wanglab/gogpt-training-data huggingface dataset:
Protein: 26S proteasome regulatory subunit 6B homolog (Protein YNT1) (Tat-binding homolog 2) (P33298)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- Proteasome subunit beta type-3
- Proteasome subunit beta type-7
- Proteasome subunit alpha type-6
- Proteasome subunit beta type-1
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-2
- Proteasome subunit beta type-5
- 26S proteasome regulatory subunit RPN7
- 26S proteasome regulatory subunit RPN1
- 26S proteasome regulatory subunit RPN10
Sequence:
MEELGIVTPVEKAVEEKPAVKSYASLLAQLNGTVNNNSALSNVNSDIYFKLKKLEKEYELLTLQEDYIKDEQRHLKRELKRAQEEVKRIQSVPLVIGQFLEPIDQNTGIVSSTTGMSYVVRILSTLDRELLKPSMSVALHRHSNALVDILPPDSDSSISVMGENEKPDVTYADVGGLDMQKQEIREAVELPLVQADLYEQIGIDPPRGVLLYGPPGTGKTMLVKAVANSTKAAFIRVNGSEFVHKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGSDREVQRILIELLTQMDGFDQSTNVKVIMATNRADTLDPALLRPGRLDRKIEFPSLRDRRERRLIFGTIASKMSLAPEADLDSLIIRNDSLSGAVIAAIMQEAGLRAVRKNRYVILQSDLEEAYATQVKTDNTVDKFDFYK
Protein: DUF1769 family protein (Q9UUA7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKCFLICGSKKEPISINGTPNVVKSKYFEGDVKVRLRDYETPDEEYFEQSNDTCSIMIRGRFLPTESTLTADDILFGNQFEKPLRDVLPMGSNLLMKGLQYVDPSIEFDLYCDQPWAFSPFFATMTKMQVSDALLPMEYFEDHSSRRSQMQQQVIRQESSIDPNKYILADFCNPFFNPSTLSISIPYTKMSFSIKNYYNGQPLRYFCKTRDGNVIFAVEFDL
Protein: Kinesin-like protein KIF3A (Microtubule plus end-directed kinesin motor 3A) (Q9Y496)
Organism: Homo sapiens (Human)
Function: Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation. Plays a role in centriole cohesion and subdistal appendage organization and function. Regulates the formation of the subdistal appendage via recruitment of DCTN1 to the centriole. Also required for ciliary basal feet formation and microtubule anchoring to mother centriole.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:P28741}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}. Note=Localizes to the subdistal appendage region of the centriole. {ECO:0000269|PubMed:23386061}.
Interaction partners:
- Kinesin-associated protein 3
- Kinesin-like protein KIF3B
- Kinesin-like protein KIF3C
- Protein smoothened
- Intraflagellar transport protein 88 homolog
- Beta-arrestin-2
- Beta-arrestin-1
- Intraflagellar transport protein 172 homolog
- Mitogen-activated protein kinase kinase kinase 10
- Suppressor of fused homolog
Sequence:
MPINKSEKPESCDNVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTLRYANRAKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQLSRELRLQMLIIDNFIPRDYQEMIENYVHWNEDIGEWQLKCVAYTGNNMRKQTPVPDKKEKDPFEVDLSHVYLAYTEESLRQSLMKLERPRTSKGKARPKTGRRKRSAKPETVIDSLLQ
Protein: Protein Tax-1 (Protein X-LOR) (Protein PX) (Trans-activating transcriptional regulatory protein of HTLV-1) (P03409)
Organism: Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1)
Function: Transcriptional activator that governs the viral transcription from the 5'LTR via the recruitment of dimers of host phosphorylated CREB1. Together they bind cAMP response elements within the viral promoter and mediate high-level viral transcription. Increases host CREB1 O-GlcNAcylation to further increase 5'LTR transactivation. Modulates also the expression of cellular genes leading to the deregulation of T-cell proliferation, perturbing the integrity of cell cycle checkpoints, the DNA damage response and apopototic pathways. Acts as an ubiquitin E3 ligase and stimulates host IKK complex by catalyzing the assembly of free mixed-linkage polyubiquitin chains, resulting in constitutive activation of the transcription factor NF-kappa-B. Inhibits the host nonsense-mediated mRNA decay (NMD), a cellular process that can actively degrade mRNAs by interacting with host UPF1.
