INT2_HUMAN - dbPTM
INT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INT2_HUMAN
UniProt AC Q9H0H0
Protein Name Integrator complex subunit 2
Gene Name INTS2
Organism Homo sapiens (Human).
Sequence Length 1204
Subcellular Localization Nucleus membrane
Single-pass membrane protein . Cytoplasm .
Protein Description Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. [PubMed: 23904267]
Protein Sequence MKDQQTVIMTECTSLQFVSPFAFEAMQKVDVVCLASLSDPELRLLLPCLVRMALCAPADQSQSWAQDKKLILRLLSGVEAVNSIVALLSVDFHALEQDASKEQQLRHKLGGGSGESILVSQLQHGLTLEFEHSDSPRRLRLVLSELLAIMNKVSESNGEFFFKSSELFESPVYLEEAADVLCILQAELPSLLPIVDVAEALLHVRNGAWFLCLLVANVPDSFNEVCRGLIKNGERQDEESLGGRRRTDALRFLCKMNPSQALKVRGMVVEECHLPGLGVALTLDHTKNEACEDGVSDLVCFVSGLLLGTNAKVRTWFGTFIRNGQQRKRETSSSVLWQMRRQLLLELMGILPTVRSTRIVEEADVDMEPNVSVYSGLKEEHVVKASALLRLYCALMGIAGLKPTEEEAEQLLQLMTSRPPATPAGVRFVSLSFCMLLAFSTLVSTPEQEQLMVVWLSWMIKEEAYFESTSGVSASFGEMLLLVAMYFHSNQLSAIIDLVCSTLGMKIVIKPSSLSRMKTIFTQEIFTEQVVTAHAVRVPVTSNLSANITGFLPIHCIYQLLRSRSFTKHKVSIKDWIYRQLCETSTPLHPQLLPLIDVYINSILTPASKSNPEATNQPVTEQEILNIFQGVIGGDNIRLNQRFSITAQLLVLYYILSYEEALLANTKTLAAMQRKPKSYSSSLMDQIPIKFLIRQAQGLQQELGGLHSALLRLLATNYPHLCIVDDWICEEEITGTDALLRRMLLTNNAKNHSPKQLQEAFSAVPVNNTQVMQIIEHLTLLSASELIPYAEVLTSNMSQLLNSGVPRRILQTVNKLWMVLNTVMPRRLWVMTVNALQPSIKFVRQQKYTQNDLMIDPLIVLRCDQRVHRCPPLMDITLHMLNGYLLASKAYLSAHLKETEQDRPSQNNTIGLVGQTDAPEVTREELKNALLAAQDSAAVQILLEICLPTEEEKANGVNPDSLLRNVQSVITTSAPNKGMEEGEDNLLCNLREVQCLICCLLHQMYIADPNIAKLVHFQGYPCELLPLTVAGIPSMHICLDFIPELIAQPELEKQIFAIQLLSHLCIQYALPKSLSVARLAVNVMGTLLTVLTQAKRYAFFMPTLPSLVSFCRAFPPLYEDIMSLLIQIGQVCASDVATQTRDIDPIITRLQQIKEKPSGWSQICKDSSYKNGSRDTGSMDPDVQLCHCIERTVIEIINMSVSGI
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
61PhosphorylationLCAPADQSQSWAQDK
HHCCCCCCCCHHHHH		27.0827080861
63PhosphorylationAPADQSQSWAQDKKL
CCCCCCCCHHHHHHH		29.6227080861
69UbiquitinationQSWAQDKKLILRLLS
CCHHHHHHHHHHHHH		49.39-
108UbiquitinationKEQQLRHKLGGGSGE
HHHHHHHHHCCCCCH		42.2521906983
133PhosphorylationLTLEFEHSDSPRRLR
CEEEEECCCCHHHHH		32.3626699800
135PhosphorylationLEFEHSDSPRRLRLV
EEEECCCCHHHHHHH		24.2626699800
231UbiquitinationEVCRGLIKNGERQDE
HHHHHHHHCCCCCCH		65.03-
247PhosphorylationSLGGRRRTDALRFLC
HCCCCHHHHHHHHHH		24.6624825855
255UbiquitinationDALRFLCKMNPSQAL
HHHHHHHHCCHHHCC		43.81-
263UbiquitinationMNPSQALKVRGMVVE
CCHHHCCEECCEEEE		32.6621906983
282PhosphorylationPGLGVALTLDHTKNE
CCCCEEEEECCCCCH		22.0230257219
286PhosphorylationVALTLDHTKNEACED
EEEEECCCCCHHCCC		34.92-
331PhosphorylationGQQRKRETSSSVLWQ
CCHHCCCCCHHHHHH		37.6324043423
332PhosphorylationQQRKRETSSSVLWQM
CHHCCCCCHHHHHHH		18.8324043423
333PhosphorylationQRKRETSSSVLWQMR
HHCCCCCHHHHHHHH		31.7024043423
334PhosphorylationRKRETSSSVLWQMRR
HCCCCCHHHHHHHHH		22.4624043423
353PhosphorylationELMGILPTVRSTRIV
HHHCCCCCCCCCCCC		25.7128464451
356PhosphorylationGILPTVRSTRIVEEA
