UniProt ID | PAXI1_HUMAN | |
---|---|---|
UniProt AC | Q6ZW49 | |
Protein Name | PAX-interacting protein 1 | |
Gene Name | PAXIP1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1069 | |
Subcellular Localization | Nucleus matrix . Chromosome . Localizes to DNA damage foci upon ionizing radiation. | |
Protein Description | Involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. Plays a role in early development. In DNA damage response is required for cell survival after ionizing radiation. In vitro shown to be involved in the homologous recombination mechanism for the repair of double-strand breaks (DSBs). Its localization to DNA damage foci requires RNF8 and UBE2N. Recruits TP53BP1 to DNA damage foci and, at least in particular repair processes, effective DNA damage response appears to require the association with TP53BP1 phosphorylated by ATM at 'Ser-25'. Together with TP53BP1 regulates ATM association. Proposed to recruit PAGR1 to sites of DNA damage and the PAGR1:PAXIP1 complex is required for cell survival in response to DNA damage; the function is probably independent of MLL-containing histone methyltransferase (HMT) complexes. However, this function has been questioned (By similarity). Promotes ubiquitination of PCNA following UV irradiation and may regulate recruitment of polymerase eta and RAD51 to chromatin after DNA damage. Proposed to be involved in transcriptional regulation by linking MLL-containing histone methyltransferase (HMT) complexes to gene promoters by interacting with promoter-bound transcription factors such as PAX2. Associates with gene promoters that are known to be regulated by KMT2D/MLL2. During immunoglobulin class switching in activated B-cells is involved in trimethylation of histone H3 at 'Lys-4' and in transcription initiation of downstream switch regions at the immunoglobulin heavy-chain (Igh) locus; this function appears to involve the recruitment of MLL-containing HMT complexes. Conflictingly, its function in transcriptional regulation during immunoglobulin class switching is reported to be independent of the MLL2/MLL3 complex (By similarity).. | |
Protein Sequence | MSDQAPKVPEEMFREVKYYAVGDIDPQVIQLLKAGKAKEVSYNALASHIISEDGDNPEVGEAREVFDLPVVKPSWVILSVQCGTLLPVNGFSPESCQIFFGITACLSQVSSEDRSALWALVTFYGGDCQLTLNKKCTHLIVPEPKGEKYECALKRASIKIVTPDWVLDCVSEKTKKDEAFYHPRLIIYEEEEEEEEEEEEVENEEQDSQNEGSTDEKSSPASSQEGSPSGDQQFSPKSNTEKSKGELMFDDSSDSSPEKQERNLNWTPAEVPQLAAAKRRLPQGKEPGLINLCANVPPVPGNILPPEVRGNLMAAGQNLQSSERSEMIATWSPAVRTLRNITNNADIQQMNRPSNVAHILQTLSAPTKNLEQQVNHSQQGHTNANAVLFSQVKVTPETHMLQQQQQAQQQQQQHPVLHLQPQQIMQLQQQQQQQISQQPYPQQPPHPFSQQQQQQQQAHPHQFSQQQLQFPQQQLHPPQQLHRPQQQLQPFQQQHALQQQFHQLQQHQLQQQQLAQLQQQHSLLQQQQQQQIQQQQLQRMHQQQQQQQMQSQTAPHLSQTSQALQHQVPPQQPPQQQQQQQPPPSPQQHQLFGHDPAVEIPEEGFLLGCVFAIADYPEQMSDKQLLATWKRIIQAHGGTVDPTFTSRCTHLLCESQVSSAYAQAIRERKRCVTAHWLNTVLKKKKMVPPHRALHFPVAFPPGGKPCSQHIISVTGFVDSDRDDLKLMAYLAGAKYTGYLCRSNTVLICKEPTGLKYEKAKEWRIPCVNAQWLGDILLGNFEALRQIQYSRYTAFSLQDPFAPTQHLVLNLLDAWRVPLKVSAELLMSIRLPPKLKQNEVANVQPSSKRARIEDVPPPTKKLTPELTPFVLFTGFEPVQVQQYIKKLYILGGEVAESAQKCTHLIASKVTRTVKFLTAISVVKHIVTPEWLEECFRCQKFIDEQNYILRDAEAEVLFSFSLEESLKRAHVSPLFKAKYFYITPGICPSLSTMKAIVECAGGKVLSKQPSFRKLMEHKQNSSLSEIILISCENDLHLCREYFARGIDVHNAEFVLTGVLTQTLDYESYKFN | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSDQAPKVP ------CCCCCCCCC | 50.13 | 28348404 | |
7 | Ubiquitination | -MSDQAPKVPEEMFR -CCCCCCCCCHHHHH | 73.72 | - | |
17 | Ubiquitination | EEMFREVKYYAVGDI HHHHHHCCEEECCCC | 27.99 | 29967540 | |
33 | Ubiquitination | PQVIQLLKAGKAKEV HHHHHHHHHCCCCEE | 64.78 | 29967540 | |
36 | Ubiquitination | IQLLKAGKAKEVSYN HHHHHHCCCCEECHH | 62.23 | - | |
115 | Phosphorylation | QVSSEDRSALWALVT HCCCCCHHHHHHHHH | 39.78 | - | |
122 | Phosphorylation | SALWALVTFYGGDCQ HHHHHHHHHCCCCEE | 16.40 | - | |
124 | Phosphorylation | LWALVTFYGGDCQLT HHHHHHHCCCCEEEE | 15.72 | - | |
131 | Phosphorylation | YGGDCQLTLNKKCTH CCCCEEEEECCCCCE | 11.47 | - | |
137 | Phosphorylation | LTLNKKCTHLIVPEP EEECCCCCEEEECCC | 28.70 | - | |
149 | Phosphorylation | PEPKGEKYECALKRA CCCCCCCCHHHHHHC | 16.37 | 24719451 | |
218 | Phosphorylation | EGSTDEKSSPASSQE CCCCCCCCCCCCCCC | 39.23 | 23186163 | |
219 | Phosphorylation | GSTDEKSSPASSQEG CCCCCCCCCCCCCCC | 35.24 | 23186163 | |
227 | Phosphorylation | PASSQEGSPSGDQQF CCCCCCCCCCCCCCC | 18.36 | 29978859 | |
229 | Phosphorylation | SSQEGSPSGDQQFSP CCCCCCCCCCCCCCC | 57.61 | 23186163 | |
235 | Phosphorylation | PSGDQQFSPKSNTEK CCCCCCCCCCCCCCC | 27.38 | 25159151 | |
238 | Phosphorylation | DQQFSPKSNTEKSKG CCCCCCCCCCCCCCC | 52.98 | 26074081 | |
243 | Phosphorylation | PKSNTEKSKGELMFD CCCCCCCCCCEECCC | 39.39 | 24144214 | |
252 | Phosphorylation | GELMFDDSSDSSPEK CEECCCCCCCCCHHH | 37.58 | 25159151 | |
253 | Phosphorylation | ELMFDDSSDSSPEKQ EECCCCCCCCCHHHH | 48.81 | 25159151 | |
255 | Phosphorylation | MFDDSSDSSPEKQER CCCCCCCCCHHHHHH | 50.14 | 25159151 | |
256 | Phosphorylation | FDDSSDSSPEKQERN CCCCCCCCHHHHHHC | 41.91 | 25159151 | |
267 | Phosphorylation | QERNLNWTPAEVPQL HHHCCCCCHHHHHHH | 16.14 | 25159151 | |
278 | Acetylation | VPQLAAAKRRLPQGK HHHHHHHHHCCCCCC | 33.07 | 25953088 | |
285 | Acetylation | KRRLPQGKEPGLINL HHCCCCCCCCCCEEC | 56.33 | 26051181 | |
321 | Phosphorylation | AAGQNLQSSERSEMI HCCCCCCCCCHHHHH | 37.01 | - | |
322 | Phosphorylation | AGQNLQSSERSEMIA CCCCCCCCCHHHHHH | 24.86 | - | |
325 | Phosphorylation | NLQSSERSEMIATWS CCCCCCHHHHHHHHC | 27.71 | 20068231 | |
330 | Phosphorylation | ERSEMIATWSPAVRT CHHHHHHHHCHHHHH | 18.62 | 29978859 | |
332 | Phosphorylation | SEMIATWSPAVRTLR HHHHHHHCHHHHHHH | 9.91 | 21815630 | |