Subcellular location: Host nucleus {ECO:0000269|PubMed:15269214, ECO:0000269|PubMed:22789739}. Host cytoplasm {ECO:0000269|PubMed:15269214, ECO:0000269|PubMed:22789739, ECO:0000269|PubMed:29665857}. Note=Shuttles from the host nucleus to the cytoplasm. Found predominantly in the nucleus, where it is equally distributed between the nucleoplasm and the nuclear matrix.
Interaction partners:
Sequence:
MAHFPGFGQSLLFGYPVYVFGDCVQGDWCPISGGLCSARLHRHALLATCPEHQITWDPIDGRVIGSALQFLIPRLPSFPTQRTSKTLKVLTPPITHTTPNIPPSFLQAMRKYSPFRNGYMEPTLGQHLPTLSFPDPGLRPQNLYTLWGGSVVCMYLYQLSPPITWPLLPHVIFCHPGQLGAFLTNVPYKRIEELLYKISLTTGALIILPEDCLPTTLFQPARAPVTLTAWQNGLLPFHSTLTTPGLIWTFTDGTPMISGPCPKDGQPSLVLQSSSFIFHKFQTKAYHPSFLLSHGLIQYSSFHSLHLLFEEYTNIPISLLFNEKEADDNDHEPQISPGGLEPPSEKHFRETEV
Protein: Uncharacterized protein (Q57Z40)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEEGHAMEDDVNEINTTLLGLQQAFAAAMRESGVMGKMRAQLRAAAIGVIRADPCLRDSALGTVLQPAELPLEGRVALLLIEDFLRTHGLKLAGGVFEEECNISMVGEAERHIVEQQRQYQPSQGTPRSSLLESLLARVIDPRECQQLQQQKTGAAPVAHALPHLGQSVAPSPAAATSTTHTVKRERRRPAAELSVPLEVQGRSEITAWLKEYEDSVDFSDSSLEDMPCVDEQIFDAVIHL
Protein: Aminotransferase class IV (Q584G3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- hydroxymethylglutaryl-CoA lyase
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MQTGPFAAVTRVPDHVRNMILNEIASENIWLFDRGRCEAVTVGDMRSSSFSIPMAESPPAVGCELDNNEHLLLYDLMRVRNGQVMFENDHFSRIRQNCILTAPTACDAANVSEDEDLGKLSTYIEGVRSTTRDFIKCNPWENGDVNLKFVTWVLPSQLSDVSTAERRSELLRTLSYAVYYVTSFFPPEDWYEEGTRYAMLYDAQRHTPNAKILQVPLRERAKALQQTTNAFEVLLVSDNRRHYLVPEGSRSNYLIVSGDESLLCSLEEDILVGITLRVARRAAACARLPPLRHRKLVLGDICLAKSIAMLGTSPGVLPIKEIQVFYDEESKQNFLLAMEDYMQDKDEEIQRAVINVRGRILNDDGLLRLESPSCDTLKRLRAAYEAEALL
Protein: Protein prenylyltransferase superfamily protein (F4K5W3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Periodic tryptophan protein 2
- Putative WD-repeat membrane protein
- Transducin family protein / WD-40 repeat family protein
- Protein TORMOZ EMBRYO DEFECTIVE
- DNA-directed RNA polymerase I subunit 2
- Uncharacterized protein At3g06530
- U3 small nucleolar RNA-associated protein 18 homolog
- DNA-directed RNA polymerase III subunit 2
- RNA cytidine acetyltransferase 1
- RNA cytidine acetyltransferase 2
Sequence:
