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Q6KC79

- NIPBL_HUMAN

UniProt

Q6KC79 - NIPBL_HUMAN

Protein

Nipped-B-like protein

Gene

NIPBL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Probably plays a structural role in chromatin. Involved in sister chromatid cohesion, possibly by interacting with the cohesin complex By similarity.By similarity

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. chromo shadow domain binding Source: BHF-UCL
    3. histone deacetylase binding Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. protein C-terminus binding Source: UniProtKB
    6. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

    1. brain development Source: BHF-UCL
    2. cellular protein localization Source: UniProtKB
    3. cellular response to DNA damage stimulus Source: UniProtKB
    4. cellular response to X-ray Source: UniProtKB
    5. cognition Source: BHF-UCL
    6. developmental growth Source: BHF-UCL
    7. ear morphogenesis Source: BHF-UCL
    8. embryonic digestive tract morphogenesis Source: BHF-UCL
    9. embryonic forelimb morphogenesis Source: BHF-UCL
    10. embryonic viscerocranium morphogenesis Source: Ensembl
    11. external genitalia morphogenesis Source: BHF-UCL
    12. eye morphogenesis Source: BHF-UCL
    13. face morphogenesis Source: BHF-UCL
    14. fat cell differentiation Source: Ensembl
    15. forelimb morphogenesis Source: BHF-UCL
    16. gall bladder development Source: BHF-UCL
    17. heart morphogenesis Source: BHF-UCL
    18. maintenance of mitotic sister chromatid cohesion Source: UniProtKB
    19. metanephros development Source: BHF-UCL
    20. mitotic cell cycle Source: Reactome
    21. mitotic sister chromatid cohesion Source: UniProtKB
    22. negative regulation of transcription, DNA-templated Source: BHF-UCL
    23. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    24. outflow tract morphogenesis Source: BHF-UCL
    25. positive regulation of histone deacetylation Source: BHF-UCL
    26. positive regulation of multicellular organism growth Source: Ensembl
    27. positive regulation of ossification Source: Ensembl
    28. regulation of developmental growth Source: BHF-UCL
    29. regulation of embryonic development Source: BHF-UCL
    30. regulation of hair cycle Source: BHF-UCL
    31. sensory perception of sound Source: BHF-UCL
    32. stem cell maintenance Source: Ensembl
    33. uterus morphogenesis Source: BHF-UCL

    Keywords - Biological processi

    Cell cycle

    Enzyme and pathway databases

    ReactomeiREACT_150421. Cohesin Loading onto Chromatin.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nipped-B-like protein
    Alternative name(s):
    Delangin
    SCC2 homolog
    Gene namesi
    Name:NIPBL
    Synonyms:IDN3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:28862. NIPBL.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. SMC loading complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Cornelia de Lange syndrome 1 (CDLS1) [MIM:122470]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. Characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1206 – 12061Missing in CDLS1. 1 Publication
    VAR_038413
    Natural varianti1246 – 12461A → G in CDLS1. 1 Publication
    VAR_021598
    Natural varianti1311 – 13111C → R in CDLS1. 1 Publication
    VAR_019519
    Natural varianti1312 – 13121L → P in CDLS1. 1 Publication
    VAR_021599
    Natural varianti1348 – 13481L → R in CDLS1. 1 Publication
    VAR_019520
    Natural varianti1789 – 17891R → L in CDLS1. 1 Publication
    VAR_021600
    Natural varianti1803 – 18031D → V in CDLS1. 1 Publication
    VAR_021601
    Natural varianti1856 – 18561R → T in CDLS1. 1 Publication
    VAR_021602
    Natural varianti1897 – 18971Missing in CDLS1. 1 Publication
    VAR_064544
    Natural varianti2081 – 20811G → A in CDLS1. 1 Publication
    VAR_064545
    Natural varianti2090 – 20901S → I in CDLS1. 1 Publication
    VAR_064546
    Natural varianti2150 – 21501L → P in CDLS1. 1 Publication
    VAR_064547
    Natural varianti2298 – 22981R → C in CDLS1. 1 Publication
    VAR_021603
    Natural varianti2298 – 22981R → H in CDLS1. 1 Publication
    VAR_021604
    Natural varianti2312 – 23121G → R in CDLS1. 1 Publication
    VAR_021605
    Natural varianti2381 – 23811G → A in CDLS1. 1 Publication
    VAR_021606
    Natural varianti2390 – 23901A → T in CDLS1. 1 Publication
    VAR_021607
    Natural varianti2430 – 24301Y → C in CDLS1. 1 Publication
    VAR_019521
    Natural varianti2440 – 24401Y → H in CDLS1. 1 Publication
    VAR_021608

