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Protein

Integrator complex subunit 3

Gene

INTS3

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

Functioni

Component of the Integrator complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.
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. The SOSS complex is required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. In the SOSS complex, it is required for the assembly of the complex and for stabilization of the complex at DNA damage sites.

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: UniProtKB
  • mitotic cell cycle checkpoint Source: UniProtKB
  • response to ionizing radiation Source: UniProtKB
  • snRNA processing Source: HGNC
  • snRNA transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiR-HSA-6807505. RNA polymerase II transcribes snRNA genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrator complex subunit 3
Short name:
Int3
Alternative name(s):
SOSS complex subunit A
Sensor of single-strand DNA complex subunit A
Short name:
SOSS-A
Short name:
Sensor of ssDNA subunit A
Gene namesi
Name:INTS3
Synonyms:C1orf193, C1orf60
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:26153. INTS3.

Subcellular locationi

GO - Cellular componenti

  • integrator complex Source: HGNC
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • SOSS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672510.

Polymorphism and mutation databases

BioMutaiINTS3.
DMDMi74724494.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10431043Integrator complex subunit 3PRO_0000259534Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei502 – 5021PhosphoserineCombined sources
Modified residuei537 – 5371PhosphoserineCombined sources
Modified residuei995 – 9951PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ68E01.
MaxQBiQ68E01.
PaxDbiQ68E01.
PRIDEiQ68E01.

PTM databases

iPTMnetiQ68E01.
PhosphoSiteiQ68E01.

Expressioni

Gene expression databases

BgeeiQ68E01.
ExpressionAtlasiQ68E01. baseline and differential.
GenevisibleiQ68E01. HS.

Interactioni

Subunit structurei

Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, CPSF3L/INTS11 and INTS12. 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 SOSS-B1/NABP2, SOSS-B2/NABP1 and SOSS-C/INIP; the interaction is direct. Interacts with NBN/NBS1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ZBTB14O438293EBI-2680854,EBI-10176632

Protein-protein interaction databases

BioGridi122401. 60 interactions.
IntActiQ68E01. 16 interactions.
MINTiMINT-4534920.
STRINGi9606.ENSP00000318641.

Structurei

Secondary structure

1
1043
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 373Combined sources
Beta strandi41 – 433Combined sources
Helixi47 – 6317Combined sources
Helixi69 – 7911Combined sources
Helixi83 – 9917Combined sources
Turni101 – 1033Combined sources
Helixi104 – 11411Combined sources
Helixi120 – 13213Combined sources
Helixi134 – 1363Combined sources
Helixi139 – 15416Combined sources
Helixi160 – 16910Combined sources
Helixi179 – 19416Combined sources
Helixi196 – 1994Combined sources
Helixi203 – 21715Combined sources
Helixi224 – 24320Combined sources
Helixi245 – 2484Combined sources
Helixi249 – 2513Combined sources
Helixi253 – 2619Combined sources
Turni262 – 2643Combined sources
Helixi266 – 27712Combined sources
Helixi279 – 2824Combined sources
Helixi289 – 2935Combined sources
Helixi299 – 3046Combined sources
Helixi308 – 31710Combined sources
Beta strandi320 – 3223Combined sources
Helixi327 – 33711Combined sources
Beta strandi338 – 3414Combined sources
Helixi342 – 3454Combined sources
Helixi346 – 35611Combined sources
Helixi362 – 3665Combined sources
Beta strandi367 – 3693Combined sources
Helixi372 – 38110Combined sources
Helixi386 – 39611Combined sources
Turni397 – 4026Combined sources
Turni405 – 4073Combined sources
Helixi410 – 42314Combined sources
Turni424 – 4263Combined sources
Helixi428 – 44417Combined sources
Helixi447 – 4493Combined sources
Helixi450 – 46617Combined sources
Beta strandi469 – 4713Combined sources
Helixi474 – 4774Combined sources
Helixi484 – 49310Combined sources
Helixi495 – 4973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OWTX-ray2.00A35-499[»]
4OWWX-ray2.30A1-501[»]
4OWXX-ray2.30A1-501[»]
ProteinModelPortaliQ68E01.
SMRiQ68E01. Positions 33-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 3426Ala/Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the Integrator subunit 3 family.Curated

Phylogenomic databases

eggNOGiKOG4262. Eukaryota.
ENOG410XRCW. LUCA.
GeneTreeiENSGT00390000014184.
HOVERGENiHBG081800.
InParanoidiQ68E01.
KOiK13140.
OMAiTWQLFLA.
PhylomeDBiQ68E01.
TreeFamiTF323623.

