wanglab/gogpt-training-data huggingface dataset:
Protein: 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (MAD1) (O35593)
Organism: Mus musculus (Mouse)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading.
Interaction partners:
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome regulatory subunit 10B
- Proteasome subunit beta type-1
- Ubiquitin carboxyl-terminal hydrolase 14
- 26S proteasome non-ATPase regulatory subunit 12
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-4
- 26S proteasome regulatory subunit 7
- Proteasome subunit alpha type-3
Sequence:
MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK
Protein: Protein IDA-LIKE 2 (Q6DUW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in floral abscission.
Subcellular location: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Receptor-like protein kinase HSL1
- Protein IDA-LIKE 1
- Somatic embryogenesis receptor kinase 1
- Precursor of CEP15
- Precursor of CEP8
- Protein IDA
- Precursor of CEP14
- Precursor of CEP7
- Precursor of CEP4
- Precursor of CEP6
Sequence:
MSSRNQRSRITSSFFVSFFTRTILLLLILLLGFCNGARTNTNVFNSKPHKKHNDAVSSSTKQFLGFLPRHFPVPASGPSRKHNDIGLLSWHRSSP
Protein: MRN complex-interacting protein (MRN-interacting protein) (Q6NTE8)
Organism: Homo sapiens (Human)
Function: Plays a role in the cellular response to DNA damage and the maintenance of genome stability through its association with the MRN damage-sensing complex. Promotes chromatin loading and activity of the MRN complex to facilitate subsequent ATM-mediated DNA damage response signaling and DNA repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:27568553}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27568553}. Note=Recruited to sites of DNA damage (PubMed:27568553). Phosphorylation on Ser-115 induces its nuclear localization and promotes genome stability (PubMed:27568553). {ECO:0000269|PubMed:27568553}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL36
Sequence:
MASLQRSRVLRCCSCRLFQAHQVKKSVKWTCKACGEKQSFLQAYGEGSGADCRRHVQKLNLLQGQVSELPLRSLEETVSASEEENVGHQQAGNVKQQEKSQPSESRWLKYLEKDSQELELEGTGVCFSKQPSSKMEEPGPRFSQDLPRKRKWSRSTVQPPCSRGVQDSGGSEVAWGPQKGQAGLTWKVKQGSSPCLQENSADCSAGELRGPGKELWSPIQQVTATSSKWAQFVLPPRKSSHVDSEQPRSLQRDPRPAGPAQAKQGTPRAQASREGLSRPTAAVQLPRATHPVTSGSERPCGKTSWDARTPWAEGGPLVLEAQNPRPTRLCDLFITGEDFDDDV
Protein: 5-aminolevulinate synthase, erythroid-specific, mitochondrial (ALAS-E) (EC 2.3.1.37) (5-aminolevulinic acid synthase 2) (Delta-ALA synthase 2) (Delta-aminolevulinate synthase 2) (P22557)
Organism: Homo sapiens (Human)
Function: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products. Contributes significantly to heme formation during erythropoiesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14643893}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000269|PubMed:14643893}.; SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrion inner membrane {ECO:0000269|PubMed:14643893}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000269|PubMed:14643893}.
Interaction partners:
- Delta-aminolevulinic acid dehydratase
- Ferrochelatase, mitochondrial
- Erythroid transcription factor
- Sarcosine dehydrogenase, mitochondrial
- Glycine dehydrogenase
- Serine hydroxymethyltransferase, mitochondrial
- Alanine--glyoxylate aminotransferase
- Serine hydroxymethyltransferase, cytosolic
- Peroxisomal sarcosine oxidase
- Alpha-hemoglobin-stabilizing protein
Sequence:
MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGGDSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQEQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
Protein: Lysine-specific demethylase 4C (EC 1.14.11.66) (Gene amplified in squamous cell carcinoma 1 protein) (GASC-1 protein) (JmjC domain-containing histone demethylation protein 3C) (Jumonji domain-containing protein 2C) ([histone H3]-trimethyl-L-lysine(9) demethylase 4C) (Q9H3R0)
Organism: Homo sapiens (Human)
Function: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}.