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1003 – 10031V → E: Abolishes interaction with CBX5; when associated with Glu-1005. 1 Publication
    Mutagenesisi1005 – 10051L → E: Abolishes interaction with CBX5; when associated with Glu-1003. 1 Publication

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi122470. phenotype.
    Orphaneti329802. 5p13 microduplication syndrome.
    199. Cornelia de Lange syndrome.
    PharmGKBiPA134962343.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 28042804Nipped-B-like proteinPRO_0000218596Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei150 – 1501Phosphoserine1 Publication
    Modified residuei162 – 1621Phosphoserine1 Publication
    Modified residuei256 – 2561Phosphoserine1 Publication
    Modified residuei280 – 2801PhosphoserineBy similarity
    Modified residuei306 – 3061Phosphoserine1 Publication
    Modified residuei318 – 3181Phosphoserine2 Publications
    Modified residuei350 – 3501Phosphoserine3 Publications
    Modified residuei713 – 7131Phosphothreonine1 Publication
    Modified residuei746 – 7461Phosphothreonine1 Publication
    Modified residuei912 – 9121Phosphoserine1 Publication
    Modified residuei1082 – 10821N6-acetyllysineBy similarity
    Modified residuei1089 – 10891Phosphoserine2 Publications
    Modified residuei1090 – 10901Phosphoserine2 Publications
    Modified residuei1096 – 10961Phosphoserine4 Publications
    Modified residuei1150 – 11501Phosphoserine3 Publications
    Modified residuei1152 – 11521Phosphoserine2 Publications
    Modified residuei1154 – 11541Phosphoserine3 Publications
    Modified residuei1160 – 11601Phosphoserine3 Publications
    Modified residuei2509 – 25091Phosphoserine2 Publications
    Modified residuei2511 – 25111Phosphoserine2 Publications
    Modified residuei2513 – 25131Phosphoserine2 Publications
    Modified residuei2515 – 25151Phosphoserine2 Publications
    Modified residuei2658 – 26581Phosphoserine8 Publications
    Modified residuei2667 – 26671Phosphothreonine2 Publications
    Modified residuei2672 – 26721Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6KC79.
    PaxDbiQ6KC79.
    PRIDEiQ6KC79.

    PTM databases

    PhosphoSiteiQ6KC79.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in heart, skeletal muscle, fetal and adult liver, fetal and adult kidney. Expressed at intermediates level in thymus, placenta, peripheral leukocyte and small intestine. Weakly or not expressed in brain, colon, spleen and lung.2 Publications

    Developmental stagei

    In embryos, it is expressed in developing limbs and later in cartilage primordia of the ulna and of various hand bones. Sites of craniofacial expression include the cartilage primordium of the basioccipital and basisphenoid skull bones and elsewhere in the head and face, including a region encompassing the mesenchyme adjacent to the cochlear canal. Also expressed in the spinal column, notochord and surface ectoderm sclerotome and what seem to be migrating myoblasts. Expressed in the developing heart in the atrial and ventricular myocardium and in the ventricular tubeculae but absent in the endocardial cushions. Also expressed in the developing esophagus, trachea and midgut loops, in the bronchi of the lung and in the tubules of the metanephros. Expression in organs and tissues not typically affected in CDL (e.g. the developing trachea, bronchi, esophagus, heart and kidney) may reflect a bias towards underreporting of more subtle aspects of the phenotype or problems that typically present later in life. Expressed in the mesenchyme surrounding the cochlear canal possibly reflecting the hearing impairment commonly found. Weakly or not expressed in embryonic brain.1 Publication