CCCCCCCCCCCCCCC		20.0828464451
357PhosphorylationILPTVRSTRIVEEAD
CCCCCCCCCCCCCCC		17.5328464451
372PhosphorylationVDMEPNVSVYSGLKE
CCCCCCCEECCCCCH		23.21-
386PhosphorylationEEHVVKASALLRLYC
HHHHHHHHHHHHHHH		17.4624719451
510UbiquitinationLGMKIVIKPSSLSRM
CCCEEEECHHHHHHC		28.14-
565PhosphorylationYQLLRSRSFTKHKVS
HHHHHCCCCCCCCCC		38.2224719451
574UbiquitinationTKHKVSIKDWIYRQL
CCCCCCHHHHHHHHH		39.2321906983
675UbiquitinationTLAAMQRKPKSYSSS
HHHHHHHCCCCCCCC		39.65-
677UbiquitinationAAMQRKPKSYSSSLM
HHHHHCCCCCCCCHH		66.13-
690UbiquitinationLMDQIPIKFLIRQAQ
HHHHCCHHHHHHHHH		28.85-
746PhosphorylationLLRRMLLTNNAKNHS
HHHHHHHHCCCCCCC		23.59-
750UbiquitinationMLLTNNAKNHSPKQL
HHHHCCCCCCCHHHH		58.26-
847UbiquitinationIKFVRQQKYTQNDLM
HHHHHCCCCCCCCCC		41.7621906983
848PhosphorylationKFVRQQKYTQNDLMI
HHHHCCCCCCCCCCC		14.8217525332
849PhosphorylationFVRQQKYTQNDLMID
HHHCCCCCCCCCCCC		28.1217525332
877PhosphorylationCPPLMDITLHMLNGY
CCCHHHHHHHHHHHH		13.32-
897UbiquitinationAYLSAHLKETEQDRP
HHHHHHHHHCCCCCC		53.36-
905PhosphorylationETEQDRPSQNNTIGL
HCCCCCCCCCCCEEE		46.5720068231
909PhosphorylationDRPSQNNTIGLVGQT
CCCCCCCCEEECCCC		24.7920068231
922PhosphorylationQTDAPEVTREELKNA
CCCCCCCCHHHHHHH		30.6020068231
961PhosphorylationANGVNPDSLLRNVQS
HCCCCHHHHHHHHHH		30.4724719451
977UbiquitinationITTSAPNKGMEEGED
HHCCCCCCCCCCCCC		59.58-
1075PhosphorylationYALPKSLSVARLAVN
HHCCCCHHHHHHHHH		22.33-
1086PhosphorylationLAVNVMGTLLTVLTQ
HHHHHHHHHHHHHHH		10.66-
1089PhosphorylationNVMGTLLTVLTQAKR
HHHHHHHHHHHHHHH		19.3120068231
1092PhosphorylationGTLLTVLTQAKRYAF
HHHHHHHHHHHHHHH		23.3420068231
1095UbiquitinationLTVLTQAKRYAFFMP
HHHHHHHHHHHHHCC		35.8022053931
1154UbiquitinationITRLQQIKEKPSGWS
HHHHHHHHCCCCCHH		56.18-
1156UbiquitinationRLQQIKEKPSGWSQI
HHHHHHCCCCCHHHH		39.21-
1165UbiquitinationSGWSQICKDSSYKNG
CCHHHHCCCCCCCCC		63.37-
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

Oops, there are no upstream regulatory protein records of INT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INT2_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 INT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INT7_HUMANINTS7physical
22939629
INT8_HUMANINTS8physical
22939629
SNX4_HUMANSNX4physical
22939629
VATB2_HUMANATP6V1B2physical
22939629
VATB1_HUMANATP6V1B1physical
22939629
KDM1A_HUMANKDM1Aphysical
23455924
SUV91_HUMANSUV39H1physical
23455924
ABCF3_HUMANABCF3physical
26344197
CG026_HUMANC7orf26physical
26344197
INT1_HUMANINTS1physical
26344197
RPP30_HUMANRPP30physical
26344197
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 INT2_HUMAN

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Related Literatures of Post-Translational Modification
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 TYR-848 AND THR-849, ANDMASS SPECTROMETRY.

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