Interaction partners:
- Hypoxia-inducible factor 1-alpha
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- Probable JmjC domain-containing histone demethylation protein 2C
- Lysine-specific demethylase 3A demethylase 3A)
- Histone H3.3
- Histone H3.1
- Androgen receptor
- Histone H3.2
- Histone-lysine N-methyltransferase SUV39H1
- Lysine-specific demethylase 6A
Sequence:
MEVAEVESPLNPSCKIMTFRPSMEEFREFNKYLAYMESKGAHRAGLAKVIPPKEWKPRQCYDDIDNLLIPAPIQQMVTGQSGLFTQYNIQKKAMTVKEFRQLANSGKYCTPRYLDYEDLERKYWKNLTFVAPIYGADINGSIYDEGVDEWNIARLNTVLDVVEEECGISIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAQGFFPSSSQGCDAFLRHKMTLISPSVLKKYGIPFDKITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATVRWIDYGKVAKLCTCRKDMVKISMDIFVRKFQPDRYQLWKQGKDIYTIDHTKPTPASTPEVKAWLQRRRKVRKASRSFQCARSTSKRPKADEEEEVSDEVDGAEVPNPDSVTDDLKVSEKSEAAVKLRNTEASSEEESSASRMQVEQNLSDHIKLSGNSCLSTSVTEDIKTEDDKAYAYRSVPSISSEADDSIPLSSGYEKPEKSDPSELSWPKSPESCSSVAESNGVLTEGEESDVESHGNGLEPGEIPAVPSGERNSFKVPSIAEGENKTSKSWRHPLSRPPARSPMTLVKQQAPSDEELPEVLSIEEEVEETESWAKPLIHLWQTKSPNFAAEQEYNATVARMKPHCAICTLLMPYHKPDSSNEENDARWETKLDEVVTSEGKTKPLIPEMCFIYSEENIEYSPPNAFLEEDGTSLLISCAKCCVRVHASCYGIPSHEICDGWLCARCKRNAWTAECCLCNLRGGALKQTKNNKWAHVMCAVAVPEVRFTNVPERTQIDVGRIPLQRLKLKCIFCRHRVKRVSGACIQCSYGRCPASFHVTCAHAAGVLMEPDDWPYVVNITCFRHKVNPNVKSKACEKVISVGQTVITKHRNTRYYSCRVMAVTSQTFYEVMFDDGSFSRDTFPEDIVSRDCLKLGPPAEGEVVQVKWPDGKLYGAKYFGSNIAHMYQVEFEDGSQIAMKREDIYTLDEELPKRVKARFSTASDMRFEDTFYGADIIQGERKRQRVLSSRFKNEYVADPVYRTFLKSSFQKKCQKRQ
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FK45)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Mitogen-activated protein kinase
- Transcription activator MSS11
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
- Serine/threonine-protein kinase STE11
- Mating-type-like protein ALPHA1
Sequence:
MSPFIKGRQRRTEEILKGDLKHHNDDGLVKSVIDDLEDAISAIEDLKFFLATAPLNWHENQVIRRYYLNNSQGFISCVFWNSLYYMTGTDIVKACMYRMEKFGRKVIERKKFEEGLFSDLRNLKCGLDATLEQPKSKFLKFLFRNLCLKTQKKQKVFFWFSIPHDKLFADALERDLKREFNGQNPTTIAIQEPALSFNYDQDSKLSLQEQLSRHISTKKCNTITKSGDKDISKNKITNAVVDNQNEEQKEANDISSLEEVSNSVNIGDPLSRSNHSSSYAYSKFQSCNTSHAQSAISSPLSPTNNLPASMDTDYSSDLKELTSDSPNFDNDDNFMNIKIEYPDENISNGFLATSLNPDQSFLYYDDRNMEIDKNSSIDTNKIVTAQFSPFLVSASLDPQYLLPHVQRTPFQDIKSAAKDGAFTTQKINPSVGNNLHFPYPEVTSPGLVDSITLSELLDENCNNASFELNNERVKISSQELSIWNMLPHNSTSHMTPVFHSLLSAGIKGTHLPAYSPFLTTTPWGSLSSPFSSAKSNKSSQRRQSQFDTRTLGKRRKTKTCSKYSSPNGIARNTKPNKVLKNSINKMIDTLRSNTKNVS
Protein: Gem-associated protein 4b (Gemin4b) (Q8IRT0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Gem-associated protein 2
- Gem-associated protein 5
- RNA helicase
- Survival motor neuron protein
- Gem-associated protein 4c
- Gem-associated protein 4a
- Ribonucleoside-diphosphate reductase large subunit
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- COMM domain-containing protein 10 homolog Vlet
- LSM12 homolog B
Sequence:
