Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q96AH0

- SOSB2_HUMAN

UniProt

Q96AH0 - SOSB2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

SOSS complex subunit B2

Gene

NABP1

Organism
Homo sapiens (Human)
Status
Reviewed - 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. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with 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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi26 – 9974OBAdd
BLAST

GO - Molecular functioni

  1. RNA binding Source: Ensembl
  2. single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. DNA repair Source: UniProtKB
  3. double-strand break repair via homologous recombination Source: UniProtKB
  4. mitotic cell cycle checkpoint Source: UniProtKB
  5. response to ionizing radiation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
SOSS complex subunit B2
Alternative name(s):
Nucleic acid-binding protein 1
Oligonucleotide/oligosaccharide-binding fold-containing protein 2A
Sensor of single-strand DNA complex subunit B2
Sensor of ssDNA subunit B2
Short name:
SOSS-B2
Single-stranded DNA-binding protein 2
Short name:
hSSB2
Gene namesi
Name:NABP1
Synonyms:OBFC2A, SSB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:26232. NABP1.

Subcellular locationi

Nucleus 2 Publications
Note: Localizes to nuclear foci following DNA damage.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: UniProtKB
  3. SOSS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti520. Acute promyelocytic leukemia.
PharmGKBiPA143485566.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204SOSS complex subunit B2PRO_0000333954Add
BLAST

Proteomic databases

MaxQBiQ96AH0.
PaxDbiQ96AH0.
PRIDEiQ96AH0.

Expressioni

Gene expression databases

BgeeiQ96AH0.
CleanExiHS_OBFC2A.
ExpressionAtlasiQ96AH0. baseline and differential.
GenevestigatoriQ96AH0.

Organism-specific databases

HPAiHPA054978.

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/NABP1.2 Publications

Protein-protein interaction databases

BioGridi122332. 5 interactions.
STRINGi9606.ENSP00000403683.

Structurei

3D structure databases

ProteinModelPortaliQ96AH0.
SMRiQ96AH0. Positions 10-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SOSS-B family. SOSS-B2 subfamily.Curated
Contains 1 OB DNA-binding domain.Curated

Phylogenomic databases

eggNOGiNOG285523.
GeneTreeiENSGT00390000001913.
HOGENOMiHOG000006622.
InParanoidiQ96AH0.
OMAiSASARFY.
PhylomeDBiQ96AH0.
TreeFamiTF313902.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PfamiPF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96AH0-1) [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
MNRVNDPLIF IRDIKPGLKN LNVVFIVLEI GRVTKTKDGH EVRSCKVADK
60 70 80 90 100
TGSITISVWD EIGGLIQPGD IIRLTRGYAS MWKGCLTLYT GRGGELQKIG
110 120 130 140 150
EFCMVYSEVP NFSEPNPDYR GQQNKGAQSE QKNNSMNSNM GTGTFGPVGN
160 170 180 190 200
GVHTGPESRE HQFSHAGRSN GRGLINPQLQ GTASNQTVMT TISNGRDPRR

AFKR
Length:204
Mass (Da):22,423
Last modified:December 1, 2001 - v1
Checksum:iEF7579A452381E47
GO
Isoform 2 (identifier: Q96AH0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: Missing.

Show »
Length:124
Mass (Da):13,579
Checksum:i285E087256426CAC
GO
Isoform 3 (identifier: Q96AH0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-134: EFCMVYSEVPNFSEPNPDYRGQQNKGAQSEQKNN → DLGAVQAAAMRDSIHYYPGNDLHPDLEEPSSLGV
     135-204: Missing.

Show »
Length:134
Mass (Da):14,677
Checksum:i9243CCF90A5E06E2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541T → S.
Corresponds to variant rs12612256 [ dbSNP | Ensembl ].
VAR_043340

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8080Missing in isoform 2. 2 PublicationsVSP_033600Add
BLAST
Alternative sequencei101 – 13434EFCMV…EQKNN → DLGAVQAAAMRDSIHYYPGN DLHPDLEEPSSLGV in isoform 3. 1 PublicationVSP_033601Add
BLAST
Alternative sequencei135 – 20470Missing in isoform 3. 1 PublicationVSP_033602Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026486 mRNA. Translation: BAB15491.1.
AL832659 mRNA. Translation: CAH56209.1.
AC114778 Genomic DNA. Translation: AAY24348.1.
CH471058 Genomic DNA. Translation: EAX10836.1.
CH471058 Genomic DNA. Translation: EAX10837.1.
CH471058 Genomic DNA. Translation: EAX10838.1.
BC017114 mRNA. Translation: AAH17114.1.
BC107723 mRNA. Translation: AAI07724.1.
CCDSiCCDS33352.1. [Q96AH0-1]
CCDS58745.1. [Q96AH0-2]
RefSeqiNP_001026886.1. NM_001031716.2. [Q96AH0-1]
NP_001241665.1. NM_001254736.1. [Q96AH0-2]
UniGeneiHs.591610.

