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Protein Page:
XRN1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
XRN1 Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA. Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). Belongs to the 5'-3' exonuclease family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.11.-; Ribonuclease
Cellular Component: membrane; cytosol
Molecular Function: 5'-3' exonuclease activity; protein binding; DNA binding
Biological Process: RNA metabolic process; rRNA catabolic process; gene expression; mRNA metabolic process; mRNA catabolic process, deadenylation-dependent decay
Reference #:  Q8IZH2 (UniProtKB)
Alt. Names/Synonyms: 5'-3' exoribonuclease 1; DKFZp434P0721; DKFZp686B22225; DKFZp686F19113; FLJ41903; SEP1; Strand-exchange protein 1 homolog; XRN1
Gene Symbols: XRN1
Molecular weight: 194,107 Da
Basal Isoelectric point: 6.78  Predict pI for various phosphorylation states
Select Structure to View Below

XRN1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 K79-ub FRIIKPRkVFFMAVD
0 1 K268-ac EFSVLKEkITFKYDI
0 1 K368-ub FESKVGNkYLNEAAG
0 2 Y384-p AAEEARNyKEKKKLK
0 1 K652 KITRIDQKALYFCGF
0 1 Y655 RIDQKALYFCGFPTL
0 1 K736 AVSDGETKFYLEEPP
0 1 T753-p QKLYSGRtAPPSKVV
0 1 Y797-p NETSAVVyAQLLtGR
0 1 T802-p VVyAQLLtGRKYQIN
0 2 Y829-p KQVVPFVyQTIVKDI
0 1 S844-p RAFDSRFsNIkTLDD
0 2 K847-ub DSRFsNIkTLDDLFP
0 1 R939-m1 TGSIFIGrGSRRNPH
0 1 Y990-p AEQLLAEyLERAPEL
0 71 Y1248-p QGSGKMQyFQPTIQE
0 2 Y1282-p FNDNSVKyQQRKHDP
0 7 S1299-p KFKEECKsPKAECWs
0 1 S1306-p sPKAECWsQKMSNKQ
0 2 - gap
0 3 S1348 PPSEEHLSPQSFAMG
0 1 K1364-ac RMLKEILkIDGSNTV
0 116 Y1394-p SSNRRDEyGLPsQPK
0 1 S1398-p RDEyGLPsQPKQNKK
0 1 K1412-ac KLASYMNkPHSANEy
0 3 Y1419-p kPHSANEyHNVQSMD
0 7 S1451-p TELSRICsLVGMPQP
0 1 T1629-p EAQSSQAtPVQtSQP
0 1 T1633-p SQAtPVQtSQPDsSN
0 1 S1638-p VQtSQPDsSNIVKVs
0 9 S1645-p sSNIVKVsPRESSSA
0 1 S1649 VKVsPRESSSASLKS
0 1 S1657 SSASLKSSPIAQPAS
0 1 S1664 SPIAQPASSFQVETA
0 1 S1665 PIAQPASSFQVETAS
0 3 S1692-p ISSSRRKsRKLAVNF
  XRN1 iso2  
K79 FRIIKPRKVFFMAVD
K268 EFSVLKEKITFKYDI
K368 FESKVGNKYLNEAAG
Y384 AAEEARNYKEKKKLK
K652 KITRIDQKALYFCGF
Y655 RIDQKALYFCGFPTL
K736 AVSDGETKFYLEEPP
T753 QKLYSGRTAPPSKVV
Y797 NETSAVVYAQLLTGR
T802 VVYAQLLTGRKYQIN
Y829 KQVVPFVYQTIVKDI
S844 RAFDSRFSNIKTLDD
K847 DSRFSNIKTLDDLFP
R939 TGSIFIGRGSRRNPH
Y990 AEQLLAEYLERAPEL
Y1248 QGSGKMQYFQPTIQE
Y1282 FNDNSVKYQQRKHDP
S1299 KFKEECKSPKAECWS
S1306 SPKAECWSQKMSNKQ
- gap
S1348-p PPSEEHLsPQSFAMK
K1365 RMLKEILKIDGSNTV
Y1395 SSNRRDEYGLPSQPK
S1399 RDEYGLPSQPKQNKK
K1413 KLASYMNKPHSANEY
Y1420 KPHSANEYHNVQSMD
S1452 TELSRICSLVGMPQP
T1617 EAQSSQATPVQTSQP
T1621 SQATPVQTSQPDSSN
S1626 VQTSQPDSSNIVKVS
S1633 SSNIVKVSPRESSSA
S1637 VKVSPRESSSASLKS
S1645 SSASLKSSPIAQPAS
S1652 SPIAQPASSFQVETA
S1653 PIAQPASSFQVETAS
S1680 ISSSRRKSRKLAVNF
  mouse