MITAEKHPLDNCQLFVQLKKIFHDNNEQAKCLKDMIYWSGNDEHIEKICDQVTDLLEEHDLIIQPPDTMDPFAMNQLRGLLVYLVLNTAHDYFLCKSQWSANVMHLCNQLPPIPLFLTIAIAVNCCLMEPLEEFLACGPRWLTIQYFEAFNEALSVINSDCVETLPLLSAALRAAGRAIVNCNLPAENKQLLRQIACMEHRHILDSKQRLHTLPRPSTRKIYLAKAMDHLIEVLLYTLNDPLKREKPNCFAVYSQITEDISDSNSSDPMPDLRHFAQILLDVLQRIFQLVSVDTYMYWHEMKSKSALYNCQELICRQTAELLKVLQSDKLLGEHPVCKQMQSFADAAKTLEQRVAEMRMGELLVFLDSGMATDEELLAGLDNLFSRFIAFGNDECVETMANHLIMLTKKHAQIILSFLGQVVESEMVVEDEGISVTEVNQGDDEDETSSNDDYEELLSLVLRPLFMQLNVEDKMEVLLLRDEQNVTQGFNFKAPDHRERRIRFFNQLDYNKRFPITKFLVLCFENARQTWIDFSHLGVTHTRFSKLFWHIAQSCPKHAAFHISACADNILVNEQLLQKPYALQFTLYLYGHRQILNGLYTSARQLCVSLKDGRCPYGEDELRQAQNRFLDACAYGLAKFIEPMNLPSLQLILKLLKQISLGESNLITRGTAELNALEKEHPKLENGDDAPAVKVAKHYTYLNASLPEWRLKHWKLISHVMKTIDALRWDLATFEDFRVDNLELAVWYWQDGLSHLTFLGTECRQRILNQVNSLKHKGFWLIYLKEDTLKDTRSFLKLLTQSSAQEANDLFNKLLKKRADCAVMGDLSDAVVKVNSESAFMAFRFLFREYLIAFRSHAKHNKTITKRQHWDHLMAVVAKAPFSIRNEIMKLASKAFAVRFGINIQEQQAAKC
Protein: Dual serine/threonine and tyrosine protein kinase (EC 2.7.12.1) (Dusty protein kinase) (Dusty PK) (Receptor-interacting serine/threonine-protein kinase 5) (Q6XUX1)
Organism: Mus musculus (Mouse)
Function: Acts as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. Involved in the regulation of both caspase-dependent apoptosis and caspase-independent cell death. In the skin, it plays a predominant role in suppressing caspase-dependent apoptosis in response to UV stress in a range of dermal cell types.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23862974}. Cell membrane {ECO:0000269|PubMed:23862974}. Apical cell membrane {ECO:0000269|PubMed:23862974}. Basolateral cell membrane {ECO:0000269|PubMed:23862974}. Cell junction {ECO:0000269|PubMed:23862974}. Note=Detected in basolateral and apical membranes of all tubular epithelia. Detected at apical cell-cell junctions. Colocalized with FGF receptors to the cell membrane. {ECO:0000269|PubMed:23862974}.
Interaction partners:
Sequence:
MEADGQSWAGESVSGPGPGGGGMIRELCRGFSRYRRYLGRLRQNLRETQKFFRDIKCSHSHSCPSSPAGGGAAELGPAGDVAEAPLPAGQLSCISFPPMEETYLQQLVDRLPCILILGQDCNAKCQLLNLLLGVQVLPTLKLDSDESCKLRRLRFTYGTRTRVSLALPGQYELVHTLASHQDNWETIPEEDLEVQEDSEDAAHVLADLEVTMHHALLQEVDIVVAPCPSHRPSVDVLSDLANDFLPVITYALHKDELSERGEQELREVRQYFSFPMFFFKVPKLEIISSSSGRAESERSPLYGQLVDLGYLSSSHRNCVPSDQDCKAQSMLVEQSEKLKQLSTFSHQLLQNRLVDAAKALNVVHSHCLDIFINQAFDMQRDLQITPKRLEYTRKKENELYESLMNIANRKQEEMKDMIVETLNTMKEELLDDAANMEFKDVIVPENGETIGTREIKSCIRQIQELIISRLNQAVANKLISSVDYLRESFVGTLERCLQSLEKSQDVSVHITSNYLKQILNAAYHVEVTFHSGSSVTRMLWEQIKQIIQRITWVNPPTITLEWKRKVAQEAIDSLSASKLAKSICSQFRTRLNSSHEAFAASLRQLEAGHSGRLEKTEDLWLKVRKDHAPRLARLSLESRSLQDVLLHRKPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSVAVLLIMERLHRDLYTGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPLKRPLLGIVQPMLRSIMDRLCKCSSEQPNRGLDDST
Protein: Cobalt transport protein CbiM (Energy-coupling factor transporter probable substrate-capture protein CbiM) (ECF transporter S component CbiM) (D5AUZ9)
Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity. A Cbi(MN) fusion protein has about 70% import capacity, but the holo-Cbi(MN)QO complex cannot be isolated, suggesting CbiN may destabilize it.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:20868747}; Multi-pass membrane protein {ECO:0000305|PubMed:20868747}.