    Gene expression databases

    ArrayExpressiQ6KC79.
    BgeeiQ6KC79.
    CleanExiHS_NIPBL.
    GenevestigatoriQ6KC79.

    Organism-specific databases

    HPAiHPA040834.

    Interactioni

    Subunit structurei

    Interacts directly with CBX5 via the PxVxL motif.2 Publications

    Protein-protein interaction databases

    BioGridi117363. 26 interactions.
    DIPiDIP-29199N.
    IntActiQ6KC79. 9 interactions.
    MINTiMINT-4103787.
    STRINGi9606.ENSP00000282516.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6KC79.
    SMRiQ6KC79. Positions 1768-1856, 2063-2096, 2173-2201.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1767 – 180539HEAT 1Add
    BLAST
    Repeati1843 – 188139HEAT 2Add
    BLAST
    Repeati1945 – 198440HEAT 3Add
    BLAST
    Repeati2227 – 226741HEAT 4Add
    BLAST
    Repeati2313 – 235139HEAT 5Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi996 – 100914PxVxL motifAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi418 – 46245Gln-richAdd
    BLAST

    Domaini

    Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain.

    Sequence similaritiesi

    Belongs to the SCC2/Nipped-B family.Curated
    Contains 5 HEAT repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG128278.
    HOVERGENiHBG052626.
    InParanoidiQ6KC79.
    KOiK06672.
    OMAiRDICIEQ.
    OrthoDBiEOG7CZK4Q.
    PhylomeDBiQ6KC79.
    TreeFamiTF313121.

    Family and domain databases

    Gene3Di1.25.10.10. 3 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR026003. Cohesin_HEAT.
    IPR024986. Nipped-B_C.
    [Graphical view]
    PfamiPF12765. Cohesin_HEAT. 1 hit.
    PF12830. Nipped-B_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 3 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6KC79-1) [UniParc]FASTAAdd to Basket

