wanglab/gogpt-training-data huggingface dataset:
Protein: Inhibitor of growth protein 4 (p29ING4) (Q8C0D7)
Organism: Mus musculus (Mouse)
Function: Component of HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), and have reduced activity toward histone H4. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1) (By similarity). Can enhance apoptosis induced by serum starvation in mammary epithelial cell line HC11.
Subcellular location: Nucleus {ECO:0000269|PubMed:11888890}.
Interaction partners:
- Histone acetyltransferase KAT7
- Protein Jade-1
- Chromatin modification-related protein MEAF6
- Cellular tumor antigen p53
- Histone acetyltransferase KAT6A
- Peregrin
- E3 ubiquitin-protein ligase Jade-2
- Inhibitor of growth protein 5
- Bromodomain-containing 1.
- Protein Jade-3
Sequence:
MAAGMYLEHYLDSIENLPFELQRNFQLMRDLDQRTEDLKAEIDKLATEYMSSARSLSSEEKLALLRQIQEAYGKCKEFGDDKVQLAMQTYEMVDKHIRRLDTDLARFEADLKEKQIESSDYDSSSSKGKKKGRTQKEKKAARARSKGKNSDEEAPKAAQKKLKLVRTSPEYGMPSVTFGSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPRGKWFCPRCSQERKKK
Protein: Type-2 angiotensin II receptor (Angiotensin II type-2 receptor) (AT2 receptor) (P50052)
Organism: Homo sapiens (Human)
Function: Receptor for angiotensin II, a vasoconstricting peptide. Signals primarily via a non-canonical G-protein- and beta-arrestin independent pathways. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P35374}; Multi-pass membrane protein {ECO:0000269|PubMed:28379944, ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086, ECO:0000269|PubMed:32669569}.
Interaction partners:
- Angiotensinogen
- Type-1 angiotensin II receptor
- Angiotensin-converting enzyme 2
- Angiotensin-converting enzyme
- Renin
- Guanine nucleotide-binding protein G
- Kininogen-1
- Microtubule-associated tumor suppressor 1
- Metalloproteinase inhibitor 3
- Endothelin-1
Sequence:
MKGNSTLATTSKNITSGLHFGLVNISGNNESTLNCSQKPSDKHLDAIPILYYIIFVIGFLVNIVVVTLFCCQKGPKKVSSIYIFNLAVADLLLLATLPLWATYYSYRYDWLFGPVMCKVFGSFLTLNMFASIFFITCMSVDRYQSVIYPFLSQRRNPWQASYIVPLVWCMACLSSLPTFYFRDVRTIEYLGVNACIMAFPPEKYAQWSAGIALMKNILGFIIPLIFIATCYFGIRKHLLKTNSYGKNRITRDQVLKMAAAVVLAFIICWLPFHVLTFLDALAWMGVINSCEVIAVIDLALPFAILLGFTNSCVNPFLYCFVGNRFQQKLRSVFRVPITWLQGKRESMSCRKSSSLREMETFVS
Protein: Putative vacuolar protein sorting-associated protein (G0SH11)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Interaction partners:
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 26-like protein
- Vacuolar protein sorting-associated protein 17
- Transcription initiation factor TFIID subunit 5
- Clathrin heavy chain
Sequence:
MEDPWADTASPNSSAPLSQHVEDSSSAPAAAAETPSNTATTTAPSISTSSRPSRATPRRIVAKPKSLEAVEDDPLGPLGAPTPSSDSDNNGLGGATARGVQPPVPPLKEQLPLRTTLPPSTTNRGGRGRRSGPPDPHHIDDDDDDAALFGSAGRGRPPPPVPASLPSPVKSSTAPSMSVEQAARPTFHITVGDPHKVGDLATSHIVYSVRTKTTSKAYKQPEFEVKRRYRDFLWLYNTLHSNNPGVVVPPPPEKQAVGRFESNFVESRRAALEKMLNKIAAHPTLQLDADLKLFLESESFNIDVKHKERKEPPLGESKGVFGSLGFGGGGNKFVEQDDWFHDRRVYLDALENQLKALLKAMDNMVAQRKAMAEAAADFSASLHALSTVELSPTLSGPLDALSELQLAIRDVYERQAQQDVLTFGIIIEEYIRLIGSVKQAFSQRQKAFHSWHSAESELMKKKAAQDKLLRQGKTQQDRLNQVNAEVIDAERKVHQARLLFEDMGRLLRSELDRFEREKVEDFKSGVETFLESAVEAQKELIEKWETFLMQLDAEDDESVFYRPPPVQTKKPAGDTAVDRARARIDEDSD
Protein: Serine/threonine-protein kinase SCH9 (EC 2.7.11.1) (Q5AHG6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Protein kinase that is part of growth control pathway which is at least partially redundant with the cAMP pathway (By similarity). Plays a role in filamentous growth and virulence. Prevents hypha formation specifically under hypoxia at high CO(2) levels. Required for chlamydospore formation, distinctive morphological feature of the fungal pathogen C.albicans that can be induced to form in oxygen-limited environments and has been reported in clinical specimens.
