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Q6KC79 (NIPBL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nipped-B-like protein
Alternative name(s):
Delangin
SCC2 homolog
Gene names
Name:NIPBL
Synonyms:IDN3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2804 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts directly with CBX5 via the PxVxL motif. Ref.7 Ref.17

Subcellular location

Nucleus By similarity.

Tissue specificity

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. Ref.1 Ref.6

Developmental stage

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. Ref.1

Domain

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.6 Ref.21 Ref.23

Sequence similarities

Belongs to the SCC2/Nipped-B family.

Contains 5 HEAT repeats.

Sequence caution

The sequence AAH33847.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA77335.1 differs from that shown. Reason: Chimeric cDNA.

The sequence BAA77349.1 differs from that shown. Reason: Chimeric cDNA.

The sequence BAC86701.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAE45790.1 differs from that shown. Reason: Frameshift at position 278.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from mutant phenotype PubMed 8291537. Source: BHF-UCL

cellular protein localization

Inferred from mutant phenotype PubMed 17468178. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 17468178. Source: UniProtKB

cellular response to X-ray

Inferred from mutant phenotype PubMed 17468178. Source: UniProtKB

cognition

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

developmental growth

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

ear morphogenesis

Inferred from mutant phenotype PubMed 8291537. Source: BHF-UCL

embryonic digestive tract morphogenesis

Inferred from mutant phenotype PubMed 19242925PubMed 8291537. Source: BHF-UCL

embryonic forelimb morphogenesis

Inferred from mutant phenotype PubMed 19242925PubMed 8291537. Source: BHF-UCL

embryonic viscerocranium morphogenesis

Inferred from electronic annotation. Source: Ensembl

external genitalia morphogenesis

Inferred from mutant phenotype Ref.6PubMed 19242925. Source: BHF-UCL

eye morphogenesis

Inferred from mutant phenotype PubMed 8291537. Source: BHF-UCL

face morphogenesis

Inferred from mutant phenotype Ref.6PubMed 19242925. Source: BHF-UCL

fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

forelimb morphogenesis

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

gall bladder development

Inferred from mutant phenotype PubMed 19242925. Source: BHF-UCL

heart morphogenesis

Inferred from mutant phenotype PubMed 8291537. Source: BHF-UCL

maintenance of mitotic sister chromatid cohesion

Inferred from mutant phenotype PubMed 16682347. Source: UniProtKB

metanephros development

Non-traceable author statement Ref.1. Source: BHF-UCL

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic sister chromatid cohesion

Inferred from mutant phenotype PubMed 16100726. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18854353. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18854353. Source: BHF-UCL

outflow tract morphogenesis

Inferred from mutant phenotype PubMed 19242925. Source: BHF-UCL

positive regulation of histone deacetylation

Inferred from direct assay PubMed 18854353. Source: BHF-UCL

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of ossification

Inferred from electronic annotation. Source: Ensembl

regulation of developmental growth

Inferred from mutant phenotype PubMed 19242925. Source: BHF-UCL

regulation of embryonic development

Inferred from mutant phenotype PubMed 19242925. Source: BHF-UCL

regulation of hair cycle

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

sensory perception of sound

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

uterus morphogenesis

Inferred from mutant phenotype PubMed 19242925. Source: BHF-UCL

   Cellular_componentSMC loading complex

Inferred from direct assay PubMed 16682347. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 16802858. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

chromo shadow domain binding

Inferred from physical interaction Ref.7. Source: BHF-UCL

histone deacetylase binding

Inferred from physical interaction PubMed 18854353. Source: BHF-UCL

protein C-terminus binding

Inferred from physical interaction PubMed 17577209. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 16802858. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16682347. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6KC79-1)

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.
Isoform 2 (identifier: Q6KC79-2)

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.
Isoform 3 (identifier: Q6KC79-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1102-2804: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 28042804Nipped-B-like protein
PRO_0000218596

Regions

Repeat1767 – 180539HEAT 1
Repeat1843 – 188139HEAT 2
Repeat1945 – 198440HEAT 3
Repeat2227 – 226741HEAT 4
Repeat2313 – 235139HEAT 5
Motif996 – 100914PxVxL motif
Compositional bias418 – 46245Gln-rich