Family and domain databases

InterProiIPR019333. Int_cplx_su3.
[Graphical view]
PfamiPF10189. DUF2356. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q68E01-1) [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
MELQKGKGAA AAAAASGAAG GGGGGAGAGA PGGGRLLLST SLDAKDELEE
60 70 80 90 100
RLERCMSIVT SMTAGVSERE ANDALNAYVC KGLPQHEEIC LGLFTLILTE
110 120 130 140 150
PAQAQKCYRD LALVSRDGMN IVLNKINQIL MEKYLKLQDT CRTQLVWLVR
160 170 180 190 200
ELVKSGVLGA DGVCMTFMKQ IAGGGDVTAK NIWLAESVLD ILTEQREWVL
210 220 230 240 250
KSSILIAMAV YTYLRLIVDH HGTAQLQALR QKEVDFCISL LRERFMECLM
260 270 280 290 300
IGRDLVRLLQ NVARIPEFEL LWKDIIHNPQ ALSPQFTGIL QLLQSRTSRK
310 320 330 340 350
FLACRLTPDM ETKLLFMTSR VRFGQQKRYQ DWFQRQYLST PDSQSLRCDL
360 370 380 390 400
IRYICGVVHP SNEVLSSDIL PRWAIIGWLL TTCTSNVAAS NAKLALFYDW
410 420 430 440 450
LFFSPDKDSI MNIEPAILVM HHSMKPHPAI TATLLDFMCR IIPNFYPPLE
460 470 480 490 500
GHVRQGVFSS LNHIVEKRVL AHLAPLFDNP KLDKELRAML REKFPEFCSS
510 520 530 540 550
PSPPVEVKIE EPVSMEMDNH MSDKDESCYD NAEAAFSDDE EDLNSKGKKR
560 570 580 590 600
EFRFHPIKET VVEEPVDITP YLDQLDESLR DKVLQLQKGS DTEAQCEVMQ
610 620 630 640 650
EIVDQVLEED FDSEQLSVLA SCLQELFKAH FRGEVLPEEI TEESLEESVG
660 670 680 690 700
KPLYLIFRNL CQMQEDNSSF SLLLDLLSEL YQKQPKIGYH LLYYLRASKA
710 720 730 740 750
AAGKMNLYES FAQATQLGDL HTCLMMDMKA CQEDDVRLLC HLTPSIYTEF
760 770 780 790 800
PDETLRSGEL LNMIVAVIDS AQLQELVCHV MMGNLVMFRK DSVLNILIQS
810 820 830 840 850
LDWETFEQYC AWQLFLAHNI PLETIIPILQ HLKYKEHPEA LSCLLLQLRR
860 870 880 890 900
EKPSEEMVKM VLSRPCHPDD QFTTSILRHW CMKHDELLAE HIKSLLIKNN
910 920 930 940 950
SLPRKRQSLR SSSSKLAQLT LEQILEHLDN LRLNLTNTKQ NFFSQTPILQ
960 970 980 990 1000
ALQHVQASCD EAHKMKFSDL FSLAEEYEDS STKPPKSRRK AALSSPRSRK
1010 1020 1030 1040
NATQPPNAEE ESGSSSASEE EDTKPKPTKR KRKGSSAVGS DSD
Length:1,043
Mass (Da):118,070
Last modified:October 11, 2004 - v1
Checksum:i66A49C646077C3F4
GO
Isoform 2 (identifier: Q68E01-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     173-173: Missing.

Show »
Length:1,042
Mass (Da):118,013
Checksum:i51F57DCE22F577C9
GO
Isoform 3 (identifier: Q68E01-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-207: Missing.
     942-942: F → CMPSTLGVQCRRCCPGPDYAWSQAGGRGRTPGATTHTRDKTTCACCLISSQTSDCFSFPALPFLPLV

Note: No experimental confirmation available.
Show »
Length:902
Mass (Da):103,152
Checksum:i369B918545703C6B
GO
Isoform 4 (identifier: Q68E01-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-488: Missing.

Note: No experimental confirmation available.
Show »
Length:555
Mass (Da):63,586
Checksum:i41F78C0B7C259B51
GO