Interaction partners:
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase TOR
- Ubiquitin-binding TORC1 subunit
- Target of rapamycin complex subunit LST8
- Mitogen-activated protein kinase MKC1
- Transcriptional regulator MNL1
- Ras-like protein 1
- cAMP-dependent protein kinase regulatory subunit
- Small ribosomal subunit protein eS6
- Serine/threonine-protein kinase PKH2
Sequence:
MVDFAKSLFGFGNYKKESSSQSPTPPPSAHSSQEQHHKSNTEEYPQSHLSQQQHSHRYQPPHMSEQSHQFPQQQQQQQQSGTNKFFPKTLVSAAPTTAVANHSSVYGTTSTTTNNYPEAYLNQTFKNNIYNPQQQQQQQAQQPPPEQQQSSAPYQNSANIQQPYGNQWGSSQDQDANIITIDKTGNKLSPASRDSPIKGKLKVTILEAKDIFATQPYVVCSFESSEFVTNAPDSYGKSPVSSFGHNNNQGHNGPRNMYNSNHGPSPKALPMKNSGNLFGQRPSMYQRQLSTPHLNLPNDSSNPIWNHDTIFDVVGSKSELDISVYDGARDDAFLGHVRISPSTDKNNKNESEWLQLGARITGETVSSGHIKIKWEYTSFDNNIKRSYGPDDFHFLRLLGKGTFGQVFQVRKKDTNRVYAMKILSKKVIVKKKEIAHTIGERNILVRTSAASSPFIVGLKFSFQTPSDLFLVTDFMSGGELFFHLQKEGRFNEDRSKFYTAELILALEHLHDNDIVYRDLKPENILLDANGHIALCDFGLSKADLNMDGTTNTFCGTTEYLAPEVLLDEQGYTKMVDFWSLGVLIFEMTCGWSPFHAENTQQMYKNIAFGKVRFPKDVLSPEGRSFVKGLLNRNPKHRLGATDDARELKAHPFFADIDWDLLRAKNIPPPFKPHIVSETDISNFDTEFTSENTSALKRQMEMATTPLSPGIQANFKGFTYVDDSTMDDHFARSYRANAFRPPGSFIPGDPNLPPDEEVLAEQIEEEDEMEVDEDQHMDDEFVNGRFDL
Protein: RNA-binding protein 7 (RNA-binding motif protein 7) (Q6P0F4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: RNA-binding subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation. NEXT is involved in surveillance and turnover of aberrant transcripts and non-coding RNAs. Binds preferentially polyuridine sequences and associates with newly synthesized RNAs, including pre-mRNAs and short-lived exosome substrates such as promoter upstream transcripts (PROMPTs), enhancer RNAs (eRNAs), and 3'-extended products from small nuclear RNAs (snRNAs).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y580}. Nucleus {ECO:0000250|UniProtKB:Q9CQT2}. Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:Q9Y580}.
Interaction partners:
- Zinc finger, CCHC domain-containing 8.
- Mtr4 exosome RNA helicase.
- Exosome component 8.