    Also known as: A, IDN3-A

    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

    MNGDMPHVPI TTLAGIASLT DLLNQLPLPS PLPATTTKSL LFNARIAEEV     50
    NCLLACRDDN LVSQLVHSLN QVSTDHIELK DNLGSDDPEG DIPVLLQAVL 100
    ARSPNVFREK SMQNRYVQSG MMMSQYKLSQ NSMHSSPASS NYQQTTISHS 150
    PSSRFVPPQT SSGNRFMPQQ NSPVPSPYAP QSPAGYMPYS HPSSYTTHPQ 200
    MQQASVSSPI VAGGLRNIHD NKVSGPLSGN SANHHADNPR HGSSEDYLHM 250
    VHRLSSDDGD SSTMRNAASF PLRSPQPVCS PAGSEGTPKG SRPPLILQSQ 300
    SLPCSSPRDV PPDILLDSPE RKQKKQKKMK LGKDEKEQSE KAAMYDIISS 350
    PSKDSTKLTL RLSRVRSSDM DQQEDMISGV ENSNVSENDI PFNVQYPGQT 400
    SKTPITPQDI NRPLNAAQCL SQQEQTAFLP ANQVPVLQQN TSVAAKQPQT 450
    SVVQNQQQIS QQGPIYDEVE LDALAEIERI ERESAIERER FSKEVQDKDK 500
    PLKKRKQDSY PQEAGGATGG NRPASQETGS TGNGSRPALM VSIDLHQAGR 550
    VDSQASITQD SDSIKKPEEI KQCNDAPVSV LQEDIVGSLK STPENHPETP 600
    KKKSDPELSK SEMKQSESRL AESKPNENRL VETKSSENKL ETKVETQTEE 650
    LKQNESRTTE CKQNESTIVE PKQNENRLSD TKPNDNKQNN GRSETTKSRP 700
    ETPKQKGESR PETPKQKSDG HPETPKQKGD GRPETPKQKG ESRPETPKQK 750
    NEGRPETPKH RHDNRRDSGK PSTEKKPEVS KHKQDTKSDS PRLKSERAEA 800
    LKQRPDGRSV SESLRRDHDN KQKSDDRGES ERHRGDQSRV RRPETLRSSS 850
    RNEHGIKSDS SKTDKLERKH RHESGDSRER PSSGEQKSRP DSPRVKQGDS 900
    NKSRSDKLGF KSPTSKDDKR TEGNKSKVDT NKAHPDNKAE FPSYLLGGRS 950
    GALKNFVIPK IKRDKDGNVT QETKKMEMKG EPKDKVEKIG LVEDLNKGAK 1000
    PVVVLQKLSL DDVQKLIKDR EDKSRSSLKP IKNKPSKSNK GSIDQSVLKE 1050
    LPPELLAEIE STMPLCERVK MNKRKRSTVN EKPKYAEISS DEDNDSDEAF 1100
    ESSRKRHKKD DDKAWEYEER DRRSSGDHRR SGHSHEGRRS SGGGRYRNRS 1150
    PSDSDMEDYS PPPSLSEVAR KMKKKEKQKK RKAYEPKLTP EEMMDSSTFK 1200
    RFTASIENIL DNLEDMDFTA FGDDDEIPQE LLLGKHQLNE LGSESAKIKA 1250
    MGIMDKLSTD KTVKVLNILE KNIQDGSKLS TLLNHNNDTE EEERLWRDLI 1300
    MERVTKSADA CLTTINIMTS PNMPKAVYIE DVIERVIQYT KFHLQNTLYP 1350
    QYDPVYRLDP HGGGLLSSKA KRAKCSTHKQ RVIVMLYNKV CDIVSSLSEL 1400
    LEIQLLTDTT ILQVSSMGIT PFFVENVSEL QLCAIKLVTA VFSRYEKHRQ 1450
