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Protein

Integrator complex subunit 1

Gene

INTS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the Integrator complex, a complex 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.

GO - Biological processi

  • snRNA processing Source: HGNC
  • snRNA transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Integrator complex subunit 1
Short name:
Int1
Gene namesi
Name:INTS1
Synonyms:KIAA1440
ORF Names:UNQ1821/PRO3434
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:24555. INTS1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1159 – 117921HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • integrator complex Source: HGNC
  • membrane Source: UniProtKB
  • nuclear membrane Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA144596420.

Polymorphism and mutation databases

BioMutaiINTS1.
DMDMi97052424.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21902190Integrator complex subunit 1PRO_0000236044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei47 – 471N6-acetyllysineCombined sources
Modified residuei83 – 831PhosphothreonineCombined sources
Modified residuei87 – 871PhosphoserineCombined sources
Modified residuei307 – 3071PhosphoserineCombined sources
Modified residuei924 – 9241PhosphoserineCombined sources
Modified residuei1318 – 13181PhosphoserineCombined sources
Modified residuei1326 – 13261PhosphoserineBy similarity
Modified residuei1327 – 13271PhosphoserineBy similarity
Modified residuei1395 – 13951PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8N201.
MaxQBiQ8N201.
PaxDbiQ8N201.
PeptideAtlasiQ8N201.
PRIDEiQ8N201.

PTM databases

iPTMnetiQ8N201.
PhosphoSiteiQ8N201.

Expressioni

Gene expression databases

BgeeiQ8N201.
ExpressionAtlasiQ8N201. baseline and differential.
GenevisibleiQ8N201. HS.

Organism-specific databases

HPAiHPA021658.
HPA053009.

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 INTS12.1 Publication

Protein-protein interaction databases

BioGridi117596. 56 interactions.
DIPiDIP-48476N.
IntActiQ8N201. 9 interactions.
MINTiMINT-1420278.
STRINGi9606.ENSP00000385722.

Structurei

3D structure databases

ProteinModelPortaliQ8N201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 644Poly-Ala
Compositional biasi1580 – 15834Poly-Val
Compositional biasi1875 – 18784Poly-Leu

Sequence similaritiesi

Belongs to the Integrator subunit 1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4596. Eukaryota.
ENOG410XTAB. LUCA.
GeneTreeiENSGT00390000015743.
HOVERGENiHBG081799.
InParanoidiQ8N201.
KOiK13138.
OMAiHIPRIWQ.
OrthoDBiEOG7R830Q.
PhylomeDBiQ8N201.
TreeFamiTF313809.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR022145. DUF3677.
[Graphical view]
PfamiPF12432. DUF3677. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.

Sequencei

Sequence statusi: Complete.