Amino acid modifications

Modified residue1501Phosphoserine Ref.12
Modified residue1621Phosphoserine Ref.12
Modified residue2561Phosphoserine Ref.18
Modified residue2801Phosphoserine By similarity
Modified residue3061Phosphoserine Ref.12
Modified residue3181Phosphoserine Ref.8 Ref.18
Modified residue3501Phosphoserine Ref.12 Ref.18 Ref.20
Modified residue7131Phosphothreonine Ref.8
Modified residue7461Phosphothreonine Ref.8
Modified residue9121Phosphoserine Ref.12
Modified residue10821N6-acetyllysine By similarity
Modified residue10891Phosphoserine Ref.12 Ref.15
Modified residue10901Phosphoserine Ref.12 Ref.15
Modified residue10961Phosphoserine Ref.8 Ref.12 Ref.15 Ref.20
Modified residue11501Phosphoserine Ref.12 Ref.15 Ref.20
Modified residue11521Phosphoserine Ref.12 Ref.20
Modified residue11541Phosphoserine Ref.12 Ref.15 Ref.20
Modified residue11601Phosphoserine Ref.12 Ref.15 Ref.20
Modified residue25091Phosphoserine Ref.12 Ref.20
Modified residue25111Phosphoserine Ref.12 Ref.20
Modified residue25131Phosphoserine Ref.12 Ref.20
Modified residue25151Phosphoserine Ref.12 Ref.20
Modified residue26581Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.18 Ref.20
Modified residue26671Phosphothreonine Ref.8 Ref.12 Ref.20
Modified residue26721Phosphoserine Ref.12 Ref.18 Ref.20

Natural variations

Alternative sequence1102 – 28041703Missing in isoform 3.
VSP_011091
Alternative sequence2684 – 269714SLRRS…DSTEL → VRRRRSQRISQRIT in isoform 2.
VSP_011092
Alternative sequence2698 – 2804107Missing in isoform 2.
VSP_011093
Natural variant1351S → N.
Corresponds to variant rs3822471 [ dbSNP | Ensembl ].
VAR_019518
Natural variant2611S → A.
Corresponds to variant rs16903425 [ dbSNP | Ensembl ].
VAR_038411
Natural variant3841N → S.
Corresponds to variant rs2291703 [ dbSNP | Ensembl ].
VAR_038412
Natural variant6741N → S. Ref.21
Corresponds to variant rs3822471 [ dbSNP | Ensembl ].
VAR_021596
Natural variant12061I → V. Ref.21
VAR_021597
Natural variant12061Missing in CDLS1. Ref.1
VAR_038413
Natural variant12461A → G in CDLS1. Ref.21
VAR_021598
Natural variant13111C → R in CDLS1. Ref.1
VAR_019519
Natural variant13121L → P in CDLS1. Ref.21
VAR_021599
Natural variant13481L → R in CDLS1. Ref.1
VAR_019520
Natural variant16471E → K in a breast cancer sample; somatic mutation. Ref.22
VAR_036164
Natural variant17891R → L in CDLS1. Ref.21
VAR_021600
Natural variant18031D → V in CDLS1. Ref.21
VAR_021601
Natural variant18561R → T in CDLS1. Ref.21
VAR_021602
Natural variant18971Missing in CDLS1. Ref.23
VAR_064544
Natural variant20811G → A in CDLS1. Ref.23
VAR_064545
Natural variant20901S → I in CDLS1. Ref.23
VAR_064546
Natural variant21501L → P in CDLS1. Ref.23
VAR_064547
Natural variant22981R → C in CDLS1. Ref.21
VAR_021603
Natural variant22981R → H in CDLS1. Ref.21
VAR_021604
Natural variant23121G → R in CDLS1. Ref.21
VAR_021605
Natural variant23811G → A in CDLS1. Ref.21
VAR_021606
Natural variant23901A → T in CDLS1. Ref.21
VAR_021607
Natural variant24301Y → C in CDLS1. Ref.1
VAR_019521
Natural variant24401Y → H in CDLS1. Ref.21
VAR_021608

Experimental info

Mutagenesis10031V → E: Abolishes interaction with CBX5; when associated with Glu-1005. Ref.17
Mutagenesis10051L → E: Abolishes interaction with CBX5; when associated with Glu-1003. Ref.17
Sequence conflict3181S → F Ref.3
Sequence conflict5481A → T in CAD98051. Ref.2
Sequence conflict5481A → T in CAD98052. Ref.2
Sequence conflict5741N → S in CAD98051. Ref.2
Sequence conflict5741N → S in CAD98052. Ref.2
Sequence conflict6481T → I in CAD98051. Ref.2
Sequence conflict6481T → I in CAD98052. Ref.2
Sequence conflict11721M → K in CAD98051. Ref.2
Sequence conflict11721M → K in CAD98052. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) (IDN3-A) [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: C275425DF53058A3

