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Protein

SOSS complex subunit C

Gene

INIP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways.2 Publications

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: UniProtKB
  • response to ionizing radiation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
SOSS complex subunit C
Alternative name(s):
INTS3- and NABP-interacting protein
Sensor of single-strand DNA complex subunit C
Sensor of ssDNA subunit C
Short name:
SOSS-C
Single-stranded DNA-binding protein-interacting protein 1
Short name:
SSB-interacting protein 1
Short name:
hSSBIP1
Gene namesi
Name:INIP
Synonyms:C9orf80, SSBIP1
ORF Names:HSPC043, HSPC291
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:24994. INIP.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • SOSS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134992982.

Polymorphism and mutation databases

BioMutaiINIP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 104103SOSS complex subunit CPRO_0000279419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei50 – 501PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NRY2.
MaxQBiQ9NRY2.
PaxDbiQ9NRY2.
PeptideAtlasiQ9NRY2.
PRIDEiQ9NRY2.

PTM databases

iPTMnetiQ9NRY2.
PhosphoSiteiQ9NRY2.

Expressioni

Gene expression databases

BgeeiQ9NRY2.
CleanExiHS_C9orf80.
ExpressionAtlasiQ9NRY2. baseline and differential.
GenevisibleiQ9NRY2. HS.

Organism-specific databases

HPAiHPA020382.

Interactioni

Subunit structurei

Component of the SOSS complex, composed of SOSS-B (SOSS-B1/NABP2 or SOSS-B2/NABP1), SOSS-A/INTS3 and SOSS-C/INIP. SOSS complexes containing SOSS-B1/NABP2 are more abundant than complexes containing SOSS-B2/NABP1. Interacts with INTS3; the interaction is direct.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RBPMSQ930623EBI-2881520,EBI-740322

Protein-protein interaction databases

BioGridi121823. 12 interactions.
IntActiQ9NRY2. 5 interactions.
STRINGi9606.ENSP00000363360.

Structurei

Secondary structure

1
104
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 7814Combined sources
Beta strandi83 – 853Combined sources
Beta strandi89 – 913Combined sources
Beta strandi93 – 964Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OWTX-ray2.00C1-104[»]
4OWWX-ray2.30C1-104[»]
ProteinModelPortaliQ9NRY2.
SMRiQ9NRY2. Positions 63-101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SOSS-C family.Curated

Phylogenomic databases

eggNOGiENOG410IXVU. Eukaryota.
ENOG4111QHU. LUCA.
GeneTreeiENSGT00390000006366.
HOGENOMiHOG000007001.
InParanoidiQ9NRY2.
OMAiANPPGQG.
OrthoDBiEOG7966KB.
PhylomeDBiQ9NRY2.
TreeFamiTF328613.

Family and domain databases

InterProiIPR031821. SOSSC.
[Graphical view]
PfamiPF15925. SOSSC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NRY2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAANSSGQGF QNKNRVAILA ELDKEKRKLL MQNQSSTNHP GASIALSRPS
60 70 80 90 100
LNKDFRDHAE QQHIAAQQKA ALQHAHAHSS GYFITQDSAF GNLILPVLPR

LDPE
Length:104
Mass (Da):11,425
Last modified:October 1, 2000 - v1
Checksum:i87B2467920C58C1E
GO
Isoform 2 (identifier: Q9NRY2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-44: SI → RY
     45-104: Missing.

Note: No experimental confirmation available.
Show »
Length:44
Mass (Da):4,904
Checksum:i1C28B5D5743145D1
GO

Sequence cautioni

The sequence AAF28969.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH13097.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAH71934.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei43 – 442SI → RY in isoform 2. 1 PublicationVSP_023423
Alternative sequencei45 – 10460Missing in isoform 2. 1 PublicationVSP_023424Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161409 mRNA. Translation: AAF28969.1. Different initiation.
AF161411 mRNA. Translation: AAF28971.2.
AL390067 Genomic DNA. Translation: CAH71934.1. Sequence problems.
AL390067 Genomic DNA. Translation: CAH71936.1.
BC013097 mRNA. Translation: AAH13097.1. Different initiation.
BC014881 mRNA. Translation: AAH14881.1.
BC065210 mRNA. Translation: AAH65210.1.
CCDSiCCDS6785.1. [Q9NRY2-1]
RefSeqiNP_067041.1. NM_021218.1. [Q9NRY2-1]
UniGeneiHs.658575.