- Exosome complex component RRP4
- Zinc finger CCHC domain-containing protein 7
- Glycoprotein integral membrane protein 1
- Exosome complex component CSL4
- Exosome complex component RRP40
- Exosome component 3.
- Terminal nucleotidyltransferase 4A
Sequence:
MGIADEADRTLFVGNLDPQVTEEVIFELFLQAGPLIKVKIPKDNEGKSKLFAFVNFKHEVSVPYALNLLNGIRLHGRQLNIKFKTGSSHINQEGKSPANSQNPSPANTPGHRGGRTPEQMGSPSYSPPQHMQRPFSSPDTLQRQAMMNNMWQVQMQQLQMLSGTFQQGMQQLRGNADGGWSGHRGQRHSPQDNNNHQGRDQRHGNGANNYERNRRDGQRGDFYHHDDRSGGHNRNYPPDRRRDSREGRWKHF
Protein: EFF-1A (Protein kinase domain-containing protein) (G5ECA1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEPPFEWSPQFILLLLAVTTYGFPLEEKFDGLFRAEPPHCSKTPIVRAQTSQNAMSSIARGMQMQFSIGLHTAVCFRLYEDTQLASQEINDDENAGNQTSLLHTIRLEKLEHHHPITQRYTFGIPEVHASCICECDATSSTCTAESHQFTACPESDKSDETSSCYRTFFPNQTPIGCSEDDIPKLCCDVRFKPYKNMTFLAVKLEQPTTYATFVYAAYDFVNGYWVEKDKTKIRSQLDGGTQDRHLDQKRRISLAVTAGGRASHQLETGMYFSRTSNGGETEELRMQPLNEITDNNFDRLGWYRMDDSGHFHVNNGVVKMDDIHKAKVKNCKEQTYKSILSANHYMPGHFNLTRPLEVIKPWIQSARIFDSSLRQAVVTHAEGTNLQISIHLDDEVESQNLVFFHNASRIRDFSGSIIVDSKSNRLFNLTVYEASGKIDGSVKMSTGFGSDTIHTFTAYVSDLHASNRSMIIPLPAIVGQGARAICLRADSMADIDKICHVIEYFESPLEIDLVEGKWHEMIGTCPTCNQINFNGMMKFLNPAHWIKGISSIGDGVMIATDIVVYLGVLCILYLLITKIIVPLVRCWVCPMSIFCNGSSSSSKNKNDKRRKEREERRRKDKFVSESEDGARSSSEPHDTLARYHGNHSERHYSSSQYI
Protein: Phosphoadenosine phosphosulfate reductase (EC 1.8.4.8) (3'-phosphoadenylylsulfate reductase) (PAPS reductase, thioredoxin dependent) (PAdoPS reductase) (P56859)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier.
Interaction partners:
- Adenylyl-sulfate kinase
- Sulfite reductase subunit beta
- assimilatory sulfite reductase
- Sulfate adenylyltransferase
- 3'
- 3'
- Thiosulfate sulfurtransferase, putative
- Sulfite oxidase, putative
- Luciferase-like domain-containing protein
- Siroheme synthase, putative
Sequence:
MPAKMHSNYPSDSETAELRDSTESGYVSGGSSEEYLPEIVFTKPHLQFLNRQLQFLEPQDVLRWCVTSLPHLYQTTAFGLTGLVIMDMLSKLSIPRPQMVNLIFLDTLHHFPETLKLVDNVRKRYPLQHIHVYKPQGVETEEEFAKKHGERLWEKDDQLYDWIAKVEPAQRAYRELNVHAVLTGRRRSQGGKRGDLDIIEVDEAGLIKINPLANWTFDQVKQYVKENDIPYNELLDKGYKSVGDYHSTSPVKENEDERSGRWKGQAKTECGIHNPRSKYAQYLMDMERKRQEEALSQALQNKLTTA
Protein: adenine phosphoribosyltransferase (EC 2.4.2.7) (Q57V32)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- GMP synthase
- Adenosine kinase
- Adenosine kinase
- Hypoxanthine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
- Adenylosuccinate lyase
- Guanine deaminase
- Guanylate kinase, putative
- Guanylate kinase, putative
- Inosine-adenosine-guanosine-nucleoside hydrolase
Sequence:
MSLVEVLPNYFTLSKDSPLRKKFEKVYKWYSPAFSPHDVPRFAEVGNITENPEVMRGIRDFFVDRYKNLQQPITHILGFDSRGFLLGPMIAVELNVPFVLIRKANKIAGVIIKSEPYTKEYAAESEECMTVRFGSFDKNSRVVLIDDVIATGGTMLAGVQLVDACGATLVEVAGILGLTFLKGTQPAHTFAGGRYSNVPFVTLVDETVLSDENCGDPLHHKGSRIISCAEAKKLI
Protein: Inclusion body clearance protein IML2 (Increased minichromosome loss protein 2) (P47031)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Inclusion body (IB) resident protein that interacts strongly with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing after protein folding stress, probably by enabling access to the IBs of an LD-stored soluble sterol derivative that acts as chaperone in inclusion clearing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. Note=Localized exclusively in cytoplasmic inclusion bodies under protein folding stress conditions. {ECO:0000269|PubMed:26004510}.