MVGGEVKILRGYELRLIRCTVSLPLSDPPLDESQPGTHPHDSLIKSLLSSIEAGNYLEALASEATNLILGEYEFDPVDSAERVYSELLNKVESFVLNDSSDEIDKARRSFLVMCLAIAAAFWFTCCNLTGSTQGSTKCSLPFRVPESKELVEWENWAKIHLMSAGSDLLGKFSNLQHLVFARLLLLKLKDLLFETSASETFQLRSISWWLVRVLLIHQRVLHEPSSSLFEMLQVYMAEALDHFGALEKVESYWGAKLLQDEASSITSIIHLEACVLQYIYRRIDPFRLQLESAKAAAGLEFSVTGALGFRTIHQVVPKAQMVLVANTSSSNGAVRLASEKADVGPYGAWEGETPQVFMTPKLVNNESEAGTDSVPLKPVEQALILAQCLLIERGSRHDAMQSWDMAPYIEAIDSQKSTYFVLRCFCDLLRVRWESSRYRTRERARDMMDKLVGAISKSDPGVSNRIPLCYAVYLPTIPALRKEYGELLVSCGYVGEAITIFESLELWDNLIYCYCSMGKKSAAVDLINARLLERPNDPRLWCSLGDVTISDSCYEKALEVSNDKSVRAKRALARSAYNRGDFEKSKILWEAAMALNSLYSDGWFALGAAALKARDLQKALDAFTLAVHLDPDNWLAWNNIASLHMIKKKSKESFIAFKEVLKLNRDSWQIWENFSHVAMDVGNTDQAFEAIQQIMRLTQNKSISVVLLDRLMTDLENRNISYESSSNELIKTKPTTTERLYIELFGKIIQQIVKTESTFENWGLYARWSRINGDLTICSEALLKQVRSYLGVEMWKDKERFKKFARASLELCRVYIEISASVESKRELFSAEMHLKNTIKQARKSFGETEELKELESCLEEVRNVTQKFEGTTNIKT
Protein: Chitin synthase export chaperone (Q5AA40)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Chaperone required for the export of the chitin synthase CHS3 from the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GTPase-activating protein
- G protein subunit beta
- Chitin biosynthesis protein CHS5
- chitin synthase
- Chs6p
- chitin synthase
- chitin deacetylase
- chitin synthase
- chitin synthase
- Chs4p
Sequence:
MSFGSFDHICNKTALPLCSVVGAVNQSAFFQRGIVPDCYARSVELANTMIFQIGNAFVHFGGLIILLIIIFNVRAKYTAIGRKEMLFFLYLAIGLIVSSLIVDCGVSPPSSTSYAYFVAVQIGLSSALCICLLYNGFLCFQFWEDGTSRSMWILRVGCFAWFAVNFIVCIITFKHWDTALDYRKTTTLFIFAYVLNAVILAVYVVSQIILVVFALESYWSLGAILLGVFFFVAGQVLTYVFSDKICRGASHYVDGLFFGSACNVFTFMMIYKFWDMITSDDLEFSVANVEQPINEFGVGADDEKRSSMFF
Protein: Growth hormone 2 (B2Z9Z4)
Organism: Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MGQVFLLMPVLLVSCFLSQGAAMENQRLFNIAVNRVQHLHLLAQKMFNDFEGTLLSDERRQLNKIFLVDFCNSDSIVSPIDKQETQKSSVLKLLHISFRLIESWEYPSQTLTISNSLMVRNYNQISEKLSDLKVGINLLIKGSQDGVLSLDDNDSLHLPPYGNYYQNLGGDGNVRRNYELLACFKKDMHKVETYLTVAKCRKSLEANCTL
Protein: Alpha-carbonic anhydrase domain-containing protein (Q8WQD8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAAAQRQSPIDIVPQHVCCDTDVCKADALNIDYKSGDCCDVLVSEGGFLVNVKRNCGTFLTANHLPSSKFALAQFHAHWGSNSKEGSEHFLDGKQLSGEVHFVFWNTSYESFNVALSKPDGLAVVGVFLKEGKYNDNYHGLIDTVRKATGNATPIAMPKDFHIEHLLPSPDKREFVTYLGSLTTPPYNECVIWTLFTEPVEVSFGQLNVLRNIIPANHRACQDRCDREIRSSFNF
