UniProt ID | ARP5_HUMAN | |
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UniProt AC | Q9H9F9 | |
Protein Name | Actin-related protein 5 | |
Gene Name | ACTR5 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 607 | |
Subcellular Localization |
Nucleus . Cytoplasm . Predominantly nuclear but undergoes nucleo-cytoplasmic shuttling (PubMed:19014934). Localized to interphase nuclei, but not nucleoli excluded from chromosomes as mitosis progresses (PubMed:18163988). |
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Protein Description | Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Involved in DNA double-strand break repair and UV-damage excision repair.. | |
Protein Sequence | MAANVFPFRDARAAPDPVLEAGPVAHGPLPVPLVLDNGSFQVRAGWACPGQDPGPEPRLQFRAVCARGRGGARGASGPQVGNALGSLEPLRWMLRSPFDRNVPVNLELQELLLDYSFQHLGVSSQGCVDHPIVLTEAVCNPLYSRQMMSELLFECYGIPKVAYGIDSLFSFYHNKPKNSMCSGLIISSGYQCTHVLPILEGRLDAKNCKRINLGGSQAAGYLQRLLQLKYPGHLAAITLSRMEEILHEHSYIAEDYVEELHKWRCPDYYENNVHKMQLPFSSKLLGSTLTSEEKQERRQQQLRRLQELNARRREEKLQLDQERLDRLLYVQELLEDGQMDQFHKALIELNMDSPEELQSYIQKLSIAVEQAKQKILQAEVNLEVDVVDSKPETPDLEQLEPSLEDVESMNDFDPLFSEETPGVEKPVTTVQPVFNLAAYHQLFVGTERIRAPEIIFQPSLIGEEQAGIAETLQYILDRYPKDIQEMLVQNVFLTGGNTMYPGMKARMEKELLEMRPFRSSFQVQLASNPVLDAWYGARDWALNHLDDNEVWITRKEYEEKGGEYLKEHCASNIYVPIRLPKQASRSSDAQASSKGSAAGGGGAGEQA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
69 | Methylation | RAVCARGRGGARGAS EEECCCCCCCCCCCC | 34.51 | - | |
73 | Methylation | ARGRGGARGASGPQV CCCCCCCCCCCCCCH | 44.48 | - | |
76 | Phosphorylation | RGGARGASGPQVGNA CCCCCCCCCCCHHHC | 54.55 | 27050516 | |
86 | Phosphorylation | QVGNALGSLEPLRWM CHHHCCCCCCCHHHH | 30.34 | 50563365 | |
96 | Phosphorylation | PLRWMLRSPFDRNVP CHHHHHCCCCCCCCC | 26.42 | 28555341 | |
144 | Phosphorylation | AVCNPLYSRQMMSEL HHHCHHHCHHHHHHH | 24.58 | 24719451 | |
175 | Acetylation | LFSFYHNKPKNSMCS HHHHHCCCCCCCCCC | 44.02 | 25953088 | |
175 | Ubiquitination | LFSFYHNKPKNSMCS HHHHHCCCCCCCCCC | 44.02 | - | |
229 | Ubiquitination | LQRLLQLKYPGHLAA HHHHHCCCCCCCEEH | 36.12 | - | |
275 | Ubiquitination | YYENNVHKMQLPFSS HHHCCCCCCCCCCCH | 24.86 | 29967540 | |
283 | Sumoylation | MQLPFSSKLLGSTLT CCCCCCHHHHCCCCC | 46.67 | 28112733 | |
283 | Ubiquitination | MQLPFSSKLLGSTLT CCCCCCHHHHCCCCC | 46.67 | 22817900 | |
287 | Phosphorylation | FSSKLLGSTLTSEEK CCHHHHCCCCCHHHH | 21.88 | 25954137 | |
288 | Phosphorylation | SSKLLGSTLTSEEKQ CHHHHCCCCCHHHHH | 32.05 | 25954137 | |
290 | Phosphorylation | KLLGSTLTSEEKQER HHHCCCCCHHHHHHH | 33.89 | 26270265 | |
291 | Phosphorylation | LLGSTLTSEEKQERR HHCCCCCHHHHHHHH | 47.04 | 21815630 | |
294 | Ubiquitination | STLTSEEKQERRQQQ CCCCHHHHHHHHHHH | 54.10 | 29967540 | |
390 | Sumoylation | EVDVVDSKPETPDLE EEEEECCCCCCCCHH | 42.27 | - | |
459 | Phosphorylation | PEIIFQPSLIGEEQA CEEEECHHHCCHHHH | 23.10 | 46158863 | |
509 | Ubiquitination | GMKARMEKELLEMRP CHHHHHHHHHHHHCC | 44.30 | - | |
574 | Phosphorylation | EHCASNIYVPIRLPK HHHCCCEEEEEECCC | 12.39 | 27642862 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of ARP5_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of ARP5_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 ARP5_HUMAN !! |
Kegg Disease | ||||||
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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. |
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