 
K79 FRIIKPRKVFFMAVD
K268 EFSALKEKITFKYDI
K368 FESKVGNKYLNEAAG
C384 AAEEAKNCKEKRKPK
K652-ub KITRVDQkALyFCGF
Y655-p RVDQkALyFCGFPTL
K736-ub AVSDGETkFYIEEPP
T753 QKVYLGKTAPPSKVI
Y797 NETSAVVYAQLLTGR
T802 VVYAQLLTGRKYQIS
Y829 KQILPFVYQTIVKDI
S844 RAFDSRFSNIKTLDD
K847 DSRFSNIKTLDDLFP
R939 TGSIFIGRGSRRNPH
Y990 AEQLLAEYIERAPEL
H1245 QGAGKTQHLQPTVQE
H1279 FTDHSVRHQQRKHDS
S1296-p KFKEEYKsPKAECQS
S1303 sPKAECQSQKLSSKQ
S1328-p KLLKRNEsPGTSEAQ
S1382-p PPDEADLsPQSFAMK
K1399 RMLKEILKIDSPDTR
R1428 VSSRRDERGVSAHPK
A1432 RDERGVSAHPKPTCH
K1442 KPTCHMNKPHGTNEF
F1449 KPHGTNEFQNVASVD
S1479 TELSRICSLVGMPQP
T1644 EAQSSQATPLQTNKP
T1648 SQATPLQTNKPGSSE
S1653 LQTNKPGSSEATKMt
T1660-p SSEATKMtPQEsPPA
S1664-p TKMtPQEsPPASSSS
S1672-p PPASSSSsQAAQPVs
S1679-p sQAAQPVssHVETAS
S1680-p QAAQPVssHVETASQ
S1705 PSSSKRKSRKLAVNF
  rat

 
K79 FRIIKPRKVFFMAVD
K268 EFSALKEKITFKYDI
K368 FESKVGNKYLNEAAG
C384 AAEEAKSCKDKRKEK
K652 KITRVDQKALYFCGF
Y655 RVDQKALYFCGFPTL
K736 AVSDGETKFYMEEPP
T753 QKVYLGKTAPPCKVI
Y797 NETSAVVYAQLLTGR
T802 VVYAQLLTGRRYQVN
Y829 KQSLPFVYQTIVKDV
S844 RAFDSRFSNIKTLDD
K847 DSRFSNIKTLDDLFP
R939 TGSIFIGRGSRRNPH
Y990 AEQLLAEYIERAPEL
H1248 QGSGKIQHLQPTVQE
H1282 FNDHSVRHQQRKHDP
S1299 KFKEEYKSPKAECQN
N1306 SPKAECQNQKLSNKQ
S1331 KLLKRNESPGTSEAQ
S1384 PPDEAHLSPQSFAMK
K1401 RMLKEILKIDSPDTT
H1431 SSSRRDEHGPSSHPK
S1435 RDEHGPSSHPKPSKK
Q1449 KLASHVSQPHSTNEY
Y1456 QPHSTNEYQSVDSVC
S1483 TELSRICSLVGMPQP
T1648 EAQSSQATPLQTNKP
T1652 SQATPLQTNKPGSSE
S1657 LQTNKPGSSEATRMT
T1664 SSEATRMTPQEGSPA
G1668 TRMTPQEGSPASSAS
S1676 SPASSASSQATQPVS
S1683 SQATQPVSSHVETAS
S1684 QATQPVSSHVETASQ
S1709 PSSSRRKSRKLAVNF
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