Interaction partners:
- Cobalt transport protein CbiN
- Cobalt import ATP-binding protein CbiO
- Cobalt transport protein CbiQ
- Nickel transport protein NikQ
- Nickel import ATP-binding protein NikO
- Fused nickel transport protein NikMN
- Cobalamin biosynthesis protein CbiG
- DUF4198 domain-containing protein
- Energy-coupling factor transporter transmembrane protein BioN
- Precorrin-6A reductase
Sequence:
MHIMEGYLPVTHAIGWSLAAGPFVVAGAVKIRKIVAERPEARMTLAASGAFAFVLSALKIPSVTGSCSHPTGTGLGAVVFGPSVMAVLGVIVLLFQALLLAHGGLTTLGANAFSMAIVGPWVAWGVYKLAGKAGASMAVAVFLAAFLGDLATYVTTSLQLALAYPDPVSGFLGAALKFGSVFALTQIPLAIAEGFLTVIVVDALAGKVDDKDKLRILAGEAR
Protein: Secretin/TonB short N-terminal domain-containing protein (Q9HUR6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}.
Interaction partners:
- Probable sigma-70 factor, ECF subfamily
- Probable sigma-70 factor, ECF subfamily
- Probable transmembrane sensor
- Probable sigma-70 factor, ECF subfamily
- Probable TonB-dependent receptor
- Probable transmembrane sensor
- Sigma factor regulator, FemR
- Probable transmembrane sensor
- Anti-sigma factor FoxR
- Cobalt-precorrin-6A reductase
Sequence:
MPGANPASEEVMSLQRPIPSLARPLSRLSPLTLALRWALLGLSAAGAGLLGGDLAHAQSVGQHSAATRLDDATPRSYDIPAGSLGASLGAFASQSGLLLSFDPELTRGRTAPALKGRYSVLEGLQRVLSNTGLQVAAGTSGAYLLVEPRMSGEAPADLSPVVVSAAELADPQKETYTAPRSSVYLSSEDIDRFGRVSVGDLLQGIPGVQVGDSRNGGALDVNIRGIQGQSRVAVRVDGAEQALDVYRGYAGTQQRSYIDPDLVSSVTVDKGPSTRSGAIGGSVEMRTIGVKDILVDGKDLGVRFTGDVWNNGVAPQHRSASSKTENLSSVPHDDRGSLFGSQAKSGSAAFAYRNEHLDLVAAYAQRNQGNYFSGKKGQDRYRVYNRYGREESSVAKVYNAGEEVLNSSSETESYLLKATWRIADEHTLDLGYRRYDGRTGEIMPSDIFRFGTAGIYQYPLSEVKIDTYTARYRYLPENNPLVDLSTGLWMTEAKSDMLTSVLAPRSQAYRSDRNWTRQDNRRIGGDLNNVARFETDFGDFKLDLGGSFQVEDIQPQKSVVTTLHDINANRTLRDATRQEYGLNGKLEFKPVERLTLWGGGRYSHFNSKDNGISASPRREDRDMRFITVSRPGYYGSMMWFPDQNGQYTDATDPRLNNGIVTNNTNNPFEGIPFDEFGPANVTVHPSRVTNVVTGYNYSKKGSSRGGGFSPAFGINFELAPDTFVYASYTEGLRLPSLFETSQGTLQVEPGKDLKPERSRSWEIGASALRDSLLADGDSAAIKLAYFNNTIKNYITRYYDPGQMGLMTFSNTDSYRTSGLELQSHYDAGRVFADLSATYYLKTETCDAAFAARLRAGANRYQRTENTPNCTPGSFMGSYTNTQNPPRLATNLTAGLRFFDQALTLGGRMTYTSGPTATADKPWQVGATTPQIEYRSVQLFDLFLKYKLFEHTELNASLQNLTDRYYLDPLAQSFMPAPGRTLRVGMQAKF
Protein: TOX high mobility group box family member 3 (Trinucleotide repeat-containing gene 9 protein) (Q80W03)
Organism: Mus musculus (Mouse)
Function: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Activates transactivation through cAMP response element (CRE) sites. Protects against cell death by inducing antiapoptotic and repressing pro-apoptotic transcripts. Stimulates transcription from the estrogen-responsive or BCL-2 promoters. Required for depolarization-induced transcription activation of the C-FOS promoter in neurons. Associates with chromatin to the estrogen-responsive C3 promoter region (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DENN domain-containing protein 1A
