STPAP_HUMAN - dbPTM
STPAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STPAP_HUMAN
UniProt AC Q9H6E5
Protein Name Speckle targeted PIP5K1A-regulated poly(A) polymerase
Gene Name TUT1
Organism Homo sapiens (Human).
Sequence Length 874
Subcellular Localization Nucleus, nucleolus . Nucleus speckle .
Protein Description Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation..
Protein Sequence MAAVDSDVESLPRGGFRCCLCHVTTANRPSLDAHLGGRKHRHLVELRAARKAQGLRSVFVSGFPRDVDSAQLSEYFLAFGPVASVVMDKDKGVFAIVEMGDVGAREAVLSQSQHSLGGHRLRVRPREQKEFQSPASKSPKGAAPDSHQLAKALAEAADVGAQMIKLVGLRELSEAERQLRSLVVALMQEVFTEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLEEPQPVPKAPESPSLDSALASPLDPQALACTPASPPDSQPPASPQDSEALDFETPSSSLAPQTPDSALASETLASPQSLPPASPLLEDREEGDLGKASELAETPKEEKAEGAAMLELVGSILRGCVPGVYRVQTVPSARRPVVKFCHRPSGLHGDVSLSNRLALHNSRFLSLCSELDGRVRPLVYTLRCWAQGRGLSGSGPLLSNYALTLLVIYFLQTRDPPVLPTVSQLTQKAGEGEQVEVDGWDCSFPRDASRLEPSINVEPLSSLLAQFFSCVSCWDLRGSLLSLREGQALPVAGGLPSNLWEGLRLGPLNLQDPFDLSHNVAANVTSRVAGRLQNCCRAAANYCRSLQYQRRSSRGRDWGLLPLLQPSSPSSLLSATPIPLPLAPFTQLTAALVQVFREALGCHIEQATKRTRSEGGGTGESSQGGTSKRLKVDGQKNCCEEGKEEQQGCAGDGGEDRVEEMVIEVGEMVQDWAMQSPGQPGDLPLTTGKHGAPGEEGQPSHAALAERGPKGHEAAQEWSQGEAGKGASLPSSASWRCALWHRVWQGRRRARRRLQQQTKEGAGGGAGTRAGWLATEAQVTQELKGLSGGEERPETEPLLSFVASVSPADRMLTVTPLQDPQGLFPDLHHFLQVFLPQAIRHLK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAVDSDVE
------CCCCCCCHH		19.05-
6Phosphorylation--MAAVDSDVESLPR
--CCCCCCCHHHCCC		36.6429255136
10PhosphorylationAVDSDVESLPRGGFR
CCCCCHHHCCCCCEE		43.4523663014
13MethylationSDVESLPRGGFRCCL
CCHHHCCCCCEEEEE		64.26115490667
44PhosphorylationGRKHRHLVELRAARK
CCCCHHHHHHHHHHH		5.4919651622
48PhosphorylationRHLVELRAARKAQGL
HHHHHHHHHHHHHCC		25.01-
51MethylationVELRAARKAQGLRSV
HHHHHHHHHHCCHHE		40.09-
112PhosphorylationREAVLSQSQHSLGGH
HHHHHHHCCCCCCCC		26.8717525332
115PhosphorylationVLSQSQHSLGGHRLR
HHHHCCCCCCCCCCE		22.5228555341
133PhosphorylationREQKEFQSPASKSPK
HHHHHCCCCCCCCCC		27.9625159151
136PhosphorylationKEFQSPASKSPKGAA
HHCCCCCCCCCCCCC		36.7328450419
138PhosphorylationFQSPASKSPKGAAPD
CCCCCCCCCCCCCCC		29.3728450419
146PhosphorylationPKGAAPDSHQLAKAL
CCCCCCCHHHHHHHH		16.4526074081
150PhosphorylationAPDSHQLAKALAEAA
CCCHHHHHHHHHHHH		6.6317525332
151UbiquitinationPDSHQLAKALAEAAD
CCHHHHHHHHHHHHH		53.15-
163SulfoxidationAADVGAQMIKLVGLR
HHHHHHHHHHHHCHH		2.6421406390
165UbiquitinationDVGAQMIKLVGLREL
HHHHHHHHHHCHHHH		31.60-
171PhosphorylationIKLVGLRELSEAERQ
HHHHCHHHHHHHHHH		62.79-
176PhosphorylationLRELSEAERQLRSLV
HHHHHHHHHHHHHHH		36.59-
178UbiquitinationELSEAERQLRSLVVA
HHHHHHHHHHHHHHH		32.50-
189UbiquitinationLVVALMQEVFTEFFP
HHHHHHHHHHHHHCC		26.1521906983
203UbiquitinationPGCVVHPFGSSINSF
CCCEEECCCCCCCCC		10.01-
238PhosphorylationPVPKAPESPSLDSAL
CCCCCCCCCCHHHHH		20.8026074081
240PhosphorylationPKAPESPSLDSALAS
CCCCCCCCHHHHHCC		54.8326074081
243PhosphorylationPESPSLDSALASPLD
CCCCCHHHHHCCCCC		30.4025137130
247PhosphorylationSLDSALASPLDPQAL
CHHHHHCCCCCCCHH		27.1825137130
309PhosphorylationPQSLPPASPLLEDRE
