia; 15240; 44 antibodies from 10 providers.
DR DNASU; 58493; -.
DR Ensembl; ENST00000374242.9; ENSP00000363360.3; ENSG00000148153.14. [Q9NRY2-1]
DR GeneID; 58493; -.
DR KEGG; hsa:58493; -.
DR MANE-Select; ENST00000374242.9; ENSP00000363360.3; NM_021218.3; NP_067041.1.
DR UCSC; uc004bgg.4; human. [Q9NRY2-1]
DR CTD; 58493; -.
DR DisGeNET; 58493; -.
DR GeneCards; INIP; -.
DR HGNC; HGNC:24994; INIP.
DR HPA; ENSG00000148153; Low tissue specificity.
DR MIM; 613273; gene.
DR neXtProt; NX_Q9NRY2; -.
DR OpenTargets; ENSG00000148153; -.
DR PharmGKB; PA134992982; -.
DR VEuPathDB; HostDB:ENSG00000148153; -.
DR eggNOG; ENOG502S23S; Eukaryota.
DR GeneTree; ENSGT00390000006366; -.
DR InParanoid; Q9NRY2; -.
DR OMA; DCKVLTN; -.
DR OrthoDB; 1596201at2759; -.
DR PhylomeDB; Q9NRY2; -.
DR TreeFam; TF328613; -.
DR PathwayCommons; Q9NRY2; -.
DR SignaLink; Q9NRY2; -.
DR BioGRID-ORCS; 58493; 17 hits in 1056 CRISPR screens.
DR ChiTaRS; INIP; human.
DR GenomeRNAi; 58493; -.
DR Pharos; Q9NRY2; Tbio.
DR PRO; PR:Q9NRY2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NRY2; protein.
DR Bgee; ENSG00000148153; Expressed in ileal mucosa and 192 other tissues.
DR ExpressionAtlas; Q9NRY2; baseline and differential.
DR Genevisible; Q9NRY2; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0070876; C:SOSS complex; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IDA:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR DisProt; DP01943; -.
DR InterPro; IPR031821; SOSSC.
DR PANTHER; PTHR31526; PTHR31526; 1.
DR Pfam; PF15925; SOSSC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; DNA damage; DNA repair;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..104
FT /note="SOSS complex subunit C"
FT /id="PRO_0000279419"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 43..44
FT /note="SI -> RY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023423"
FT VAR_SEQ 45..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023424"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:4OWT"
SQ SEQUENCE 104 AA; 11425 MW; 87B2467920C58C1E CRC64;
MAANSSGQGF QNKNRVAILA ELDKEKRKLL MQNQSSTNHP GASIALSRPS LNKDFRDHAE
QQHIAAQQKA ALQHAHAHSS GYFITQDSAF GNLILPVLPR LDPE