FASTA2,804316,051
        10         20         30         40         50         60 
MNGDMPHVPI TTLAGIASLT DLLNQLPLPS PLPATTTKSL LFNARIAEEV NCLLACRDDN 

        70         80         90        100        110        120 
LVSQLVHSLN QVSTDHIELK DNLGSDDPEG DIPVLLQAVL ARSPNVFREK SMQNRYVQSG 

       130        140        150        160        170        180 
MMMSQYKLSQ NSMHSSPASS NYQQTTISHS PSSRFVPPQT SSGNRFMPQQ NSPVPSPYAP 

       190        200        210        220        230        240 
QSPAGYMPYS HPSSYTTHPQ MQQASVSSPI VAGGLRNIHD NKVSGPLSGN SANHHADNPR 

       250        260        270        280        290        300 
HGSSEDYLHM VHRLSSDDGD SSTMRNAASF PLRSPQPVCS PAGSEGTPKG SRPPLILQSQ 

       310        320        330        340        350        360 
SLPCSSPRDV PPDILLDSPE RKQKKQKKMK LGKDEKEQSE KAAMYDIISS PSKDSTKLTL 

       370        380        390        400        410        420 
RLSRVRSSDM DQQEDMISGV ENSNVSENDI PFNVQYPGQT SKTPITPQDI NRPLNAAQCL 

       430        440        450        460        470        480 
SQQEQTAFLP ANQVPVLQQN TSVAAKQPQT SVVQNQQQIS QQGPIYDEVE LDALAEIERI 

       490        500        510        520        530        540 
ERESAIERER FSKEVQDKDK PLKKRKQDSY PQEAGGATGG NRPASQETGS TGNGSRPALM 

       550        560        570        580        590        600 
VSIDLHQAGR VDSQASITQD SDSIKKPEEI KQCNDAPVSV LQEDIVGSLK STPENHPETP 

       610        620        630        640        650        660 
KKKSDPELSK SEMKQSESRL AESKPNENRL VETKSSENKL ETKVETQTEE LKQNESRTTE 

       670        680        690        700        710        720 
CKQNESTIVE PKQNENRLSD TKPNDNKQNN GRSETTKSRP ETPKQKGESR PETPKQKSDG 

       730        740        750        760        770        780 
HPETPKQKGD GRPETPKQKG ESRPETPKQK NEGRPETPKH RHDNRRDSGK PSTEKKPEVS 

       790        800        810        820        830        840 
KHKQDTKSDS PRLKSERAEA LKQRPDGRSV SESLRRDHDN KQKSDDRGES ERHRGDQSRV 

       850        860        870        880        890        900 
RRPETLRSSS RNEHGIKSDS SKTDKLERKH RHESGDSRER PSSGEQKSRP DSPRVKQGDS 

       910        920        930        940        950        960 
NKSRSDKLGF KSPTSKDDKR TEGNKSKVDT NKAHPDNKAE FPSYLLGGRS GALKNFVIPK 

       970        980        990       1000       1010       1020 
IKRDKDGNVT QETKKMEMKG EPKDKVEKIG LVEDLNKGAK PVVVLQKLSL DDVQKLIKDR 

      1030       1040       1050       1060       1070       1080 
EDKSRSSLKP IKNKPSKSNK GSIDQSVLKE LPPELLAEIE STMPLCERVK MNKRKRSTVN 

      1090       1100       1110       1120       1130       1140 
EKPKYAEISS DEDNDSDEAF ESSRKRHKKD DDKAWEYEER DRRSSGDHRR SGHSHEGRRS 

      1150       1160       1170       1180       1190       1200 
SGGGRYRNRS PSDSDMEDYS PPPSLSEVAR KMKKKEKQKK RKAYEPKLTP EEMMDSSTFK 

      1210       1220       1230       1240       1250       1260 
RFTASIENIL DNLEDMDFTA FGDDDEIPQE LLLGKHQLNE LGSESAKIKA MGIMDKLSTD 