Sequence cautioni

The sequence AAH25254.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH54513.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB15174.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC11329.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAH18229.1 differs from that shown.Intron retention.Curated
The sequence CAH71415.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAH71417.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAH71418.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341Y → C in CAE45974 (PubMed:17974005).Curated
Sequence conflicti300 – 3001K → E in BAF82714 (PubMed:14702039).Curated
Sequence conflicti363 – 3631E → G in CAE45974 (PubMed:17974005).Curated
Sequence conflicti685 – 6851P → T in CAE45974 (PubMed:17974005).Curated
Sequence conflicti803 – 8031W → R in CAE45876 (PubMed:17974005).Curated
Sequence conflicti827 – 8271P → L in BAC11329 (PubMed:14702039).Curated
Sequence conflicti896 – 8961L → P in BAG60890 (PubMed:14702039).Curated
Sequence conflicti952 – 9521L → P in BAG65611 (PubMed:14702039).Curated
Sequence conflicti967 – 9671F → L in CAE45876 (PubMed:17974005).Curated
Sequence conflicti972 – 9721S → P in BAB15174 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 488488Missing in isoform 4. 1 PublicationVSP_038130Add
BLAST
Alternative sequencei1 – 207207Missing in isoform 3. 1 PublicationVSP_038131Add
BLAST
Alternative sequencei173 – 1731Missing in isoform 2. 3 PublicationsVSP_021446
Alternative sequencei942 – 9421F → CMPSTLGVQCRRCCPGPDYA WSQAGGRGRTPGATTHTRDK TTCACCLISSQTSDCFSFPA LPFLPLV in isoform 3. 1 PublicationVSP_038132

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL832133 mRNA. Translation: CAH10398.1.
AK290025 mRNA. Translation: BAF82714.1.
AK298746 mRNA. Translation: BAG60890.1.
AK304874 mRNA. Translation: BAG65611.1.
BX640786 mRNA. Translation: CAE45876.1.
BX640950 mRNA. Translation: CAE45974.1.
CR627233 mRNA. Translation: CAH10366.1.
CR749212 mRNA. Translation: CAH18069.1.
CR749376 mRNA. Translation: CAH18229.1. Sequence problems.
AL513523 Genomic DNA. Translation: CAH71415.1. Sequence problems.
AL513523 Genomic DNA. Translation: CAH71416.1.
AL513523 Genomic DNA. Translation: CAH71417.1. Sequence problems.
AL513523 Genomic DNA. Translation: CAH71418.1. Sequence problems.
CH471121 Genomic DNA. Translation: EAW53279.1.
CH471121 Genomic DNA. Translation: EAW53283.1.
BC025254 mRNA. Translation: AAH25254.1. Different initiation.
BC054513 mRNA. Translation: AAH54513.1. Different initiation.
BC073985 mRNA. Translation: AAH73985.1.
BC098431 mRNA. Translation: AAH98431.1.
BC105092 mRNA. Translation: AAI05093.1.
BC105094 mRNA. Translation: AAI05095.1.
BC116458 mRNA. Translation: AAI16459.1.
AK025572 mRNA. Translation: BAB15174.1. Different initiation.
AK074979 mRNA. Translation: BAC11329.1. Different initiation.
BK005722 Genomic DNA. Translation: DAA05722.1.
CCDSiCCDS1052.1. [Q68E01-2]
RefSeqiNP_075391.3. NM_023015.3. [Q68E01-2]
XP_005245518.1. XM_005245461.2. [Q68E01-4]
XP_005276794.1. XM_005276737.2. [Q68E01-4]
UniGeneiHs.516522.

Genome annotation databases

EnsembliENST00000318967; ENSP00000318641; ENSG00000143624. [Q68E01-2]
ENST00000435409; ENSP00000404290; ENSG00000143624. [Q68E01-2]
ENST00000512605; ENSP00000425437; ENSG00000143624. [Q68E01-3]
ENST00000571768; ENSP00000458631; ENSG00000262826. [Q68E01-2]
ENST00000576030; ENSP00000460221; ENSG00000262826. [Q68E01-2]
ENST00000576422; ENSP00000459907; ENSG00000262826. [Q68E01-3]
GeneIDi65123.
KEGGihsa:65123.
UCSCiuc001fct.4. human. [Q68E01-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL832133 mRNA. Translation: CAH10398.1.
AK290025 mRNA. Translation: BAF82714.1.
AK298746 mRNA. Translation: BAG60890.1.
AK304874 mRNA. Translation: BAG65611.1.
BX640786 mRNA. Translation: CAE45876.1.
BX640950 mRNA. Translation: CAE45974.1.
CR627233 mRNA. Translation: CAH10366.1.
CR749212 mRNA. Translation: CAH18069.1.
CR749376 mRNA. Translation: CAH18229.1. Sequence problems.
AL513523 Genomic DNA. Translation: CAH71415.1. Sequence problems.
AL513523 Genomic DNA. Translation: CAH71416.1.
AL513523 Genomic DNA. Translation: CAH71417.1. Sequence problems.
AL513523 Genomic DNA. Translation: CAH71418.1. Sequence problems.
CH471121 Genomic DNA. Translation: EAW53279.1.
CH471121 Genomic DNA. Translation: EAW53283.1.
BC025254 mRNA. Translation: AAH25254.1. Different initiation.
BC054513 mRNA. Translation: AAH54513.1. Different initiation.
BC073985 mRNA. Translation: AAH73985.1.
BC098431 mRNA. Translation: AAH98431.1.
BC105092 mRNA. Translation: AAI05093.1.
BC105094 mRNA. Translation: AAI05095.1.
BC116458 mRNA. Translation: AAI16459.1.
AK025572 mRNA. Translation: BAB15174.1. Different initiation.
AK074979 mRNA. Translation: BAC11329.1. Different initiation.
BK005722 Genomic DNA. Translation: DAA05722.1.
CCDSiCCDS1052.1. [Q68E01-2]
RefSeqiNP_075391.3. NM_023015.3. [Q68E01-2]
XP_005245518.1. XM_005245461.2. [Q68E01-4]
XP_005276794.1. XM_005276737.2. [Q68E01-4]
UniGeneiHs.516522.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OWTX-ray2.00A35-499[»]
4OWWX-ray2.30A1-501[»]
4OWXX-ray2.30A1-501[»]
ProteinModelPortaliQ68E01.
SMRiQ68E01. Positions 33-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122401. 60 interactions.
IntActiQ68E01. 16 interactions.
MINTiMINT-4534920.
STRINGi9606.ENSP00000318641.