Interaction partners:
- Protein PET10
Sequence:
MFRVFGSFGSKGNQSSGEEQSTKTKQVLKQANDFEIALKAMDFVLDDRTDEGLNLLKKAEMETGSDQTILTLARGVIEFLQATLSFETEEMKRAAITLGKAEQMSWKSKQNAEKTNFRSSSIYPPGTVYAVTYTESCLLHALLMLFSESMMEAAKALLKLRRAYTMLQDIMVTVKKAERSKNSSSPSPSEKSQESCGSFVSAETTFISVDIPYKLSSEDKSNPLLLEFAEKIYTMRMGRLSGAHIGNTPSFHRLRDDLGLQTTPSQASDRHSVSDDFDLEQATIDEFIHSGANLCYGILQVVLSLLPPAIGAVLSIVGFKGSREEGLRLVWKATKERNVHGCIGLLGLMFYYDGPFQFTDADFDIPPNDNGSRALNKSRTNDSSLLPGYMDSATLLHPGKILEDALLKARALFPNSALWLLNEAKMLAGKGRLRDSLALMDSIDVNSIRMRQVKSLMVFERAILLVNLHEYNRAADDLISLLDISDWSHALYTYFAGCCYLENWRMTQLGLLNDGKEQFYKERARELIFDAPSLLGKKTFKSKNLPLDRFMLRKVQQFNNMQKKLNLQEPLDSIATSPVHELAYFYNGYNRMTENDLILTKKMLTEYHNPAIDSEDPDQELIRNLLLSLTLRRLGDAERGLALLDDIVLPKIFYIQNGKVKYFKKTEDPWAYPAALYERALFCWKLGGMESLNECREWLLRAQNYAADYELSTRIGMKIKAALDRVENALA
Protein: Epimerase family protein Rv2216 (P9WGP7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Octanoyltransferase
- Lipoyl synthase
- Uncharacterized protein Rv2219
Sequence:
MANAVVAIAGSSGLIGSALTAALRAADHTVLRIVRRAPANSEELHWNPESGEFDPHALTDVDAVVNLCGVNIAQRRWSGAFKQSLRDSRITPTEVLSAAVADAGVATLINASAVGYYGNTKDRVVDENDSAGTGFLAQLCVDWETATRPAQQSGARVVLARTGVVLSPAGGMLRRMRPLFSVGLGARLGSGRQYMSWISLEDEVRALQFAIAQPNLSGPVNLTGPAPVTNAEFTTAFGRAVNRPTPLMLPSVAVRAAFGEFADEGLLIGQRAIPSALERAGFQFHHNTIGEALGYATTRPG
Protein: Ubiquitin-like protein NEDD8 (Neddylin) (Neural precursor cell expressed developmentally down-regulated protein 8) (NEDD-8) (Q15843)
Organism: Homo sapiens (Human)
Function: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis via its conjugation to a limited number of cellular proteins, such as cullins or p53/TP53. Attachment of NEDD8 to cullins is critical for the recruitment of E2 to the cullin-RING-based E3 ubiquitin-protein ligase complex, thus facilitating polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins. Attachment of NEDD8 to p53/TP53 inhibits p53/TP53 transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M.