Genome annotation databases

EnsembliENST00000307849; ENSP00000307968; ENSG00000173559. [Q96AH0-3]
ENST00000409510; ENSP00000386605; ENSG00000173559. [Q96AH0-2]
ENST00000410026; ENSP00000387243; ENSG00000173559. [Q96AH0-2]
ENST00000425611; ENSP00000403683; ENSG00000173559. [Q96AH0-1]
ENST00000451500; ENSP00000390901; ENSG00000173559. [Q96AH0-3]
GeneIDi64859.
KEGGihsa:64859.
UCSCiuc002usw.3. human. [Q96AH0-1]
uc021vug.1. human. [Q96AH0-2]

Polymorphism databases

DMDMi74760705.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026486 mRNA. Translation: BAB15491.1 .
AL832659 mRNA. Translation: CAH56209.1 .
AC114778 Genomic DNA. Translation: AAY24348.1 .
CH471058 Genomic DNA. Translation: EAX10836.1 .
CH471058 Genomic DNA. Translation: EAX10837.1 .
CH471058 Genomic DNA. Translation: EAX10838.1 .
BC017114 mRNA. Translation: AAH17114.1 .
BC107723 mRNA. Translation: AAI07724.1 .
CCDSi CCDS33352.1. [Q96AH0-1 ]
CCDS58745.1. [Q96AH0-2 ]
RefSeqi NP_001026886.1. NM_001031716.2. [Q96AH0-1 ]
NP_001241665.1. NM_001254736.1. [Q96AH0-2 ]
UniGenei Hs.591610.

3D structure databases

ProteinModelPortali Q96AH0.
SMRi Q96AH0. Positions 10-115.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122332. 5 interactions.
STRINGi 9606.ENSP00000403683.

Polymorphism databases

DMDMi 74760705.

Proteomic databases

MaxQBi Q96AH0.
PaxDbi Q96AH0.
PRIDEi Q96AH0.

Protocols and materials databases

DNASUi 64859.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307849 ; ENSP00000307968 ; ENSG00000173559 . [Q96AH0-3 ]
ENST00000409510 ; ENSP00000386605 ; ENSG00000173559 . [Q96AH0-2 ]
ENST00000410026 ; ENSP00000387243 ; ENSG00000173559 . [Q96AH0-2 ]
ENST00000425611 ; ENSP00000403683 ; ENSG00000173559 . [Q96AH0-1 ]
ENST00000451500 ; ENSP00000390901 ; ENSG00000173559 . [Q96AH0-3 ]
GeneIDi 64859.
KEGGi hsa:64859.
UCSCi uc002usw.3. human. [Q96AH0-1 ]
uc021vug.1. human. [Q96AH0-2 ]

Organism-specific databases

CTDi 64859.
GeneCardsi GC02P192543.
H-InvDB HIX0002686.
HGNCi HGNC:26232. NABP1.
HPAi HPA054978.
MIMi 612103. gene.
neXtProti NX_Q96AH0.
Orphaneti 520. Acute promyelocytic leukemia.
PharmGKBi PA143485566.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG285523.
GeneTreei ENSGT00390000001913.
HOGENOMi HOG000006622.
InParanoidi Q96AH0.
OMAi SASARFY.
PhylomeDBi Q96AH0.
TreeFami TF313902.

Miscellaneous databases

GenomeRNAii 64859.
NextBioi 67011.
PROi Q96AH0.
SOURCEi Search...

Gene expression databases

Bgeei Q96AH0.
CleanExi HS_OBFC2A.
ExpressionAtlasi Q96AH0. baseline and differential.
Genevestigatori Q96AH0.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
InterProi IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view ]
Pfami PF01336. tRNA_anti-codon. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Ileal mucosa.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Bone marrow.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Uterus.
  6. "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.
  7. "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.

Entry informationi

Entry nameiSOSB2_HUMAN
AccessioniPrimary (citable) accession number: Q96AH0
Secondary accession number(s): Q658Y8, Q9H5X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 1, 2001
Last modified: October 29, 2014
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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3