Protein: Diacylglycerol O-acyltransferase 2 (AtDGAT2) (EC 2.3.1.20) (Q9ASU1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in triacylglycerol (TAG) synthesis. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA. Can use oleoyl-CoA, linoleoyl-CoA and linolenoyl-CoA as substrates. Has substrate preference for linolenoyl-CoA or oleoyl-CoA compared to linoleoyl-CoA.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23042274}; Multi-pass membrane protein {ECO:0000255}. Lipid droplet {ECO:0000269|PubMed:23042274}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Phospholipid:diacylglycerol acyltransferase 1
- Putative phospholipid:diacylglycerol acyltransferase 2
- Diacylglycerol O-acyltransferase 3
- Phosphatidate phosphatase PAH1
- Phosphatidate phosphatase PAH2
- Triacylglycerol lipase SDP1
- Lipid phosphate phosphatase 1
- Lipid phosphate phosphatase 2
- Putative lipid phosphate phosphatase 3, chloroplastic
Sequence:
MGGSREFRAEEHSNQFHSIIAMAIWLGAIHFNVALVLCSLIFLPPSLSLMVLGLLSLFIFIPIDHRSKYGRKLARYICKHACNYFPVSLYVEDYEAFQPNRAYVFGYEPHSVLPIGVVALCDLTGFMPIPNIKVLASSAIFYTPFLRHIWTWLGLTAASRKNFTSLLDSGYSCVLVPGGVQETFHMQHDAENVFLSRRRGFVRIAMEQGSPLVPVFCFGQARVYKWWKPDCDLYLKLSRAIRFTPICFWGVFGSPLPCRQPMHVVVGKPIEVTKTLKPTDEEIAKFHGQYVEALRDLFERHKSRVGYDLELKIL
Protein: Jem1p (A0A1D8PIB5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- Long chronological lifespan protein 2
- DnaJ-related protein SCJ1
- Endoplasmic reticulum chaperone BIP
- Hsp70 family chaperone
- Hsp70 family ATPase
- Heat shock protein homolog SSE1
- Heat shock protein SSC1, mitochondrial
- Heat shock protein HSP70
Sequence:
MRFPLSTLLVGAALLTFTSCLTDFDQKVLQLDKLFSEQGPTINVLQAYEEIIRTAKSSSSNTNSLPKLLFKKAIIEINLNKEIQAIADLKWALELDPAMGPAKDKIVQLLMARGEFDTVQRYLTKDNDKDIYHTIDKINQDIKTSKELIEKHEYQQCANILNEIISLSPANYEITELYYNLALNSYKETPDFQLKYLGEMLPVNKVIIQTAKNLIDINPMKSLKYFNVLSQFLLYTEVQFENSNKIIKNCLRIDNEYTLCGKLSKFYVKFQNFFKLLEDYSIIQGHYYTNTENNVKLEDEGLINPVIDYQFVIKFLFMDNLQVSKLDKRKLPSSIKNNYDYLQYQIQKFGEELGFETSPKILFLQDLNRLVCEAYSLTGSSKKAKQFCDSFDDSDNLFLPKHITEIDKYLSKKKYPQAEELLNKFNNNVKQTKLFTDRWTKVEEYHMKLNQQRQQQYFQQQQQQQQQRQRQQQYRGAQPHQQRKKPANDYYKVLDVPHDADEKTIKKGYRTQTLKYHPDKYKGDDLTPEQIEKKMQAINQAYEVLSDPELRERYDRGDDPNDPMGQSHPQWQPQGGGGQPNFNFNFGGGGGGGNQFFQQFFGGQGFKFNGQGNPFGNSHQKVKITKNKKKNRSRKQ
Protein: AAA+ ATPase domain-containing protein (Q57W41)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004572}.