Subcellular location: Nucleus {ECO:0000269|PubMed:9353319}. Note=Mainly nuclear. {ECO:0000269|PubMed:9353319}.
Interaction partners:
- E3 ubiquitin-protein ligase RBX1
- Sentrin-specific protease 8
- Cullin-5
- COP9 signalosome complex subunit 5
- Cullin-1
- NEDD8-activating enzyme E1 regulatory subunit
- Cullin-2
- NEDD8-conjugating enzyme Ubc12
- NEDD8-activating enzyme E1 catalytic subunit
- Elongin-B
Sequence:
MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGGGGLRQ
Protein: Cytotoxicity-associated immunodominant antigen (120 kDa protein) (CAG pathogenicity island protein 26) (P55980)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: May be necessary for the transcription, folding, export, or function of the cytotoxin.
Interaction partners:
- Acyl-CoA thioesterase YbgC
Sequence:
MTNETIDQTRTPDQTQSQTAFDPQQFINNLQVAFIKVDNVVASFDPDQKPIVDKNDRDNRQAFDGISQLREEYSNKAIKNPTKKNQYFSDFIDKSNDLINKDNLIDVESSTKSFQKFGDQRYQIFTSWVSHQKDPSKINTRSIRNFMENIIQPPIPDDKEKAEFLKSAKQSFAGIIIGNQIRTDQKFMGVFDESLKERQEAEKNGGPTGGDWLDIFLSFIFNKKQSSDVKEAINQEPVPHVQPDIATTTTDIQGLPPEARDLLDERGNFSKFTLGDMEMLDVEGVADIDPNYKFNQLLIHNNALSSVLMGSHNGIEPEKVSLLYAGNGGFGDKHDWNATVGYKDQQGNNVATLINVHMKNGSGLVIAGGEKGINNPSFYLYKEDQLTGSQRALSQEEIRNKVDFMEFLAQNNTKLDNLSEKEKEKFQNEIEDFQKDSKAYLDALGNDRIAFVSKKDTKHSALITEFNNGDLSYTLKDYGKKADKALDREKNVTLQGSLKHDGVMFVDYSNFKYTNASKNPNKGVGATNGVSHLEAGFNKVAVFNLPDLNNLAITSFVRRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVIINQKVTDKVDNLNQAVSVAKAMGDFSRVEQVLADLKNFSKEQLAQQAQKNEDFNTGKNSELYQSVKNSVNKTLVGNGLSGIEATALAKNFSDIKKELNEKFKNFNNNNNGLKNSTEPIYAKVNKKKTGQVASPEEPIYTQVAKKVNAKIDRLNQIASGLGGVGQAAGFPLKRHDKVDDLSKVGLSASPEPIYATIDDLGGPFPLKRHDKVDDLSKVGRSRNQELAQKIDNLNQAVSEAKAGFFGNLEQTIDKLKDSTKKNVMNLYVESAKKVPASLSAKLDNYAINSHTRINSNIQNGAINEKATGMLTQKNPEWLKLVNDKIVAHNVGSVSLSEYDKIGFNQKNMKDYSDSFKFSTKLNNAVKDIKSGFTHFLANAFSTGYYCLARENAEHGIKNVNTKGGFQKS
Protein: Pantothenate synthetase (PS) (EC 6.3.2.1) (Pantoate--beta-alanine ligase) (Pantoate-activating enzyme) (P31663)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Aspartate 1-decarboxylase
- 2-dehydropantoate 2-reductase
- Pantothenate kinase
- Coenzyme A biosynthesis bifunctional protein CoaBC
- Glutamate decarboxylase alpha
- Glutamate decarboxylase beta
- 4-aminobutyrate aminotransferase PuuE
- Cytidylate kinase
- 4-aminobutyrate aminotransferase GabT
Sequence:
MLIIETLPLLRQQIRRLRMEGKRVALVPTMGNLHDGHMKLVDEAKARADVVVVSIFVNPMQFDRPEDLARYPRTLQEDCEKLNKRKVDLVFAPSVKEIYPNGTETHTYVDVPGLSTMLEGASRPGHFRGVSTIVSKLFNLVQPDIACFGEKDFQQLALIRKMVADMGFDIEIVGVPIMRAKDGLALSSRNGYLTAEQRKIAPGLYKVLSSIADKLQAGERDLDEIITIAGQELNEKGFRADDIQIRDADTLLEVSETSKRAVILVAAWLGDARLIDNKMVELA
Protein: U6 snRNA-associated Sm-like protein LSm8 (F4IBJ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365048}.
