ul_8535----
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PPBD protein
Gene name PIN1( Description: protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1. )
Synonyms DOD; EC 5.2.1.8; PPIase Pin1; Rotamase Pin1; UBL5
GO annotations GO_component: nucleus [PMID 8606777]
GO_function:isomerase activity; peptidyl-prolyl cis-trans isomerase activity; protein binding [PMID 11470801]
GO_process: cell cycle; protein folding; regulation of mitosis [PMID 10391244]
RefSeq accession NP_006212
SwissProt accession Q13526
Substrate protein
Gene name POLR2A( Description: polymerase (RNA) II (DNA directed) polypeptide A, 220kDa. )
Synonyms DNA-directed RNA polymerase II subunit A; DNA-directed RNA polymerase III largest subunit; EC 2.7.7.6; MGC75453; POLR2; POLRA; RNA polymerase II subunit B1; RPB1; RPBh1; RPO2; RPOL2; RpIILS; hRPB220; hsRPB1
GO annotations GO_component: DNA-directed RNA polymerase II, core complex [PMID 2999107] [PMID 3145407]; nucleus [PMID 7622068]
GO_function:DNA binding [PMID 7622068]; DNA-directed RNA polymerase activity [PMID 3145407] [PMID 7622068]; metal ion binding; protein binding [PMID 10075709] [PMID 10944529]; transferase activity; zinc ion binding
GO_process: regulation of transcription, DNA-dependent [PMID 7622068]; transcription; transcription from RNA polymerase II promoter [PMID 7622068]; transcription, DNA-dependent [PMID 3145407]
RefSeq accession NP_000928
SwissProt accession P24928
Sequence:(RefSeq accession:NP_000928; substrate region highlighted if known)
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MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP
RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL VKTMKVLRCV CFFCSKLLVD
SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG KNICEGGEEM DNKFGVEQPE GDEDLTKEKG
HGGCGRYQPR IRRSGLELYA EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP
RYARPEWMIV TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA
HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV RGNLMGKRVD
FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID RLQELVRRGN SQYPGAKYII
RDNGDRIDLR FHPKPSDLHL QTGYKVERHM CDGDIVIFNR QPTLHKMSMM GHRVRILPWS
TFRLNLSVTT PYNADFDGDE MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD
TLTAVRKFTK RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI
NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG SLVHISYLEM
GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ DIQNTIKKAK QDVIEVIEKA
HNNELEPTPG NTLRQTFENQ VNRILNDARD KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN
ISQVIAVVGQ QNVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA
MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES
VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN ELEREFERMR
EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL PSDLHPIKVV EGVKELSKKL
VIVNGDDPLS RQAQENATLL FNIHLRSTLC SRRMAEEFRL SGEAFDWLLG EIESKFNQAI
AHPGEMVGAL AAQSLGEPAT QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT
VFLLGQSARD AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP
DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD NAEKLVLRIR
IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG IEQISKVYMH LPQTDNKKKI
IITEDGEFKA LQEWILETDG VSLMRVLSEK DVDPVRTTSN DIVEIFTVLG IEAVRKALER
ELYHVISFDG SYVNYRHLAL LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM
EAAAHGESDP MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG
MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA ASDASGFSPG
YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY EPRSPGGYTP QSPSYSPTSP
SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP
TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS
YSPTSPNYSP TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT
SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPTSPKYT PTSPSYSPSS PEYTPTSPKY
SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP VYTPTSPKYS PTSPTYSPTS
PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT SPTYSLTSPA ISPDDSDEEN
Records:
Category Evidence Reference
A Structure Verdecia MA, Bowman ME, Lu KP, Hunter T, Noel JP., Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan., [10932246]
A Structure Li Z, Li H, Devasahayam G, Gemmill T, Chaturvedi V, Hanes SD, Van Roey P., The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility., [15835905]
End of Record Details