Interaction partners:
- Peroxin 19
- Peroxin-13
- Peroxisome assembly protein, putative
- Peroxisomal membrane protein PEX14
- Aldehyde dehydrogenase
- ABC transporter, putative
Sequence:
MRPLDVLLNGLRGLCTAIKETPLFIWVYLSILGVVARKLTYRFGLTTKSKKIGKHVIRVTDAEETLSEDVMDVEEINATFDDVGGLEDVKKALIEHVKWPFTRPELFEGNTLRSHPKGILLYGPPGTGKTLIARALARELGCAFINVRTESLFSKWVGDTEKNAAAVFTLAAKLSPCVIFVDEIDALLGLRNSVDAAPHNNAKTIFMTHWDGVVQKKSKIVVIGATNRPLAIDEAIRRRLPLQLEVPPPDITGRRKILNILMEHDVADESNRSRLVDYVASKTFGYTGSDLTELCKAAALMPIREIGCDNELPCLECRHFDEALKRVRPSMASSV
Protein: Ras-related protein Rab-42 (Q8N4Z0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000250|UniProtKB:P62820}; Lipid-anchor {ECO:0000250|UniProtKB:P62820}.
Interaction partners:
Sequence:
MEAEGCRYQFRVALLGDAAVGKTSLLRSYVAGAPGAPEPEPEPEPTVGAECYRRALQLRAGPRVKLQLWDTAGHERFRCITRSFYRNVVGVLLVFDVTNRKSFEHIQDWHQEVMATQGPDKVIFLLVGHKSDLQSTRCVSAQEAEELAASLGMAFVETSVKNNCNVDLAFDTLADAIQQALQQGDIKLEEGWGGVRLIHKTQIPRSPSRKQHSGPCQC
Protein: Bromodomain adjacent to zinc finger domain 1A (F1SHI5)
Organism: Sus scrofa (Pig)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00475}.
Interaction partners:
- Uncharacterized protein.
- Chromatin accessibility complex subunit 1.
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5.
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1
- BPTF-associated chromatin complex component 1
- Tyrosine-protein kinase BAZ1B
Sequence:
MPLLHRKPFVRQKPPADLRPDEEVFYCKVTNEIFRHYDDFFERTILCNSLVWSCAVTGRPGLTYQEALESEKKARQNLQSFPEPLIVPVLYLTNLTHRSRLHEICDDIFAYVKNRYFVEETVEVIRNNGSRLQCRILEVLPPSHQNGFANGHDSCIDGETIIISDSDDSETQNSSFQNGKKKDAIDPLLFKYKVQPTKKELYECAIVKATQISRRKHLFSRDKLKLFLKQHCEPQDGVIKIKASSLSTYKIAEQDFSYFFPDDPPTFIFSPANRRRGRPPKRVSISQEDTIANKQTVVGFRNKVTKEREKLLKQEEIKSLAFEKAKLKRDKADALEAKKKEKEDKEKKKEELKKIVEEERMKKKEEKERLKIEREKEREKLREEKKKYMEYLKQWSKPREDMECDDLKELPEPTPVKTRLPPEIFGDALMVLEFLNAFGELFDLQDEFPEGVTLEVLEEALVGNDSEGPLCELLFFFLTAIFQAIAEEEEEVAKEQITDADTKDLTEALDEDADPTKSALSAVASLAAAWPQLHQGCSLKSLDLDSCTLSEILRLHILASGADVTSANAKYRYQKRGGFDATDDACMELRLSNPSLVKKLSSTSVYDLTPGEKMKILHALCGKLLTLVSTRDFIEDYVDILRQAKQEFRELKAEQHRKEREEAAARIRKRKEEKLKEQEQKMKEKQEKLKEDEQRNSVADVSIGEEEREDFDTSTESKEIEQKEQDQDTVTEDEDDQGLHKRGRRGKRGQNEFKEFSRQEEVNCVTREPLTADEEEALKQEHQRKEKELLEKIQNAIACTNIFPLGRDRMYRRYWIFPSIPGLFIEEDYSGLTEDMLLPRPSSFQNNVQSQDPQVSTKTGASLMSESTSSIDQGPCDDSVQLPKPVHKPNRWCFYSSCEQLDQLIGALNSRGYRESALKETLLQEKSRICAQLARFSEEKFHFSDKPQTDSKSTYSRGKSSNACDPSQMSAERQLELRLRDFLLDIEDRIYQGTLGAIKVTDRHIWRSALESGRYELLNEENKENGIIKTVNEDVEEMEIDEPAKVIVKDRLLGIKTETPSSVSTNASTPQSVSNVVHYLAMALFQIEQGIERRFLKAPLDASDSGRSYKTVLDRWRESLLSSASLSQVFLHLSTLDRSVIWSKSILNARCKICRKKGDAENMVLCDGCDRGHHTYCVRPKLKTVPEGDWFCPECRPKQRSRRLSSRQRPSLESDEELEDSLEGEDDEVDDDDEEGQSEEEEYEVEQDEDDSQEEEEVSPPKRGRPQVRLSIKTRGKLSSSFSSRGQRQDPGRYTSRSQQSTPKTTLSSKTTSRSLRKIKSAPPTETKSLRIASRSTRQSHDPLQADVFVELLSPRRKRRGRKSANNTPESSPNLPNFRVIATKSSEQSRSLNVASKLSLQDSESKRRGRKRQSTESSPMTLNRRSSGRQGGVHELSAFEQLVVELVRHDDSWPFLKLVSKIQVPDYYDIIKKPIALNIIREKVNKCEYKLASEFIDDIELMFSNCFEYNPRNTSEAKAGSRLQAFFHIQAQKLGLHVTPGNVDQVSTPPAAKKSRI
Protein: Uncharacterized protein (Q554J2)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MKYHIQSINQKSPPHVPKLGVQTLNVDEYIEICANNQFKCGNYNIPLALHGVDENLPFRYHRLTHSPDRINNRRSYTKYNVKILSIFSNVSNHRVYDLLPFSQISSTNSNPNVCSNNENDNETYDSETDNETNHSETDNIVEDTIILFQFEVLFIAATG
Protein: Nuclear pore complex-interacting protein family member A9 (A0A0B4J1W7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFCCLGYEWLSGGCKTWHSAWVINTLADHRHRGTDFGGSPWLLIITVFLRSYKFAISLCTSYLCVSFLKTIFPSQNGHDGSTDVQQRARRSNCRRQEGIKIVLEDIFTLWRQVETKVRAKIRKMKVTTKVNRHDKINGKRKTAKEHLRKLSMKEREHGEKERQVSEAEENGKLDMKEIHTYMEMFQRAQALRRRAEDYYRCKITPSARKPLCNRVRMAAVEHRHSSGLPYWPYLTAETLKNRMGHQPPPPTQQHSIIDNSLSLKTPSECVLYPLPPSADDNLKTPPECLLTPLPPSALPSADDNLKTPAECLLYPLPPSADDNLKTPPECLLTPLPPSAPPSADDNLKTPPECVCSLPFHPQRMIISRN
Protein: Lateral signaling target 1 protein (P91820)
Organism: Caenorhabditis elegans
Interaction partners:
- Fem-3 mRNA-binding factor 2
- Ecdysone-induced protein 74EF
- Mitogen-activated protein kinase mpk-1
- Lateral signaling target protein 2
- Dual specificity protein phosphatase lip-1
- Suppressor of hairless protein homolog
- Ack-related non-receptor tyrosine kinase
- Sorting nexin lst-4
Sequence:
MCSTFILPPRRNNCNKSSSTIAYSKSQHEAPKQLLQLRSEIKPLIPLNQPSNFWESSQDSGVLSSLSSSPQQRSGLRSQKLHLTYIEKNKRVRAMIPQQQHYHAFDRPTHYNSRKTSGPPPLMRTPSSGFSSASSSENMFSGLTLSDNENKIHEIMDPSVDVDLDMFLLPDCRYKQPVQPSTSTSRNNVSQISGSSRLNGSTRHVAPIVPKVAMPSELSYANVKRSSGYVDYMPTTYNSNVTSNSSAASVPMSPGTWVRCHYCWESYVKLCQRVANLEPLISCDGPWNWHTLYDMQGRVTCPRLWFAQLDRAGSEMVEQMGHARNVPV