Interaction partners:
Sequence:
MAATTGLETLVDQIISVITNDGRNIVGVLKGFDQATNIILDESHERVFSTKCHLFNRILRKLTQIFKIGLVLQFFVCMSGHVDTSLDKCSWIFLEGVQQHVLGLYIIRGDNIGVIGELDEELDASLDFSKLRAHPLKPVVH
Protein: ADP-ribosylhydrolase ARH3 (ADP-ribose glycohydrolase ARH3) (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-) (Q8CG72)
Organism: Mus musculus (Mouse)
Function: ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (By similarity). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (By similarity). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By similarity). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria (By similarity). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (By similarity). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16278211, ECO:0000269|PubMed:24191052}. Cytoplasm {ECO:0000269|PubMed:16278211}. Chromosome {ECO:0000250|UniProtKB:Q9NX46}. Mitochondrion matrix {ECO:0000269|PubMed:24191052}. Note=Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites. {ECO:0000250|UniProtKB:Q9NX46}.
Interaction partners:
- ADP-ribose glycohydrolase MACROD1
- Poly
- ADP-ribose glycohydrolase MACROD2
- ADP-ribose glycohydrolase OARD1
- tRNA 2'-phosphotransferase 1
- Poly [ADP-ribose] polymerase 2
Sequence:
MAVAAAAAATAMSAAGGGGASAARSISRFRGCLAGALLGDCVGAVYEAHDTVSLASVLSHVESLEPDPGTPGSARTETLYYTDDTAMTRALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVITVFKKLLNPKCRDVYEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGVSSSEHFLEQLLGHMEELEGDAQSVLDAKELGMEERPYSSRLKKVGELLDQDVVSREEVVSELGNGIAAFESVPTAIYCFLRCMEPHPEIPSTFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMEQVPESWQQSCEGFEETDVLAQSLHRVFQESS
Protein: Hyaluronan mediated motility receptor (Intracellular hyaluronic acid-binding protein) (Receptor for hyaluronan-mediated motility) (CD antigen CD168) (Q00547)
Organism: Mus musculus (Mouse)
Function: Receptor for hyaluronic acid (HA). Involved in cell motility. When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including the PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity. May act as a regulator of adipogenesis.
Subcellular location: Cell surface {ECO:0000269|PubMed:1376732, ECO:0000269|PubMed:9556628}. Cytoplasm {ECO:0000269|PubMed:9556628, ECO:0000269|PubMed:9601097}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:31338967}.