PTM databases

iPTMnetiQ68E01.
PhosphoSiteiQ68E01.

Polymorphism and mutation databases

BioMutaiINTS3.
DMDMi74724494.

Proteomic databases

EPDiQ68E01.
MaxQBiQ68E01.
PaxDbiQ68E01.
PRIDEiQ68E01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318967; ENSP00000318641; ENSG00000143624. [Q68E01-2]
ENST00000435409; ENSP00000404290; ENSG00000143624. [Q68E01-2]
ENST00000512605; ENSP00000425437; ENSG00000143624. [Q68E01-3]
ENST00000571768; ENSP00000458631; ENSG00000262826. [Q68E01-2]
ENST00000576030; ENSP00000460221; ENSG00000262826. [Q68E01-2]
ENST00000576422; ENSP00000459907; ENSG00000262826. [Q68E01-3]
GeneIDi65123.
KEGGihsa:65123.
UCSCiuc001fct.4. human. [Q68E01-1]

Organism-specific databases

CTDi65123.
GeneCardsiINTS3.
H-InvDBHIX0001090.
HGNCiHGNC:26153. INTS3.
MIMi611347. gene.
neXtProtiNX_Q68E01.
PharmGKBiPA142672510.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4262. Eukaryota.
ENOG410XRCW. LUCA.
GeneTreeiENSGT00390000014184.
HOVERGENiHBG081800.
InParanoidiQ68E01.
KOiK13140.
OMAiTWQLFLA.
PhylomeDBiQ68E01.
TreeFamiTF323623.

Enzyme and pathway databases

ReactomeiR-HSA-6807505. RNA polymerase II transcribes snRNA genes.

Miscellaneous databases

ChiTaRSiINTS3. human.
GeneWikiiINTS3.
GenomeRNAii65123.
PROiQ68E01.
SOURCEiSearch...

Gene expression databases

BgeeiQ68E01.
ExpressionAtlasiQ68E01. baseline and differential.
GenevisibleiQ68E01. HS.

Family and domain databases

InterProiIPR019333. Int_cplx_su3.
[Graphical view]
PfamiPF10189. DUF2356. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Amygdala, Cervix, Fetal kidney, Retina and Testis.
  2. "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] (ISOFORMS 2; 3 AND 4).
    Tissue: Hepatoma, Hippocampus, Teratocarcinoma and Uterus.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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] (ISOFORM 2).
    Tissue: Brain, Lung, Skin, Testis and Uterus.
  6. "Integrator, a multiprotein mediator of small nuclear RNA processing, associates with the C-terminal repeat of RNA polymerase II."
    Baillat D., Hakimi M.-A., Naeaer A.M., Shilatifard A., Cooch N., Shiekhattar R.
    Cell 123:265-276(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE INTEGRATOR COMPLEX.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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.
  10. "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 NABP1; INIP AND NBN.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-995, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiINT3_HUMAN
AccessioniPrimary (citable) accession number: Q68E01
Secondary accession number(s): A8K1W0
, B4DQC8, B4E3U9, D3DV57, Q4G0E5, Q5VUQ5, Q5VUQ6, Q5VUR0, Q5VUR1, Q68DJ1, Q69YR5, Q6AI57, Q6DKG7, Q6MZQ4, Q6MZZ9, Q8NC46, Q8TB23, Q9H6S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 11, 2004
Last modified: June 8, 2016
This is version 108 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 1
    Human chromosome 1: 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.