      1270       1280       1290       1300       1310       1320 
KTVKVLNILE KNIQDGSKLS TLLNHNNDTE EEERLWRDLI MERVTKSADA CLTTINIMTS 

      1330       1340       1350       1360       1370       1380 
PNMPKAVYIE DVIERVIQYT KFHLQNTLYP QYDPVYRLDP HGGGLLSSKA KRAKCSTHKQ 

      1390       1400       1410       1420       1430       1440 
RVIVMLYNKV CDIVSSLSEL LEIQLLTDTT ILQVSSMGIT PFFVENVSEL QLCAIKLVTA 

      1450       1460       1470       1480       1490       1500 
VFSRYEKHRQ LILEEIFTSL ARLPTSKRSL RNFRLNSSDM DGEPMYIQMV TALVLQLIQC 

      1510       1520       1530       1540       1550       1560 
VVHLPSSEKD SNAEEDSNKK IDQDVVITNS YETAMRTAQN FLSIFLKKCG SKQGEEDYRP 

      1570       1580       1590       1600       1610       1620 
LFENFVQDLL STVNKPEWPA AELLLSLLGR LLVHQFSNKS TEMALRVASL DYLGTVAARL 

      1630       1640       1650       1660       1670       1680 
RKDAVTSKMD QGSIERILKQ VSGGEDEIQQ LQKALLDYLD ENTETDPSLV FSRKFYIAQW 

      1690       1700       1710       1720       1730       1740 
FRDTTLETEK AMKSQKDEES SEGTHHAKEI ETTGQIMHRA ENRKKFLRSI IKTTPSQFST 

      1750       1760       1770       1780       1790       1800 
LKMNSDTVDY DDACLIVRYL ASMRPFAQSF DIYLTQILRV LGENAIAVRT KAMKCLSEVV 

      1810       1820       1830       1840       1850       1860 
AVDPSILARL DMQRGVHGRL MDNSTSVREA AVELLGRFVL CRPQLAEQYY DMLIERILDT 

      1870       1880       1890       1900       1910       1920 
GISVRKRVIK ILRDICIEQP TFPKITEMCV KMIRRVNDEE GIKKLVNETF QKLWFTPTPH 

      1930       1940       1950       1960       1970       1980 
NDKEAMTRKI LNITDVVAAC RDTGYDWFEQ LLQNLLKSEE DSSYKPVKKA CTQLVDNLVE 

      1990       2000       2010       2020       2030       2040 
HILKYEESLA DSDNKGVNSG RLVACITTLF LFSKIRPQLM VKHAMTMQPY LTTKCSTQND 

      2050       2060       2070       2080       2090       2100 
FMVICNVAKI LELVVPLMEH PSETFLATIE EDLMKLIIKY GMTVVQHCVS CLGAVVNKVT 

      2110       2120       2130       2140       2150       2160 
QNFKFVWACF NRYYGAISKL KSQHQEDPNN TSLLTNKPAL LRSLFTVGAL CRHFDFDLED 

      2170       2180       2190       2200       2210       2220 
FKGNSKVNIK DKVLELLMYF TKHSDEEVQT KAIIGLGFAF IQHPSLMFEQ EVKNLYNNIL 

      2230       2240       2250       2260       2270       2280 
SDKNSSVNLK IQVLKNLQTY LQEEDTRMQQ ADRDWKKVAK QEDLKEMGDV SSGMSSSIMQ 

      2290       2300       2310       2320       2330       2340 
LYLKQVLEAF FHTQSSVRHF ALNVIALTLN QGLIHPVQCV PYLIAMGTDP EPAMRNKADQ 

      2350       2360       2370       2380       2390       2400 
QLVEIDKKYA GFIHMKAVAG MKMSYQVQQA INTCLKDPVR GFRQDESSSA LCSHLYSMIR 

      2410       2420       2430       2440       2450       2460 
GNRQHRRAFL ISLLNLFDDT AKTDVTMLLY IADNLACFPY QTQEEPLFIM HHIDITLSVS 

      2470       2480       2490       2500       2510       2520 
GSNLLQSFKE SMVKDKRKER KSSPSKENES SDSEEEVSRP RKSRKRVDSD SDSDSEDDIN 

      2530       2540       2550       2560       2570       2580 
SVMKCLPENS APLIEFANVS QGILLLLMLK QHLKNLCGFS DSKIQKYSPS ESAKVYDKAI 