    LILEEIFTSL ARLPTSKRSL RNFRLNSSDM DGEPMYIQMV TALVLQLIQC 1500
    VVHLPSSEKD SNAEEDSNKK IDQDVVITNS YETAMRTAQN FLSIFLKKCG 1550
    SKQGEEDYRP LFENFVQDLL STVNKPEWPA AELLLSLLGR LLVHQFSNKS 1600
    TEMALRVASL DYLGTVAARL RKDAVTSKMD QGSIERILKQ VSGGEDEIQQ 1650
    LQKALLDYLD ENTETDPSLV FSRKFYIAQW FRDTTLETEK AMKSQKDEES 1700
    SEGTHHAKEI ETTGQIMHRA ENRKKFLRSI IKTTPSQFST LKMNSDTVDY 1750
    DDACLIVRYL ASMRPFAQSF DIYLTQILRV LGENAIAVRT KAMKCLSEVV 1800
    AVDPSILARL DMQRGVHGRL MDNSTSVREA AVELLGRFVL CRPQLAEQYY 1850
    DMLIERILDT GISVRKRVIK ILRDICIEQP TFPKITEMCV KMIRRVNDEE 1900
    GIKKLVNETF QKLWFTPTPH NDKEAMTRKI LNITDVVAAC RDTGYDWFEQ 1950
    LLQNLLKSEE DSSYKPVKKA CTQLVDNLVE HILKYEESLA DSDNKGVNSG 2000
    RLVACITTLF LFSKIRPQLM VKHAMTMQPY LTTKCSTQND FMVICNVAKI 2050
    LELVVPLMEH PSETFLATIE EDLMKLIIKY GMTVVQHCVS CLGAVVNKVT 2100
    QNFKFVWACF NRYYGAISKL KSQHQEDPNN TSLLTNKPAL LRSLFTVGAL 2150
    CRHFDFDLED FKGNSKVNIK DKVLELLMYF TKHSDEEVQT KAIIGLGFAF 2200
    IQHPSLMFEQ EVKNLYNNIL SDKNSSVNLK IQVLKNLQTY LQEEDTRMQQ 2250
    ADRDWKKVAK QEDLKEMGDV SSGMSSSIMQ LYLKQVLEAF FHTQSSVRHF 2300
    ALNVIALTLN QGLIHPVQCV PYLIAMGTDP EPAMRNKADQ QLVEIDKKYA 2350
    GFIHMKAVAG MKMSYQVQQA INTCLKDPVR GFRQDESSSA LCSHLYSMIR 2400
    GNRQHRRAFL ISLLNLFDDT AKTDVTMLLY IADNLACFPY QTQEEPLFIM 2450
    HHIDITLSVS GSNLLQSFKE SMVKDKRKER KSSPSKENES SDSEEEVSRP 2500
    RKSRKRVDSD SDSDSEDDIN SVMKCLPENS APLIEFANVS QGILLLLMLK 2550
    QHLKNLCGFS DSKIQKYSPS ESAKVYDKAI NRKTGVHFHP KQTLDFLRSD 2600
    MANSKITEEV KRSIVKQYLD FKLLMEHLDP DEEEEEGEVS ASTNARNKAI 2650
    TSLLGGGSPK NNTAAETEDD ESDGEDRGGG TSGSLRRSKR NSDSTELAAQ 2700
    MNESVDVMDV IAICCPKYKD RPQIARVVQK TSSGFSVQWM AGSYSGSWTE 2750
    AKRRDGRKLV PWVDTIKESD IIYKKIALTS ANKLTNKVVQ TLRSLYAAKD 2800
    GTSS 2804
    Length:2,804
    Mass (Da):316,051
    Last modified:July 19, 2004 - v2
    Checksum:iC275425DF53058A3
    GO
    Isoform 2 (identifier: Q6KC79-2) [UniParc]FASTAAdd to Basket