Genome annotation databases

EnsembliENST00000374242; ENSP00000363360; ENSG00000148153. [Q9NRY2-1]
GeneIDi58493.
KEGGihsa:58493.
UCSCiuc004bgg.4. human. [Q9NRY2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161409 mRNA. Translation: AAF28969.1. Different initiation.
AF161411 mRNA. Translation: AAF28971.2.
AL390067 Genomic DNA. Translation: CAH71934.1. Sequence problems.
AL390067 Genomic DNA. Translation: CAH71936.1.
BC013097 mRNA. Translation: AAH13097.1. Different initiation.
BC014881 mRNA. Translation: AAH14881.1.
BC065210 mRNA. Translation: AAH65210.1.
CCDSiCCDS6785.1. [Q9NRY2-1]
RefSeqiNP_067041.1. NM_021218.1. [Q9NRY2-1]
UniGeneiHs.658575.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OWTX-ray2.00C1-104[»]
4OWWX-ray2.30C1-104[»]
ProteinModelPortaliQ9NRY2.
SMRiQ9NRY2. Positions 63-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121823. 12 interactions.
IntActiQ9NRY2. 5 interactions.
STRINGi9606.ENSP00000363360.

PTM databases

iPTMnetiQ9NRY2.
PhosphoSiteiQ9NRY2.

Polymorphism and mutation databases

BioMutaiINIP.

Proteomic databases

EPDiQ9NRY2.
MaxQBiQ9NRY2.
PaxDbiQ9NRY2.
PeptideAtlasiQ9NRY2.
PRIDEiQ9NRY2.

Protocols and materials databases

DNASUi58493.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374242; ENSP00000363360; ENSG00000148153. [Q9NRY2-1]
GeneIDi58493.
KEGGihsa:58493.
UCSCiuc004bgg.4. human. [Q9NRY2-1]

Organism-specific databases

CTDi58493.
GeneCardsiINIP.
HGNCiHGNC:24994. INIP.
HPAiHPA020382.
MIMi613273. gene.
neXtProtiNX_Q9NRY2.
PharmGKBiPA134992982.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IXVU. Eukaryota.
ENOG4111QHU. LUCA.
GeneTreeiENSGT00390000006366.
HOGENOMiHOG000007001.
InParanoidiQ9NRY2.
OMAiANPPGQG.
OrthoDBiEOG7966KB.
PhylomeDBiQ9NRY2.
TreeFamiTF328613.

Miscellaneous databases

GenomeRNAii58493.
PROiQ9NRY2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRY2.
CleanExiHS_C9orf80.
ExpressionAtlasiQ9NRY2. baseline and differential.
GenevisibleiQ9NRY2. HS.

Family and domain databases

InterProiIPR031821. SOSSC.
[Graphical view]
PfamiPF15925. SOSSC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Cervix, Lymph and Uterus.
  4. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "hSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response."
    Li Y., Bolderson E., Kumar R., Muniandy P.A., Xue Y., Richard D.J., Seidman M., Pandita T.K., Khanna K.K., Wang W.
    J. Biol. Chem. 284:23525-23531(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SOSS COMPLEX.
  6. "SOSS complexes participate in the maintenance of genomic stability."
    Huang J., Gong Z., Ghosal G., Chen J.
    Mol. Cell 35:384-393(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE SOSS COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SOSS COMPLEX, INTERACTION WITH INTS3.
  7. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.

Entry informationi

Entry nameiSOSSC_HUMAN
AccessioniPrimary (citable) accession number: Q9NRY2
Secondary accession number(s): Q5VWJ7, Q96E04, Q9P090
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.