      2590       2600       2610       2620       2630       2640 
NRKTGVHFHP KQTLDFLRSD MANSKITEEV KRSIVKQYLD FKLLMEHLDP DEEEEEGEVS 

      2650       2660       2670       2680       2690       2700 
ASTNARNKAI TSLLGGGSPK NNTAAETEDD ESDGEDRGGG TSGSLRRSKR NSDSTELAAQ 

      2710       2720       2730       2740       2750       2760 
MNESVDVMDV IAICCPKYKD RPQIARVVQK TSSGFSVQWM AGSYSGSWTE AKRRDGRKLV 

      2770       2780       2790       2800 
PWVDTIKESD IIYKKIALTS ANKLTNKVVQ TLRSLYAAKD GTSS 

« Hide

Isoform 2 (B) (IDN3-B) [UniParc].

Checksum: 42207C9622A3C01D
Show »

FASTA2,697304,344
Isoform 3 [UniParc].

Checksum: 0344321AFFE6ACFA
Show »

FASTA1,101122,367

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Cornelia de Lange syndrome is caused by mutations in NIPBL, the human homolog of Drosophila melanogaster Nipped-B."
Krantz I.D., McCallum J., DeScipio C., Kaur M., Gillis L.A., Yaeger D., Jukofsky L., Wasserman N., Bottani A., Morris C.A., Nowaczyk M.J.M., Toriello H., Bamshad M.J., Carey J.C., Rappaport E., Kawauchi S., Lander A.D., Calof A.L. expand/collapse author list , Li H.-H., Devoto M., Jackson L.G.
Nat. Genet. 36:631-635(2004) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3920.1. [Q6KC79-1]
CCDS47198.1. [Q6KC79-2]
RefSeqNP_056199.2. NM_015384.4. [Q6KC79-2]
NP_597677.2. NM_133433.3. [Q6KC79-1]
XP_005248340.1. XM_005248283.2.
UniGeneHs.481927.

3D structure databases

ProteinModelPortalQ6KC79.
SMRQ6KC79. Positions 1768-1856, 2063-2096, 2173-2201.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117363. 26 interactions.
DIPDIP-29199N.
IntActQ6KC79. 9 interactions.
MINTMINT-4103787.
STRING9606.ENSP00000282516.

PTM databases

PhosphoSiteQ6KC79.

Polymorphism databases

DMDM50400865.

Proteomic databases

MaxQBQ6KC79.
PaxDbQ6KC79.
PRIDEQ6KC79.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282516; ENSP00000282516; ENSG00000164190. [Q6KC79-1]
ENST00000448238; ENSP00000406266; ENSG00000164190. [Q6KC79-2]
GeneID25836.
KEGGhsa:25836.
UCSCuc003jkk.4. human. [Q6KC79-2]
uc003jkl.4. human. [Q6KC79-1]
uc003jkm.1. human. [Q6KC79-3]

Organism-specific databases

CTD25836.
GeneCardsGC05P036876.
GeneReviewsNIPBL.
HGNCHGNC:28862. NIPBL.
HPAHPA040834.
MIM122470. phenotype.
608667. gene.
neXtProtNX_Q6KC79.
Orphanet329802. 5p13 microduplication syndrome.
199. Cornelia de Lange syndrome.
PharmGKBPA134962343.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG128278.
HOVERGENHBG052626.
InParanoidQ6KC79.
KOK06672.
OMARDICIEQ.
OrthoDBEOG7CZK4Q.
PhylomeDBQ6KC79.
TreeFamTF313121.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ6KC79.
BgeeQ6KC79.
CleanExHS_NIPBL.
GenevestigatorQ6KC79.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026003. Cohesin_HEAT.
IPR024986. Nipped-B_C.
[Graphical view]
PfamPF12765. Cohesin_HEAT. 1 hit.
PF12830. Nipped-B_C. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

ChiTaRSNIPBL. human.
GeneWikiNIPBL.
GenomeRNAi25836.
NextBio47141.
PROQ6KC79.
SOURCESearch...

Entry information

Entry nameNIPBL_HUMAN
AccessionPrimary (citable) accession number: Q6KC79
Secondary accession number(s): Q6KCD6 expand/collapse secondary AC list , Q6N080, Q6ZT92, Q7Z2E6, Q8N4M5, Q9Y6Y3, Q9Y6Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM