ID A0A2K5CQ19_AOTNA Unreviewed; 2804 AA.
AC A0A2K5CQ19;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Nipped-B protein {ECO:0000256|RuleBase:RU364107};
GN Name=NIPBL {ECO:0000313|Ensembl:ENSANAP00000010790.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000010790.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000010790.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364107}.
CC -!- SIMILARITY: Belongs to the SCC2/Nipped-B family.
CC {ECO:0000256|ARBA:ARBA00009252, ECO:0000256|RuleBase:RU364107}.
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DR RefSeq; XP_012315417.1; XM_012459994.1.
DR STRING; 37293.ENSANAP00000010790; -.
DR Ensembl; ENSANAT00000028594.1; ENSANAP00000010790.1; ENSANAG00000023189.1.
DR GeneID; 105722491; -.
DR CTD; 25836; -.
DR GeneTree; ENSGT00390000010427; -.
DR OMA; KQNENRM; -.
DR OrthoDB; 1409889at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0032039; C:integrator complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0090694; C:Scc2-Scc4 cohesin loading complex; IEA:Ensembl.
DR GO; GO:0070087; F:chromo shadow domain binding; IEA:Ensembl.
DR GO; GO:0061775; F:cohesin loader activity; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0036033; F:mediator complex binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR GO; GO:0050890; P:cognition; IEA:Ensembl.
DR GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR GO; GO:0042471; P:ear morphogenesis; IEA:Ensembl.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IEA:Ensembl.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0035261; P:external genitalia morphogenesis; IEA:Ensembl.
DR GO; GO:0048592; P:eye morphogenesis; IEA:Ensembl.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0061010; P:gallbladder development; IEA:Ensembl.
DR GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IEA:Ensembl.
DR GO; GO:0061780; P:mitotic cohesin loading; IEA:InterPro.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:2001224; P:positive regulation of neuron migration; IEA:Ensembl.
DR GO; GO:0045778; P:positive regulation of ossification; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0042634; P:regulation of hair cycle; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0061038; P:uterus morphogenesis; IEA:Ensembl.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026003; Cohesin_HEAT.
DR InterPro; IPR024986; Nipped-B_C.
DR InterPro; IPR033031; Scc2/Nipped-B.
DR PANTHER; PTHR21704:SF18; NIPPED-B-LIKE PROTEIN; 1.
DR PANTHER; PTHR21704; NIPPED-B-LIKE PROTEIN DELANGIN SCC2-RELATED; 1.
DR Pfam; PF12765; Cohesin_HEAT; 1.
DR Pfam; PF12830; Nipped-B_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU364107};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364107};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU364107}.
FT DOMAIN 2275..2455
FT /note="Sister chromatid cohesion C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12830"
FT REGION 128..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2473..2520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2651..2696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2676..2693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2804 AA; 316317 MW; A772CCF6476B70A5 CRC64;