630 | Ubiquitination | KQLLATWKRIIQAHG HHHHHHHHHHHHHCC | 29.39 | - | |
661 | Phosphorylation | ESQVSSAYAQAIRER HHHHHHHHHHHHHHH | 10.95 | - | |
679 | Phosphorylation | VTAHWLNTVLKKKKM HHHHHHHHHHHHCCC | 25.66 | - | |
735 | Phosphorylation | AYLAGAKYTGYLCRS HHHHCCCCCCEEECC | 12.59 | 28442448 | |
736 | Phosphorylation | YLAGAKYTGYLCRSN HHHCCCCCCEEECCC | 20.74 | 28442448 | |
738 | Phosphorylation | AGAKYTGYLCRSNTV HCCCCCCEEECCCEE | 8.53 | 25884760 | |
749 | Ubiquitination | SNTVLICKEPTGLKY CCEEEEECCCCCCCC | 60.79 | - | |
752 | Phosphorylation | VLICKEPTGLKYEKA EEEECCCCCCCCHHH | 57.12 | 29083192 | |
756 | Phosphorylation | KEPTGLKYEKAKEWR CCCCCCCCHHHCCCC | 27.92 | 29083192 | |
788 | Phosphorylation | EALRQIQYSRYTAFS HHHHHHCHHHCCCCC | 9.20 | 24043423 | |
789 | Phosphorylation | ALRQIQYSRYTAFSL HHHHHCHHHCCCCCC | 11.48 | 24043423 | |
791 | Phosphorylation | RQIQYSRYTAFSLQD HHHCHHHCCCCCCCC | 9.11 | 24043423 | |
792 | Phosphorylation | QIQYSRYTAFSLQDP HHCHHHCCCCCCCCC | 21.81 | 24043423 | |
795 | Phosphorylation | YSRYTAFSLQDPFAP HHHCCCCCCCCCCCC | 23.74 | 24043423 | |
803 | Phosphorylation | LQDPFAPTQHLVLNL CCCCCCCHHHHHHHH | 25.78 | 24043423 | |
835 | Ubiquitination | IRLPPKLKQNEVANV CCCCCCCCCCCCCCC | 58.15 | 29967540 | |
847 | Acetylation | ANVQPSSKRARIEDV CCCCCCCCCCCCCCC | 55.18 | 25953088 | |
847 | Ubiquitination | ANVQPSSKRARIEDV CCCCCCCCCCCCCCC | 55.18 | 29967540 | |
858 | Phosphorylation | IEDVPPPTKKLTPEL CCCCCCCCCCCCCCC | 46.73 | 29514088 | |
859 | Acetylation | EDVPPPTKKLTPELT CCCCCCCCCCCCCCC | 52.11 | 25953088 | |
885 | Ubiquitination | QVQQYIKKLYILGGE HHHHHHHHHHHCCHH | 36.64 | 29967540 | |
899 | Ubiquitination | EVAESAQKCTHLIAS HHHHHHHHHHHHHHH | 40.60 | 29967540 | |
901 | Phosphorylation | AESAQKCTHLIASKV HHHHHHHHHHHHHCH | 27.10 | - | |
907 | Ubiquitination | CTHLIASKVTRTVKF HHHHHHHCHHHHHHH | 38.31 | 29967540 | |
911 | Phosphorylation | IASKVTRTVKFLTAI HHHCHHHHHHHHHHH | 20.77 | 24505115 | |
916 | Phosphorylation | TRTVKFLTAISVVKH HHHHHHHHHHHHHHH | 25.69 | 20068231 | |
919 | Phosphorylation | VKFLTAISVVKHIVT HHHHHHHHHHHHCCC | 20.56 | 20068231 | |
938 | Ubiquitination | EECFRCQKFIDEQNY HHHHHHHHHHHCCCE | 48.16 | - | |
970 | Phosphorylation | SLKRAHVSPLFKAKY HHHHHCCCHHHCCCE | 13.15 | 23312004 | |
974 | Ubiquitination | AHVSPLFKAKYFYIT HCCCHHHCCCEEEEC | 52.21 | 29967540 | |
977 | Phosphorylation | SPLFKAKYFYITPGI CHHHCCCEEEECCCC | 13.38 | 20090780 | |
1001 | Ubiquitination | IVECAGGKVLSKQPS HHHHCCCCHHHCCHH | 38.80 | 29967540 | |
1005 | Ubiquitination | AGGKVLSKQPSFRKL CCCCHHHCCHHHHHH | 63.17 | 29967540 |
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 PAXI1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PAXI1_HUMAN !! |
* 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 PAXI1_HUMAN !! |
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. |
loading...