    Also known as: B, IDN3-B

    The sequence of this isoform differs from the canonical sequence as follows:
         2684-2697: SLRRSKRNSDSTEL → VRRRRSQRISQRIT
         2698-2804: Missing.

    Note: Contains a phosphothreonine at position 2667. Contains a phosphoserine at position 2672.

    Show »
    Length:2,697
    Mass (Da):304,344
    Checksum:i42207C9622A3C01D
    GO
    Isoform 3 (identifier: Q6KC79-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1102-2804: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,101
    Mass (Da):122,367
    Checksum:i0344321AFFE6ACFA
    GO

    Sequence cautioni

    The sequence BAA77335.1 differs from that shown. Reason: Chimeric cDNA.
    The sequence BAA77349.1 differs from that shown. Reason: Chimeric cDNA.
    The sequence CAE45790.1 differs from that shown. Reason: Frameshift at position 278.
    The sequence AAH33847.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAC86701.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti318 – 3181S → F(PubMed:14702039)Curated
    Sequence conflicti548 – 5481A → T in CAD98051. (PubMed:17974005)Curated
    Sequence conflicti548 – 5481A → T in CAD98052. (PubMed:17974005)Curated
    Sequence conflicti574 – 5741N → S in CAD98051. (PubMed:17974005)Curated
    Sequence conflicti574 – 5741N → S in CAD98052. (PubMed:17974005)Curated
    Sequence conflicti648 – 6481T → I in CAD98051. (PubMed:17974005)Curated
    Sequence conflicti648 – 6481T → I in CAD98052. (PubMed:17974005)Curated
    Sequence conflicti1172 – 11721M → K in CAD98051. (PubMed:17974005)Curated
    Sequence conflicti1172 – 11721M → K in CAD98052. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti135 – 1351S → N.
    Corresponds to variant rs3822471 [ dbSNP | Ensembl ].
    VAR_019518
    Natural varianti261 – 2611S → A.
    Corresponds to variant rs16903425 [ dbSNP | Ensembl ].
    VAR_038411
    Natural varianti384 – 3841N → S.
    Corresponds to variant rs2291703 [ dbSNP | Ensembl ].
    VAR_038412
    Natural varianti674 – 6741N → S.1 Publication
    Corresponds to variant rs3822471 [ dbSNP | Ensembl ].
    VAR_021596
    Natural varianti1206 – 12061I → V.1 Publication
    VAR_021597
    Natural varianti1206 – 12061Missing in CDLS1. 1 Publication
    VAR_038413
    Natural varianti1246 – 12461A → G in CDLS1. 1 Publication
    VAR_021598
    Natural varianti1311 – 13111C → R in CDLS1. 1 Publication
    VAR_019519
    Natural varianti1312 – 13121L → P in CDLS1. 1 Publication
    VAR_021599
    Natural varianti1348 – 13481L → R in CDLS1. 1 Publication
    VAR_019520
    Natural varianti1647 – 16471E → K in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036164
    Natural varianti1789 – 17891R → L in CDLS1. 1 Publication
    VAR_021600
    Natural varianti1803 – 18031D → V in CDLS1. 1 Publication
    VAR_021601
    Natural varianti1856 – 18561R → T in CDLS1. 1 Publication
    VAR_021602
    Natural varianti1897 – 18971Missing in CDLS1. 1 Publication
    VAR_064544
    Natural varianti2081 – 20811G → A in CDLS1. 1 Publication
    VAR_064545
    Natural varianti2090 – 20901S → I in CDLS1. 1 Publication
    VAR_064546
    Natural varianti2150 – 21501L → P in CDLS1. 1 Publication
    VAR_064547
    Natural varianti2298 – 22981R → C in CDLS1. 1 Publication
    VAR_021603
    Natural varianti2298 – 22981R → H in CDLS1. 1 Publication
    VAR_021604
    Natural varianti2312 – 23121G → R in CDLS1. 1 Publication
    VAR_021605
    Natural varianti2381 – 23811G → A in CDLS1. 1 Publication
    VAR_021606
    Natural varianti2390 – 23901A → T in CDLS1. 1 Publication
    VAR_021607
    Natural varianti2430 – 24301Y → C in CDLS1. 1 Publication
    VAR_019521
    Natural varianti2440 – 24401Y → H in CDLS1. 1 Publication
    VAR_021608

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1102 – 28041703Missing in isoform 3. 1 PublicationVSP_011091Add
    BLAST
    Alternative sequencei2684 – 269714SLRRS…DSTEL → VRRRRSQRISQRIT in isoform 2. 3 PublicationsVSP_011092Add
    BLAST
    Alternative sequencei2698 – 2804107Missing in isoform 2. 3 PublicationsVSP_011093Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ627032 mRNA. Translation: CAF25290.1.
    AJ640137 mRNA. Translation: CAG26691.1.
    BX538177 mRNA. Translation: CAD98051.1.
    BX538178 mRNA. Translation: CAD98052.1.
    BX640644 mRNA. Translation: CAE45790.1. Frameshift.
    AK126804 mRNA. Translation: BAC86701.1. Different initiation.
    AB019494 mRNA. Translation: BAA77335.1. Sequence problems.
    AB019602 mRNA. Translation: BAA77349.1. Sequence problems.
    BC033847 mRNA. Translation: AAH33847.1. Different initiation.
    CCDSiCCDS3920.1. [Q6KC79-1]
    CCDS47198.1. [Q6KC79-2]
    RefSeqiNP_056199.2. NM_015384.4. [Q6KC79-2]
    NP_597677.2. NM_133433.3. [Q6KC79-1]
    XP_005248340.1. XM_005248283.2.
    UniGeneiHs.481927.