Q8N201-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRAKPTTVR RPSAAAKPSG HPPPGDFIAL GSKGQANESK TASTLLKPAP
60 70 80 90 100
SGLPSERKRD AAAALSSASA LTGLTKRPKL SSTPPLSALG RLAEAAVAEK
110 120 130 140 150
RAISPSIKEP SVVPIEVLPT VLLDEIEAAE LEGNDDRIEG VLCGAVKQLK
160 170 180 190 200
VTRAKPDSTL YLSLMYLAKI KPNIFATEGV IEALCSLLRR DASINFKAKG
210 220 230 240 250
NSLVSVLACN LLMAAYEEDE NWPEIFVKVY IEDSLGERIW VDSPHCKTFV
260 270 280 290 300
DNIQTAFNTR MPPRSVLLQG EAGRVAGDLG AGSSPHPSLT EEEDSQTELL
310 320 330 340 350
IAEEKLSPEQ EGQLMPRYEE LAESVEEYVL DMLRDQLNRR QPIDNVSRNL
360 370 380 390 400
LRLLTSTCGY KEVRLLAVQK LEMWLQNPKL TRPAQDLLMS VCMNCNTHGS
410 420 430 440 450
EDMDVISHLI KIRLKPKVLL NHFMLCIREL LSAHKDNLGT TIKLVIFNEL
460 470 480 490 500
SSARNPNNMQ VLYTALQHSS ELAPKFLAMV FQDLLTNKDD YLRASRALLR
510 520 530 540 550
EIIKQTKHEI NFQAFCLGLM QERKEPQYLE MEFKERFVVH ITDVLAVSMM
560 570 580 590 600
LGITAQVKEA GIAWDKGEKR NLEVLRSFQN QIAAIQRDAV WWLHTVVPSI
610 620 630 640 650
SKLAPKDYVH CLHKVLFTEQ PETYYKWDNW PPESDRNFFL RLCSEVPILE
660 670 680 690 700
DTLMRILVIG LSRELPLGPA DAMELADHLV KRAAAVQADD VEVLKVGRTQ
710 720 730 740 750
LIDAVLNLCT YHHPENIQLP PGYQPPNLAI STLYWKAWPL LLVVAAFNPE
760 770 780 790 800
NIGLAAWEEY PTLKMLMEMV MTNNYSYPPC TLTDEETRTE MLNRELQTAQ
810 820 830 840 850
REKQEILAFE GHLAAASTKQ TITESSSLLL SQLTSLDPQG PPRRPPPHIL
860 870 880 890 900
DQVKSLNQSL RLGHLLCRSR NPDFLLHIIQ RQASSQSMPW LADLVQSSEG
910 920 930 940 950
SLDVLPVQCL CEFLLHDAVD DAASGEEDDE GESKEQKAKK RQRQQKQRQL
960 970 980 990 1000
LGRLQDLLLG PKADEQTTCE VLDYFLRRLG SSQVASRVLA MKGLSLVLSE
1010 1020 1030 1040 1050
GSLRDGEEKE PPMEEDVGDT DVLQGYQWLL RDLPRLPLFD SVRSTTALAL
1060 1070 1080 1090 1100
QQAIHMETDP QTISAYLIYL SQHTPVEEQA QHSDLALDVA RLVVERSTIM
1110 1120 1130 1140 1150
SHLFSKLSPS AASDAVLSAL LSIFSRYVRR MRQSKEGEEV YSWSESQDQV
1160 1170 1180 1190 1200
FLRWSSGETA TMHILVVHAM VILLTLGPPR ADDSEFQALL DIWFPEEKPL
1210 1220 1230 1240 1250
PTAFLVDTSE EALLLPDWLK LRMIRSEVLR LVDAALQDLE PQQLLLFVQS
1260 1270 1280 1290 1300
FGIPVSSMSK LLQFLDQAVA HDPQTLEQNI MDKNYMAHLV EVQHERGASG
1310 1320 1330 1340 1350
GQTFHSLLTA SLPPRRDSTE APKPKSSPEQ PIGQGRIRVG TQLRVLGPED
1360 1370 1380 1390 1400
DLAGMFLQIF PLSPDPRWQS SSPRPVALAL QQALGQELAR VVQGSPEVPG
1410 1420 1430 1440 1450
ITVRVLQALA TLLSSPHGGA LVMSMHRSHF LACPLLRQLC QYQRCVPQDT
1460 1470 1480 1490 1500
GFSSLFLKVL LQMLQWLDSP GVEGGPLRAQ LRMLASQASA GRRLSDVRGG
1510 1520 1530 1540 1550
LLRLAEALAF RQDLEVVSST VRAVIATLRS GEQCSVEPDL ISKVLQGLIE
1560 1570 1580 1590 1600
VRSPHLEELL TAFFSATADA ASPFPACKPV VVVSSLLLQE EEPLAGGKPG
1610 1620 1630 1640 1650
ADGGSLEAVR LGPSSGLLVD WLEMLDPEVV SSCPDLQLRL LFSRRKGKGQ
1660 1670 1680 1690 1700
AQVPSFRPYL LTLFTHQSSW PTLHQCIRVL LGKSREQRFD PSASLDFLWA
1710 1720 1730 1740 1750
CIHVPRIWQG RDQRTPQKRR EELVLRVQGP ELISLVELIL AEAETRSQDG
1760 1770 1780 1790 1800
DTAACSLIQA RLPLLLSCCC GDDESVRKVT EHLSGCIQQW GDSVLGRRCR
1810 1820 1830 1840 1850
DLLLQLYLQR PELRVPVPEV LLHSEGAASS SVCKLDGLIH RFITLLADTS
1860 1870 1880 1890 1900
DSRALENRGA DASMACRKLA VAHPLLLLRH LPMIAALLHG RTHLNFQEFR
1910 1920 1930 1940 1950
QQNHLSCFLH VLGLLELLQP HVFRSEHQGA LWDCLLSFIR LLLNYRKSSR
1960 1970 1980 1990 2000
HLAAFINKFV QFIHKYITYN APAAISFLQK HADPLHDLSF DNSDLVMLKS
2010 2020 2030 2040 2050
LLAGLSLPSR DDRTDRGLDE EGEEESSAGS LPLVSVSLFT PLTAAEMAPY
2060 2070 2080 2090 2100
MKRLSRGQTV EDLLEVLSDI DEMSRRRPEI LSFFSTNLQR LMSSAEECCR
2110 2120 2130 2140 2150
NLAFSLALRS MQNSPSIAAA FLPTFMYCLG SQDFEVVQTA LRNLPEYALL
2160 2170 2180 2190
CQEHAAVLLH RAFLVGMYGQ MDPSAQISEA LRILHMEAVM
Length:2,190
Mass (Da):244,297
Last modified:May 16, 2006 - v2
Checksum:i342FF560BF3F61F6
GO