Protein: cDNA FLJ77882, highly similar to Homo sapiens kruppel-like fetal and embryonic globin gene activator (FKLF) mRNA (Q53QU8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHTPDFAGPDDARAVDIMDICESILERKRHDSERSTCSILEQTDMEAVEALVCMSSWGQRSQKGDLLRIRPLTPVSDSGDVTTTVHMDAATPELPKDFHSLSTLCITPPQSPDLVEPSTRTPVSPQVTDSKACTATDVLQSSAVVARALSGGAERGLLGLEPVPSSPCRAKGTSVIRHTGESPAACFPTIQTPDCRLSDSREGEEQLLGHFETLQDTHLTDSLLSTNLVSCQPCLHKSGGLLLTDKGQQAGWPGAVQTCSPKNYENDLPRKTTPLISVSVPAPPVLCQMIPVTGQSSMLPAFLKPPPQLSVGTVRPILAQAAPAPQPVFVGPAVPQGAVMLVLPQGALPPPAPCAANVMAAGNTKLLPLAPAPVFITSSQNCVPQVDFSRRRNYVCSFPGCRKTYFKSSHLKAHLRTHTGEKPFNCSWDGCDKKFARSDELSRHRRTHTGEKKFVCPVCDRRFMRSDHLTKHARRHMTTKKIPGWQAEVGKLNRIASAESPGSPLVSMPASA
Protein: Calcium-responsive transcription coactivator (SS18-like protein 1) (Q91XJ0)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional activator which is required for calcium-dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP.
Subcellular location: Nucleus {ECO:0000269|PubMed:14716005, ECO:0000269|PubMed:15488321, ECO:0000269|PubMed:15866867}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to nuclear bodies. Colocalizes with SGO1 at kinetochore (By similarity). {ECO:0000250}.
Interaction partners:
- Zinc finger protein neuro-d4
- Actin-like protein 6B
- Double PHD fingers 3
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1
- Double PHD fingers 2
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- AT-rich interaction domain 1A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1
Sequence:
MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILDYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALSQSGSSQGLHPQGSLSDTVSTGLPPASLMQGQIGNGPNHVSMQQTAQSTLPTTSMSMSGSGHGTGPGYSHSGPTSQSVPMQGQGAISNYVSRTNINMQSNPVSMMHQQAARPTTTQRRVEASITRARRPLHDGPGWQGGSMMGQRPMAPYRPSQQGSSQQYLGQEEYYSEQYSHSQGSAEPMSQQYYPDGHSDYAYQQSSYTEQSYDRSFEDPTQHYYEGGNSQYSQQQAGYQQGTAQQQTYSQQQYPNQQSYPGQQQGYGPAQGAPSQYSGYQQGQGQQYGSYRTSQTGPSAQQQRPYGYEQGQYGNYQQ
Protein: Carboxypeptidase Rv3627c (EC 3.4.16.-) (O06380)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Carboxypeptidase that cleaves terminal D-alanine from peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala and/or D-Ala-D-Ala peptide bonds. Exerts important effects on mycobacterial cell morphology and cell division.