    Genome annotation databases

    EnsembliENST00000282516; ENSP00000282516; ENSG00000164190. [Q6KC79-1]
    ENST00000448238; ENSP00000406266; ENSG00000164190. [Q6KC79-2]
    GeneIDi25836.
    KEGGihsa:25836.
    UCSCiuc003jkk.4. human. [Q6KC79-2]
    uc003jkl.4. human. [Q6KC79-1]
    uc003jkm.1. human. [Q6KC79-3]

    Polymorphism databases

    DMDMi50400865.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ627032 mRNA. Translation: CAF25290.1 .
    AJ640137 mRNA. Translation: CAG26691.1 .
    BX538177 mRNA. Translation: CAD98051.1 .
    BX538178 mRNA. Translation: CAD98052.1 .
    BX640644 mRNA. Translation: CAE45790.1 . Frameshift.
    AK126804 mRNA. Translation: BAC86701.1 . Different initiation.
    AB019494 mRNA. Translation: BAA77335.1 . Sequence problems.
    AB019602 mRNA. Translation: BAA77349.1 . Sequence problems.
    BC033847 mRNA. Translation: AAH33847.1 . Different initiation.
    CCDSi CCDS3920.1. [Q6KC79-1 ]
    CCDS47198.1. [Q6KC79-2 ]
    RefSeqi NP_056199.2. NM_015384.4. [Q6KC79-2 ]
    NP_597677.2. NM_133433.3. [Q6KC79-1 ]
    XP_005248340.1. XM_005248283.2.
    UniGenei Hs.481927.

    3D structure databases

    ProteinModelPortali Q6KC79.
    SMRi Q6KC79. Positions 1768-1856, 2063-2096, 2173-2201.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117363. 26 interactions.
    DIPi DIP-29199N.
    IntActi Q6KC79. 9 interactions.
    MINTi MINT-4103787.
    STRINGi 9606.ENSP00000282516.

    PTM databases

    PhosphoSitei Q6KC79.

    Polymorphism databases

    DMDMi 50400865.

    Proteomic databases

    MaxQBi Q6KC79.
    PaxDbi Q6KC79.
    PRIDEi Q6KC79.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000282516 ; ENSP00000282516 ; ENSG00000164190 . [Q6KC79-1 ]
    ENST00000448238 ; ENSP00000406266 ; ENSG00000164190 . [Q6KC79-2 ]
    GeneIDi 25836.
    KEGGi hsa:25836.
    UCSCi uc003jkk.4. human. [Q6KC79-2 ]
    uc003jkl.4. human. [Q6KC79-1 ]
    uc003jkm.1. human. [Q6KC79-3 ]

    Organism-specific databases

    CTDi 25836.
    GeneCardsi GC05P036876.
    GeneReviewsi NIPBL.
    HGNCi HGNC:28862. NIPBL.
    HPAi HPA040834.
    MIMi 122470. phenotype.
    608667. gene.
    neXtProti NX_Q6KC79.
    Orphaneti 329802. 5p13 microduplication syndrome.
    199. Cornelia de Lange syndrome.
    PharmGKBi PA134962343.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG128278.
    HOVERGENi HBG052626.
    InParanoidi Q6KC79.
    KOi K06672.
    OMAi RDICIEQ.
    OrthoDBi EOG7CZK4Q.
    PhylomeDBi Q6KC79.
    TreeFami TF313121.

    Enzyme and pathway databases

    Reactomei REACT_150421. Cohesin Loading onto Chromatin.

    Miscellaneous databases

    ChiTaRSi NIPBL. human.
    GeneWikii NIPBL.
    GenomeRNAii 25836.
    NextBioi 47141.
    PROi Q6KC79.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6KC79.
    Bgeei Q6KC79.
    CleanExi HS_NIPBL.
    Genevestigatori Q6KC79.