Sequence:
MDVRFYPAAAGDPAGLDFAQCLGYYGYSKLGNNNYMNMAEANNAFFAASEQTFHTPSLGDEEFEIPPITPPPESDPTLGMPDALLPFQTLSDPLPSQGTEFTPQFPPQSLDLPSITISRNLVEQDGVLHSNGLHMDQSHTQVSQYRQDPSLVMRSIVHMTDGARSGIMPPAQLTTINQSQLSAQLGLNLGGANVSHTSPSPPASKSATPSPSSSINEEDADDANRAIGEKRTAPDSGKKPKTPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDSLGEEQKQVYKRKTEAAKKEYLKALAAYRASLVSKAAAESAEAQTIRSVQQTLASTNLTSSLLLNTSLSQHGTVPASPQTLPQSLPRSIAPKPLTMRLPMSQIVTSVTIAANMPSNIGAPLISSMGTTMVGSATSTQVSPSVQTQQHQMQLQQQQQQQQQMQQMQQQQLQQHQMHQQIQQQMQQQHFQHHMQQHLQQQQQQHLQQQLSQQQLQQQLQQHLQLQQLQHMQHQSQPSPRQHSPVTSQITSPIPAIGSPQPASQQHQPQIQSQTQTQVLPQVSIF
Protein: Pentatricopeptide repeat-containing protein 1, mitochondrial (O94368)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial RNA-binding protein required for the stability of the cox2 and cox3 mRNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:21727087}.
Interaction partners:
- Vacuolar protein sorting-associated protein vps901
- Putative exopolyphosphatase
- ATP synthase subunit e, mitochondrial
Sequence:
MLKRAHYVALHVTLNHNGLSYQRVFSCLTQFPMLRHSSTAAKNNVSMISKFQAPEDKFFPSFSLKSMPKQSSHMSASLLNSLNTSMKKSFSRKKYREAVSLFRKNLWKYEESWIRNQDFIDCCIIACSAYEKLCQPLRIKKTFIILSQLCPKLPAELCRVFLSYATGCVNYGHNVALTCFENSPKELIDYNYWLSWLSFSKSSPVVLWLTFTRISSAGLSPNAETFEILLVAFASQKNFWFFEKTYDLFMQSKLTWRPFTYRVLIESFMKFGNFEEAEKLAYSYVKNKIDSLSSDVFFSAILKFYAVGGDFQGFKKLLSFMTDYNVNFSVSTLNQLLRLNLYHAMDEKISTFSSEHITKLIEQQIKPDLESMLIISEYLNEYKPSPKMRELINWLYSNFHLPKTVSLHFLREVQSLVFRYPLLHSKIHLAISTLKDSGCDWNVGLSYLNWLFVNKRITEAINFFYTITINAGTRPPNELFDVFISNLLKFTSAETTSSAIRKVQSKYPSMCGSSPAIKLILFSKSFSVLQSTSEKIEQLLVSFQRNPSAYSKSFTLALAEWLFSRRLFQSALLYSFKVSDVDDSHFSFRSQILICWCYYRLNDFKSLIQHTNNLLQSNNASLLRRLAATLYRIQIRENNGYKRVLLDRLRKKAILRAFPSRTLNRTEKVKLYNEDAKFRSIFSRVLLHQSHLGNVIS
Protein: Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha) (Diphosphoinositide kinase 2-alpha) (Phosphatidylinositol 5-phosphate 4-kinase type II alpha) (PtdIns(5)P-4-kinase isoform 2-alpha) (B3DJ34)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Lysosome {ECO:0000256|ARBA:ARBA00004371}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Si:rp71-17i16.5
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit gamma
- Synaptojanin-1
- Phosphatidylinositol-4,5-bisphosphate 4-phosphatase
- Type I phosphatidylinositol 4,5-bisphosphate 4-phosphatase-B
- phosphatidylinositol-4,5-bisphosphate 3-kinase
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit.