Sequence cautioni

The sequence AAQ88846.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti636 – 6361R → Y (PubMed:16421571).Curated
Sequence conflicti1862 – 18621A → G in BAA92678 (PubMed:10718198).Curated
Sequence conflicti2004 – 20041G → V in CAB70710 (PubMed:17974005).Curated
Sequence conflicti2105 – 21051S → C in CAB70710 (PubMed:17974005).Curated
Sequence conflicti2162 – 21621A → AF in CAB70710 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti172 – 1721P → L.
Corresponds to variant rs3752714 [ dbSNP | Ensembl ].
VAR_049627

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC102953 Genomic DNA. No translation available.
AC093734 Genomic DNA. No translation available.
AB037861 mRNA. Translation: BAA92678.1.
AY358482 mRNA. Translation: AAQ88846.1. Different initiation.
BC013367 mRNA. Translation: AAH13367.2.
BC018777 mRNA. Translation: AAH18777.1.
BC069262 mRNA. Translation: AAH69262.1.
AL050110 mRNA. Translation: CAB43278.2.
AL137358 mRNA. Translation: CAB70710.3.
BK005720 mRNA. Translation: DAA05720.1.
CCDSiCCDS47526.1.
PIRiT08758.
T46429.
RefSeqiNP_001073922.2. NM_001080453.2.
UniGeneiHs.532188.

Genome annotation databases

EnsembliENST00000404767; ENSP00000385722; ENSG00000164880.
GeneIDi26173.
KEGGihsa:26173.
UCSCiuc003skn.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC102953 Genomic DNA. No translation available.
AC093734 Genomic DNA. No translation available.
AB037861 mRNA. Translation: BAA92678.1.
AY358482 mRNA. Translation: AAQ88846.1. Different initiation.
BC013367 mRNA. Translation: AAH13367.2.
BC018777 mRNA. Translation: AAH18777.1.
BC069262 mRNA. Translation: AAH69262.1.
AL050110 mRNA. Translation: CAB43278.2.
AL137358 mRNA. Translation: CAB70710.3.
BK005720 mRNA. Translation: DAA05720.1.
CCDSiCCDS47526.1.
PIRiT08758.
T46429.
RefSeqiNP_001073922.2. NM_001080453.2.
UniGeneiHs.532188.

3D structure databases

ProteinModelPortaliQ8N201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117596. 56 interactions.
DIPiDIP-48476N.
IntActiQ8N201. 9 interactions.
MINTiMINT-1420278.
STRINGi9606.ENSP00000385722.

PTM databases

iPTMnetiQ8N201.
PhosphoSiteiQ8N201.

Polymorphism and mutation databases

BioMutaiINTS1.
DMDMi97052424.

Proteomic databases

EPDiQ8N201.
MaxQBiQ8N201.
PaxDbiQ8N201.
PeptideAtlasiQ8N201.
PRIDEiQ8N201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000404767; ENSP00000385722; ENSG00000164880.
GeneIDi26173.
KEGGihsa:26173.
UCSCiuc003skn.3. human.

Organism-specific databases

CTDi26173.
GeneCardsiINTS1.
H-InvDBHIX0006419.
HGNCiHGNC:24555. INTS1.
HPAiHPA021658.
HPA053009.
MIMi611345. gene.
neXtProtiNX_Q8N201.
PharmGKBiPA144596420.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4596. Eukaryota.
ENOG410XTAB. LUCA.
GeneTreeiENSGT00390000015743.
HOVERGENiHBG081799.
InParanoidiQ8N201.
KOiK13138.
OMAiHIPRIWQ.
OrthoDBiEOG7R830Q.
PhylomeDBiQ8N201.
TreeFamiTF313809.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiINTS1. human.
GenomeRNAii26173.
PROiQ8N201.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N201.
ExpressionAtlasiQ8N201. baseline and differential.
GenevisibleiQ8N201. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR022145. DUF3677.
[Graphical view]
PfamiPF12432. DUF3677. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 814-2190.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1147-2190.
  4. "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] OF 1291-2190.
    Tissue: Brain, Lymph and Skin.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1558-2190.
    Tissue: 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, SUBCELLULAR LOCATION.
    Tissue: Cervix carcinoma.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-1318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-13; THR-83; SER-307 AND SER-1395, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  18. "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-87; SER-307 AND SER-924, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiINT1_HUMAN
AccessioniPrimary (citable) accession number: Q8N201
Secondary accession number(s): A6NJ44
, Q6NT70, Q6UX74, Q8WV40, Q96D36, Q9NTD1, Q9P2A8, Q9Y3W8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: July 6, 2016
This is version 102 of the entry and version 2 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 7
    Human chromosome 7: 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

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.