    Family and domain databases

    Gene3Di 1.25.10.10. 3 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR026003. Cohesin_HEAT.
    IPR024986. Nipped-B_C.
    [Graphical view ]
    Pfami PF12765. Cohesin_HEAT. 1 hit.
    PF12830. Nipped-B_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "NIPBL, encoding a homolog of fungal Scc2-type sister chromatid cohesion proteins and fly Nipped-B, is mutated in Cornelia de Lange syndrome."
      Tonkin E.T., Wang T.-J., Lisgo S., Bamshad M.J., Strachan T.
      Nat. Genet. 36:636-641(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS CDLS1 ILE-1206 DEL; ARG-1311; ARG-1348 AND CYS-2430.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1175.
      Tissue: Endometrium.
    3. "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] OF 128-2804 (ISOFORM 3).
      Tissue: Cerebellum.
    4. Aihara T., Yasuo M., Kumiko K., Sasaki Y., Imaoka S., Monden M., Nakamura Y.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 421-2804 (ISOFORMS 1 AND 2).
      Tissue: Testis.
    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] OF 2411-2697 (ISOFORM 2).
      Tissue: Urinary bladder.
    6. Cited for: TISSUE SPECIFICITY, INVOLVEMENT IN CDLS1.
    7. "The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
      Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
      Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX5.
    8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318; THR-713; THR-746; SER-1096; SER-2658 AND THR-2667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-162; SER-306; SER-350; SER-912; SER-1089; SER-1090; SER-1096; SER-1150; SER-1152; SER-1154; SER-1160; SER-2509; SER-2511; SER-2513; SER-2515 AND SER-2658, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2667 AND SER-2672 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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].
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1089; SER-1090; SER-1096; SER-1150; SER-1154; SER-1160 AND SER-2658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation."
      Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.
      Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX5, MUTAGENESIS OF VAL-1003 AND LEU-1005.
    18. "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-256; SER-318; SER-350; SER-2658 AND SER-2672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-350; SER-1096; SER-1150; SER-1152; SER-1154; SER-1160; SER-2509; SER-2511; SER-2513; SER-2515; SER-2658; THR-2667 AND SER-2672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "NIPBL mutational analysis in 120 individuals with Cornelia de Lange syndrome and evaluation of genotype-phenotype correlations."
      Gillis L.A., McCallum J., Kaur M., DeScipio C., Yaeger D., Mariani A., Kline A.D., Li H., Devoto M., Jackson L.G., Krantz I.D.
      Am. J. Hum. Genet. 75:610-623(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CDLS1 GLY-1246; PRO-1312; LEU-1789; VAL-1803; THR-1856; CYS-2298; HIS-2298; ARG-2312; ALA-2381; THR-2390 AND HIS-2440, VARIANTS SER-674 AND VAL-1206.
    22. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-1647.
    23. "Mutations and variants in the cohesion factor genes NIPBL, SMC1A, and SMC3 in a cohort of 30 unrelated patients with Cornelia de Lange syndrome."
      Pie J., Gil-Rodriguez M.C., Ciero M., Lopez-Vinas E., Ribate M.P., Arnedo M., Deardorff M.A., Puisac B., Legarreta J., de Karam J.C., Rubio E., Bueno I., Baldellou A., Calvo M.T., Casals N., Olivares J.L., Losada A., Hegardt F.G.
      , Krantz I.D., Gomez-Puertas P., Ramos F.J.
      Am. J. Med. Genet. A 152:924-929(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CDLS1 ASN-1897 DEL; ALA-2081; ILE-2090 AND PRO-2150.

    Entry informationi

    Entry nameiNIPBL_HUMAN
    AccessioniPrimary (citable) accession number: Q6KC79
    Secondary accession number(s): Q6KCD6
    , Q6N080, Q6ZT92, Q7Z2E6, Q8N4M5, Q9Y6Y3, Q9Y6Y4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 124 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 5
      Human chromosome 5: 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