CCCCCCCCCCCCCCC		23.1224275569
324PhosphorylationEGDLGKASELAETPK
CCCCCHHHHHCCCCH		36.3126270265
329PhosphorylationKASELAETPKEEKAE
HHHHHCCCCHHHHHH		33.7729255136
331UbiquitinationSELAETPKEEKAEGA
HHHCCCCHHHHHHHH		82.81-
347PhosphorylationMLELVGSILRGCVPG
HHHHHHHHHHCCCCC		2.21-
367PhosphorylationTVPSARRPVVKFCHR
ECCCCCCCEEEECCC		29.69-
376PhosphorylationVKFCHRPSGLHGDVS
EEECCCCCCCCCCCC		54.6823312004
383PhosphorylationSGLHGDVSLSNRLAL
CCCCCCCCHHHHHHH		30.7123312004
412PhosphorylationRVRPLVYTLRCWAQG
CCCCHHHHHHHHHCC		10.5524719451
414PhosphorylationRPLVYTLRCWAQGRG
CCHHHHHHHHHCCCC		13.21-
423PhosphorylationWAQGRGLSGSGPLLS
HHCCCCCCCCCCHHH		33.4622817900
425PhosphorylationQGRGLSGSGPLLSNY
CCCCCCCCCCHHHHH		33.5824043423
430PhosphorylationSGSGPLLSNYALTLL
CCCCCHHHHHHHHHH		35.1624043423
432PhosphorylationSGPLLSNYALTLLVI
CCCHHHHHHHHHHHH		10.3024043423
435PhosphorylationLLSNYALTLLVIYFL
HHHHHHHHHHHHHHH		15.1824043423
440PhosphorylationALTLLVIYFLQTRDP
HHHHHHHHHHHCCCC		7.2624043423
444PhosphorylationLVIYFLQTRDPPVLP
HHHHHHHCCCCCCCC		38.9024043423
461PhosphorylationSQLTQKAGEGEQVEV
HHHHHHCCCCCEEEE		50.94-
513PhosphorylationDLRGSLLSLREGQAL
HHCCCHHCCCCCCCC		30.5826546556
642PhosphorylationIEQATKRTRSEGGGT
HHHHCCCCCCCCCCC		39.8529978859
644PhosphorylationQATKRTRSEGGGTGE
HHCCCCCCCCCCCCC		39.7225849741
649PhosphorylationTRSEGGGTGESSQGG
CCCCCCCCCCCCCCC		40.8429978859
652PhosphorylationEGGGTGESSQGGTSK
CCCCCCCCCCCCCCC		29.3427794612
653PhosphorylationGGGTGESSQGGTSKR
CCCCCCCCCCCCCCC		28.6627794612
657PhosphorylationGESSQGGTSKRLKVD
CCCCCCCCCCCEEEC		37.5922210691
658PhosphorylationESSQGGTSKRLKVDG
CCCCCCCCCCEEECC		21.0322210691
659AcetylationSSQGGTSKRLKVDGQ
CCCCCCCCCEEECCC		62.6830591783
682PhosphorylationEEQQGCAGDGGEDRV
HHHCCCCCCCCCHHH		37.87-
707PhosphorylationVQDWAMQSPGQPGDL
HHHHHHCCCCCCCCC		20.2226074081
717PhosphorylationQPGDLPLTTGKHGAP
CCCCCCCCCCCCCCC		31.4026074081
718PhosphorylationPGDLPLTTGKHGAPG
CCCCCCCCCCCCCCC		52.4926074081
731PhosphorylationPGEEGQPSHAALAER
CCCCCCCCHHHHHHH		20.1926074081
750PhosphorylationHEAAQEWSQGEAGKG
HHHHHHHHCCCCCCC		27.7925159151
779UbiquitinationHRVWQGRRRARRRLQ
HHHHHHHHHHHHHHH		43.36-
788PhosphorylationARRRLQQQTKEGAGG
HHHHHHHHHHCCCCC		41.3918077418
790UbiquitinationRRLQQQTKEGAGGGA
HHHHHHHHCCCCCCC		50.22-
828UbiquitinationEERPETEPLLSFVAS
CCCCCCCCHHHHHHC		46.12-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
6SPhosphorylationKinaseCSNK1A1P48729
GPS
750SPhosphorylationKinaseATRQ13535
PSP
-KUbiquitinationE3 ubiquitin ligaseKLHL7Q8IXQ5
PMID:29032201
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STPAP_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of STPAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CPSF1_HUMANCPSF1physical
21102410
CPSF3_HUMANCPSF3physical
21102410
HMOX1_HUMANHMOX1physical
21102410
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STPAP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY.

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