Interaction partners:
- CD44 antigen
- Centromere protein F
- Protein regulator of cytokinesis 1
- Lymphatic vessel endothelial hyaluronic acid receptor 1
- Disks large-associated protein 5
- Stabilin-2
- Kinesin-like protein KIF11
- Hyaluronidase-2
- Kinesin-like protein KIF20A
- Centromere-associated protein E
Sequence:
MSFPKAPLKRFNDPSGCAPSPGAYDVKTSEATKGPVSFQKSQRFKNQRESQQNLNIDKDTTLLASAKKAKKSVSKKDSQKNDKDVKRLEKEIRALLQERGTQDKRIQDMESELEKTEAKLNAAVREKTSLSASNASLEKRLTELTRANELLKAKFSEDGHQKNMRALSLELMKLRNKRETKMRSMMVKQEGMELKLQATQKDLTESKGKIVQLEGKLVSIEKEKIDEKCETEKLLEYIQEISCASDQVEKCKVDIAQLEEDLKEKDREILSLKQSLEENITFSKQIEDLTVKCQLLETERDNLVSKDRERAETLSAEMQILTERLALERQEYEKLQQKELQSQSLLQQEKELSARLQQQLCSFQEEMTSEKNVFKEELKLALAELDAVQQKEEQSERLVKQLEEETKSTAEQLTRLDNLLREKEVELEKHIAAHAQAILIAQEKYNDTAQSLRDVTAQLESVQEKYNDTAQSLRDVTAQLESEQEKYNDTAQSLRDVTAQLESEQEKYNDTAQSLRDVTAQLESVQEKYNDTAQSLRDVTAQLESYKSSTLKEIEDLKLENLTLQEKVAMAEKSVEDVQQQILTAESTNQEYARMVQDLQNRSTLKEEEIKEITSSFLEKITDLKNQLRQQDEDFRKQLEEKGKRTAEKENVMTELTMEINKWRLLYEELYEKTKPFQQQLDAFEAEKQALLNEHGATQEQLNKIRDSYAQLLGHQNLKQKIKHVVKLKDENSQLKSEVSKLRSQLVKRKQNELRLQGELDKALGIRHFDPSKAFCHASKENFTPLKEGNPNCC
Protein: Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein (Methyl methanesulfonate (MMF)-inducible fragment protein 1) (Q15011)
Organism: Homo sapiens (Human)
Function: Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Could enhance presenilin-mediated amyloid-beta protein 40 generation. Binds to ubiquilins and this interaction is required for efficient degradation of CD3D via the ERAD pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10922362}; Multi-pass membrane protein {ECO:0000269|PubMed:10922362}.
Interaction partners:
- E3 ubiquitin-protein ligase synoviolin
- Cyclic AMP-dependent transcription factor ATF-4
- E3 ubiquitin-protein ligase AMFR
- X-box-binding protein 1
- Protein disulfide-isomerase A3
- DnaJ homolog subfamily B member 9
- Endoplasmic reticulum chaperone BiP
- Glucosidase 2 subunit beta
- ER degradation-enhancing alpha-mannosidase-like protein 1
- Protein sel-1 homolog 1
Sequence:
MESETEPEPVTLLVKSPNQRHRDLELSGDRGWSVGHLKAHLSRVYPERPRPEDQRLIYSGKLLLDHQCLRDLLPKQEKRHVLHLVCNVKSPSKMPEINAKVAESTEEPAGSNRGQYPEDSSSDGLRQREVLRNLSSPGWENISRPEAAQQAFQGLGPGFSGYTPYGWLQLSWFQQIYARQYYMQYLAATAASGAFVPPPSAQEIPVVSAPAPAPIHNQFPAENQPANQNAAPQVVVNPGANQNLRMNAQGGPIVEEDDEINRDWLDWTYSAATFSVFLSILYFYSSLSRFLMVMGATVVMYLHHVGWFPFRPRPVQNFPNDGPPPDVVNQDPNNNLQEGTDPETEDPNHLPPDRDVLDGEQTSPSFMSTAWLVFKTFFASLLPEGPPAIAN
Protein: Microsomal glutathione S-transferase 1 (Microsomal GST-1) (EC 2.5.1.18) (Microsomal GST-I) (P08011)
Organism: Rattus norvegicus (Rat)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:6439207}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:6439207}.
Interaction partners:
- Microsomal glutathione S-transferase 2
- Glutathione S-transferase 3, mitochondrial
- Glutathione S-transferase alpha-3
- Glutathione S-transferase Mu 1
- Hematopoietic prostaglandin D synthase
- Glutathione S-transferase Mu 7
- Glutathione S-transferase omega-1
- Glutathione S-transferase theta-2
- Glutathione S-transferase theta-1
- Glutathione S-transferase kappa 1
Sequence:
MADLKQLMDNEVLMAFTSYATIILAKMMFLSSATAFQRLTNKVFANPEDCAGFGKGENAKKFLRTDEKVERVRRAHLNDLENIVPFLGIGLLYSLSGPDLSTALIHFRIFVGARIYHTIAYLTPLPQPNRGLAFFVGYGVTLSMAYRLLRSRLYL