Interaction partners:
- D-alanyl-D-alanine carboxypeptidase DacB1
- D-alanyl-D-alanine carboxypeptidase DacB2
- Hydrolase
- tRNA
- Hypoxanthine-guanine phosphoribosyltransferase
- Protein Rv1367c
- Possible penicillin-binding lipoprotein
- Uncharacterized protein Rv0906
- PASTA domain-containing protein
- Peptidoglycan D,D-transpeptidase PbpA
Sequence:
MGPTRWRKSTHVVVGAAVLAFVAVVVAAAALVTTGGHRAGVRAPAPPPRPPTVKAGVVPVADTAATPSAAGVTAALAVVAADPDLGKLAGRITDALTGQELWQRLDDVPLVPASTNKILTAAAALLTLDRQARISTRVVAGGQNPQGPVVLVGAGDPTLSAAPPGQDTWYHGAARIGDLVEQIRRSGVTPTAVQVDASAFSGPTMAPGWDPADIDNGDIAPIEAAMIDAGRIQPTTVNSRRSRTPALDAGRELAKALGLDPAAVTIASAPAGARQLAVVQSAPLIQRLSQMMNASDNVMAECIGREVAVAINRPQSFSGAVDAVTSRLNTAHIDTAGAALVDSSGLSLDNRLTARTLDATMQAAAGPDQPALRPLLDLLPIAGGSGTLGERFLDAATDQGPAGWLRAKTGSLTAINSLVGVLTDRSGRVLTFAFISNEAGPNGRNAMDALATKLWFCGCTT
Protein: PHD finger-like domain-containing protein 5A (Q38AM4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-binding protein, putative
- Spliceosome-associated protein, putative
- G10 protein
- Splicing factor 3B subunit 1, putative
- Cell division control protein, putative
- Uncharacterized protein
- Splicing factor 3B subunit 10
- Sm protein G
- U2 small nuclear ribonucleoprotein B, putative
- Small nuclear ribonucleoprotein E
Sequence:
MLRHSKQEQQMCRKLPGVDIGYVCQQHEGRCVICDLQFDEVLPTMREVRICSDCGFGREGDERCVMCNASKPTEVAYYCQYCVALEKDRDGCPRVLNQSRHQRIATVRTR
Protein: GDP-mannose 4,6 dehydratase (EC 4.2.1.47) (GDP-D-mannose dehydratase) (GMD) (Q1ZXF7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Participates in the synthesis of GDP-L-fucose, catalyzing the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose (GDP-4-dehydro-alpha-D-rhamnose) which is further catalyzed by GDP-L-fucose synthase (ger). GDP-L-fucose is important for the synthesis of fucosylated N-glycans which are expressed on the cell surface.
Interaction partners:
- GDP-L-fucose synthase
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Mannose-1-phosphate guanylyltransferase regulatory subunit alpha
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dolichol-phosphate mannosyltransferase subunit 1
- Bifunctional glycosyltransferase pgtA
- UDP-glucose 4-epimerase
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol phosphate-mannose biosynthesis regulatory protein
- UDP-galactose:fucoside alpha-3-galactosyltransferase
Sequence:
MSEERKVALITGITGQDGSYLTEFLISKGYYVHGIIQKIFHHFNTIVKNIYIKIDMLKEKESLTLHYGDLTDASNLHSIVSKVNPTEIYNLGAQSHVKVSFDMSEYTGDVDGLGCLRLLDAIRSCGMEKKVKYYQASTSELYGKVQEIPQSETTPFYPRSPYAVAKQYAYWIVVNYREAYDMYACNGILFNHESPRRGPTFVTRKITRFVAGIACGRDEILYLGNINAKRDWGHARDYVEAMWLMLQQEKPEDFVIATGETHSVREFVEKSFKEIDIIIKWRGEAEKEEGYCEKTGKVYVKIDEKYYRPTEVDLLLGNPNKAKKLLQWQIKTSFGELVKEMVAKDIEYIKNGDKYN