- Type I phosphatidylinositol 4,5-bisphosphate 4-phosphatase-A
Sequence:
MASASNTVSSFASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGINHSINELSHVQIPIMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPLVFRNLRERFVIDDQDFQNSLTRSAPLVSEAQGRSGARFHTSYDKRYVIKTISSEDVAEMHNILKKYHQYIVECHGSTLLPQFLGMYRLTVDGDETYMIVTRNVFSHRLSVYKKYDLKGSTVAREASDKEKAKELPTYKDNDFINDGQKIYIDDESKKIFLNKLQKDVEFLALLKLMDYSLLVGIHDVERAEQEEVESEDNEGEEEGESDGGIVGTPPDSPSNTLDSTKPLSPGDFDPNIDVYAIKSHDNSPRKEVYFMAVIDILQHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFYDFITTILP
Protein: Hyaluronidase conohyal-P1 (EC 3.2.1.35) (Hyaluronoglucosaminidase) (C0HKM3)
Organism: Conus purpurascens (Purple cone)
Function: Hyaluronidase catalyzes the hydrolysis of hyaluronic acid (HA), an anionic, nonsulfated glycosaminoglycan distributed widely throughout connective, epithelial, and neural tissues. In venom, they are known to enhance diffusion of the venom by degrading the extracellular matrix (Probable).
Subcellular location: Secreted {ECO:0000269|PubMed:28479398}.
Interaction partners:
Sequence:
MRVVVVVTGLVVVVVATALSLPDHDVKSASSPLSSSSVYQGSSGDDCDEGLPPPDRPFYVVWNHPDTCKRNRIPLHLDHYGFIFNKNRLFLGEEIQTLYNTGLWPNISETGEFFNGGLPQLFTHHDYSETVEILGRYRTENFTGLGILDFEEWRAIYDTNFGIMRKYQDESIKLAKQRYPSYNKKELTMVAEQEWDQAAREIMSTKLAIGQALMPGGHWGYYGYPRTWGSKRNTQLRNNRIDWLWRQSTGLYPSIYIKDPNMTESAIAEFVSGNVEEAVRVQDEFSPPNTPIYPYAMLQSGDHIFFQVDHLKISLGLPAKMGTSGVILWASSNRYKNATRQCSRMRVHIDNVLGPYVENLTQVMADCSTTLCGGHGRCVHNSHDVLLGETDSQRLSGLCTPRHSRFRDYHCRCYSDWEGACCQTVRPSRCHKQQQGNVHEGGDLQEGHVVNVVNPLIG
Protein: Nucleoprotein TPR/MLP1 domain-containing protein (Q54JG6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear pore protein
- Uncharacterized protein
Sequence:
MTSVSDSNNQWSCSFLSRDEYNQFIATNPIGIILKAEFKIRQLNQTLESIQAKSQVEVTNSQQLFQQLEKDYMDSKKDVEQLNKQNITIKKDLQSLKLSIERESKSNTLNRFIDELQQEKSNLHSIIERKEKDLKEETETVSKLTERLNEFIKEKSDLKSKLITVENENSSNEFQIQRLKQEVNELRKQTTFLEDSQKQTTNNLFNEIKELKSFNLELKLKNENQADEILKLNQINQNLKKQTSELEKKNQQLNEEIKKITTEKVQMTSSFETELNSQKNLASLYQERSEESSKKVTLLQNRLDALKEADKKLRKEHEDAYHKMEEAYDILEADYQKVIKEFDEFKQHTQANAQNQSFNGVGSSSDLSQMDIPILSDTVKERLSDATTLGSRDELRRELLDMIQRYDDLTKIALNEKKEKRYVQDHLSHILREVEKKAPLIHEQNREYQRLLKSQEKLLNSYQQLQSQKETLSLKVTTISSENNKLKQEINDLQKQIRCLLQEALEKKQLQSQSQLNKSQFNGQQSTLFGNSVLNNSTSTSSDDSIIPDSLITFTNIEELQLRNQDLLRQIRILSQDIQSHNENDKKLEMALKELDHLKTARERQAEMIQSLVKQRDHYKNVSSPNSQPINQVGNNNNNNSSSGGMMTLSDLSSSTNGMLNDSSMNGSINKNNNNNNSMNDSFNNSIKNNNNNNNNNNNNSLLSSSTLIQQQQSNEILTQELEKIKQSYQLLQKDYEQVMKDRSISDKELLGKIEQMREQNTSLKIQISQIQSENTIFKERLQISTDSVKNQSQDLEQYRKKNQELMDAVVRHQQSIENLNSQLSRSEEFKSQAELRLSNIKGENQLIRASEERLIEMNKTLSLEKLSIENLLDKVNQLNASKESSETELRRRIENDLTLLETQRIQLKKELDQEKQQHKETSIAMTHQINESRERFEKKEKELSDLKESIIKLKVSEQTLLQKITFLENQLNQSELRYNTIIERTQSNQLTISPTTSSTLSTNNNNNNNQQQKLQQQQQQQQDNLDLSLAKSEIESLKDLLAQEKDNIVHYKSIAISNENDLSQLKEEYTKTKVELEERLKDAQAELAKSQETIKEQQIKLEKLENFSSSHQKDINSIIAEKDSILAEKQQLYEKIQQLTKDQQLALDEAKLQHQLCRKATENYEREVVLHAEDIKVLPKLRDDLVEARKTINQMQIKIDSNSQELEQAKQSWIQQEQLLKQQIQELEERLKDLKHHNNLLHSQIENINQQTQQIDRYSQLSSSSSVGNGLVQVSEDEINNLKELVQVQAREQKITEVKNESLQQENIRLKSTIAANQKAIETVTKKLQEEQENMRTLTVSTRKHQEVLAQLEQMNLFKESNIMLKDETRKLGAQVQELQEKLKQSQDHLLPLTESNKKLLAENQILHNEIEAQKIEITNWSGKVQKLLNKYQSIDPEVHQKLLETNETTIRENQELTQQLEDLKKQLEDLKKQLEDNKKQYEDLKKHTKHWKEEAVKFKKDKLELDQSLTQQKELFSTTKQQLDSNTATNEQTLKENQELRKKIQIANANKQANKQQIQQQQANNEEIEALKKQLEDTRKLAEDYKKLADDYKKLTDEAKSKLKVFESMKKASALNNANNINNNNNNTTPTVVSTPTTPTTTNILAPPVTPTPITPTTTTSTTIIPATATNIATPIPPPVPVEQPKKRVIKRQPTPGMSSFLSNMSNVANTTTTTTPTTTTVTSPAIPTTPTPAIFKQTPVLSPQSISTTATITPTPSIFSSQPSIFGQQSSLFTPTIATTSTPTQITPATNTESVGTTSTTDIQPESPILTNDDSNIIDDDENAEELEESVHTSKKQKMVDGSTTAITISDDEGEIDDSNDTDKLDEEGEIDDSINQDDENQMIDENNNTNESQSISSSPSSTPNTTASTIGGESTTTTTNNNNNNNNNNNNNNNNNNNNNNTNTTIPTTPTPIPTTTTVTTPNQPKKRLRLKTAQTPIPSNILPPSLTPTTKITKRPPIRVKPEDQTTTSTPDETVDNNTNDTITQDNQPSQE
Protein: Protein S100-P (Migration-inducing gene 9 protein) (MIG9) (Protein S100-E) (S100 calcium-binding protein P) (P25815)
Organism: Homo sapiens (Human)
Function: May function as calcium sensor and contribute to cellular calcium signaling. In a calcium-dependent manner, functions by interacting with other proteins, such as EZR and PPP5C, and indirectly plays a role in physiological processes like the formation of microvilli in epithelial cells. May stimulate cell proliferation in an autocrine manner via activation of the receptor for activated glycation end products (RAGE).
Subcellular location: Nucleus. Cytoplasm. Cell projection, microvillus membrane. Note=Colocalizes with S100PBP in the nucleus. Colocalizes with EZR in the microvilli in a calcium-dependent manner.
Interaction partners:
- S100P-binding protein
- Advanced glycosylation end product-specific receptor
- Protein S100-A1
Sequence:
MTELETAMGMIIDVFSRYSGSEGSTQTLTKGELKVLMEKELPGFLQSGKDKDAVDKLLKDLDANGDAQVDFSEFIVFVAAITSACHKYFEKAGLK