MNGDMPHVPI TTLAGIASLT DLLNQLPLPS PLPATTTKSL LFNARIAEEV NCLLACRDDS
LVSQLVHSLN QVSTDHIELK DNLGSDDPEG DIPVLLQAVL ARSPNVFREK SMQNRYVQSG
MMMSQYKLSQ NSMHSSPASS NYQQTTISHS PSSRFVPPQT SSGNRFMPQQ NSPVPSPYAP
QSPAGYMPYS HPSSYTTHPQ MQQASVSSPI VAGGLRNIHD NKVSGPLSGN SANHHADNPR
HGSSEDYLHM VHRLSSDDGD SSTMRNAASF PLRSPQPVCS PAGSDGTPKG SRPPLILQSQ
SLPCSSPRDV PPDILLDSPE RKQKKQKKMK LGKDEKEQSE KAAMYDIISS PSKDSTKLTL
RLSRVRSSDM DQQEDMTSGM ENSNVSENDI PFNVQYPGQT SKTPITPQDV NRPLNAAPCL
SQQEQTAFLP ANQVPVLQQN TSVATKQPQT SVVQNQPQVS QQGPIYDEVE LDALAEIERI
ERESAIERER FSKEVQDKDK PLKKRKQDSY PQEAGGATGG NRPASQETGS TGNGSRPALM
VSIDLHQAGR VDSQASITQD SDSIKKPEEI KQCNDAPISV LQEDVIGSLK PTPENHPETP
KKKSDPELSK SEMKQSESRL SESKPNENRL VETKSSENKL ETKVETQTEE LKQNESRTTE
CKQNESTTVE PKQNENRLSD TKPNDNKQNN GRSETTKSRP ETPKQKGESR PETPKQKSDG
RPETPKQKGD GRPETPKQKV ESRPETPKQK NEGRPETPKH RHDNRRDSGK PSTEKKPEVS
KHKQDVKSDS PRLKSERAEA LKQRPDGRSI CESLRRDHDN KQKSDDRGES ERHRGDQSRV
RRPETLRSSS RNEHGIKSDS SKTDKLERKH RHESGDSRER PSSGEQKSRP DSPRVKQGDS
NKSRCDKPGF KSPNSRDDKR TESNKSKVDT NKAHPDNKAE FPSYLLGGRS GALKNFVIPK
IKRDKDGNIT QETKKMEMKG EQKDKVEKMG LVEDLNKGAK PVVVLQKLSL DDVQKLIKDR
EDKSRSSLKP IRNKPSKSNK GSIDQSVLKE LPPELLAEIE STMPLCERVK MNKRKRSTVN
EKPKYAEISS DEDNDSDEAF ESSRKRHKKD DDKAWEYEER DRRSSGDHRR SGHSHEGRRS
SGGGRYRNRS PSDSDMEDYS PPPSLSEVAR KMKKKEKQKK RKAYEPKLTP EEMMDSSTFK
RFTASIENIL DNLEDMDFTA FGDDDEIPQE LLLGKHQLNE LGSESAKIKA MGIMDKLSTD
KTVKVLNILE KNIQDGSKLS TLLNHNNDTE EEERLWRDLI MERVTKSADA CLTTINIMTS
PNMPKAVYIE DVIERVIQYT KFHLQNTLYP QYDPVYRLDP HGGGLLSSKA KRAKCSTHKQ
RVIVMLYNKV CDIVSSLSEL LEIQLLTDTT ILQVSSMGIT PFFVENVSEL QLCAIKLVTA
VFSRYEKHRQ LILEEIFTSL ARLPTSKRSL RNFRLNSSDM DGEPMYIQMV TALVLQLIQC
VVHLPSSEKD SNAEEDSNKK VDQDVVITNS YETAMRTAQN FLSIFLKKCG SKQGEEDYRP
LFENFVQDLL STVNKPEWPA AELLLSLLGR LLVHQFSNKS TEMALRVASL DYLGTVAARL
RKDAVTSKMD QGSIERILKQ VSGGEDEIQQ LQKALLDYLD ENTETDPSLV FSRKFYIAQW
FRDTTLETEK AMKSQKDEES SEGTHHAKEI ETTGQIMHRA ENRKKFLRSI IKTTPSQFST
LKMNSDTVDY DDACLIVRYL ASMRPFAQSF DIYLTQILRV LGENAIAVRT KAMKCLSEVV
AVDPSILARL DMQRGVHGRL MDNSTSVREA AVELLGRFVL CRPQLAEQYY DMLIERILDT
GISVRKRVIK ILRDICIEQP TFPKITEMCV KMIRRVNDEE GIKKLVNETF QKLWFTPTPH
NDKEAMTRKI LNITDVVAAC RDTGYDWFEQ LLQNLLKSEE DSSYKPVKKA CTQLVDNLVE
HILKYEESLA DSDNKGVNSG RLVACITTLF LFSKIRPQLM VKHAMTMQPY LTTKCSTQND
FMVICNVAKI LELVVPLMEH PSETFLATIE EDLMKLIIKY GMTVVQHCVS CLGAVVNKVT
QNFKFVWACF NRYYGAISKL KSQHQEDPNN TSLLTNKPAL LRSLFTVGAL CRHFDFDLED
FKGNSKVNIK DKVLELLMYF TKHSDEEVQT KAIIGLGFAF IQHPSLMFEQ EVKNLYNNIL
SDKNSSVNLK IQVLKNLQTY LQEEDTRMQQ ADRDWKKVAK QEDLKEMGDV SSGMSSSIMQ
LYLKQVLEAF FHTQSSVRHF ALNVIALTLN QGLIHPVQCV PYLIAMGTDP EPAMRNKADQ
QLVEIDKKYA GFIHMKAVAG MKMSYQVQQA INTCLKDPVR GFRQDESSSA LCSHLYSMIR
GNRQHRRAFL ISLLNLFDDT AKTEVTMLLY IADNLACFPY QTQEEPLFIM HHIDITLSVS
GSNLLQSFKE SMVKDKRKER KSSPSKENES SESEEEVSRP RKSRKRVDSD SDSDSEDDIN
SVMKCLPENS APLIEFANVS QGILLLLMLK QHLKNLCGFS DSKIQKYSPS ESAKVYDKAI
NRKTGVHFHP KQTLDFLRSD MANSKITEEV KRNIVKQYLD FKLLMEHLDP DEEEEEGEVS
ASTNARNKAI TSLLGGGSPK NNTAAETEDD ESDGEDRGGG TSGSLRRSKR NSDSTELAAQ
MNESVDVMDV IAICCPKYKD RPQIARVVQK TSNGFSVQWM AGSYSGSWTE AKRRDGRKLV
PWVDTIKESD IIYKKIALTS ANKLTNKVVQ TLRSLYAAKD GTSS
//
