wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized exonuclease domain-containing protein At3g15140 (EC 3.1.-.-) (Q8W566)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transmembrane protein
- Putative small RNA degrading nuclease 4
- Small RNA degrading nuclease 5
- RNA exonuclease 4
- Small RNA degrading nuclease 1
- Pentatricopeptide repeat-containing protein At2g17033
Sequence:
MASAFSAFRVSLSRISPFRDTRFSYPATLALAHTKRIMCNSSHSVSPSPSPSDFSSSSSSSSSSPSTFSLMETSENARWRPMCLYYTHGKCTKMDDPAHLEIFNHDCSKELRVAAADLERKKSQEFNFFLVIDLEGKVEILEFPILIVDAKTMEVVDLFHRFVRPTKMSEQAINKYIEGKYGELGVDRVWHDTAIPFKQVVEEFEVWLAEHDLWDKDTDWGLNDAAFVTCGNWDIKTKIPEQCVVSNINLPPYFMEWINLKDVYLNFYGREARGMVSMMRQCGIKLMGSHHLGIDDTKNITRVVQRMLSEGAVLKLTARRSKSNMRNVEFLFKNRIK
Protein: Protein FLOURY ENDOSPERM 6, chloroplastic (SKIPa-interacting protein 4) (Q10F03)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in compound starch granule formation and starch synthesis in endosperm. May act as a regulatory scaffolding protein and affect starch synthesis and compound starch granule formation through direct interaction with isoamylase 1 (ISA1). Binds starch, amylopectin and amylose through its C-terminal carbohydrate-binding domain (CBM) in vitro.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:24456533}. Note=Localizes to granule-like structures in chloroplasts. {ECO:0000269|PubMed:24456533}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Os01g0633400 protein
- Os04g0136700 protein
- Os01g0920000 protein.
- Os04g0382300 protein
- Putative B3 domain-containing protein Os10g0158600
- Os04g0380000 protein
- Os05g0364650 protein
- Os04g0679600 protein
- CBS domain containing protein
Sequence:
MLPLLLPLPVTPPPPLPSPTLTLAPASAPRRRLVLLAAAAPHHHHHHRRRRVYRRQRAAPTQTRAPRRTLSASNAARGEEDLEEAIYEFMRRSDKPGAFPTRAELVAAGRADLAAAVDACGGWLSLGWSSGGAEAGRASSSVGVHPDYPPEAGAAAAAGGASDLAQGAVWASSREAEASPSGRQPETEEEETETKFGTGLDGMLTRLQRERERVRPPLPRSSDGAGGERDNVALMGQSGAPSHSATGGRYTPKVPDNGNIHSYHPQNGALEHNKSSKSLTNDAWRTWSLDKGGFSDFQAAEIHSTNSRKSFRHDGLDILAQDDVHGPSNGVAVHDYDINDVDSERDDIHARLQNLELDLTAALHTLRSRFDKVISDMSEGDGAKAPNGLSDDWEFEETKVMQAQEELRSIRAKIAVLEGKMALEIIEKNKIIEEKQRRLDEAEKALSELRTVYIVWSNPASEVLLTGSFDGWTSQRRMERSERGTFSLNLRLYPGRYEIKFIVDGVWRNDPLRPLVSNNGHENNLLTVT
Protein: Proteasome subunit alpha type-7 (Proteasome subunit RC6-1) (Proteasome subunit XAPC7) (Proteasome subunit alpha-4) (alpha-4) (O14818)
Organism: Homo sapiens (Human)
Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000269|PubMed:34711951}.
Interaction partners:
- Proteasome maturation protein
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3
- 26S proteasome regulatory subunit 10B
- Proteasome subunit beta type-2
- Proteasome subunit beta type-9
- Proteasome subunit beta type-8
- 26S proteasome regulatory subunit 4
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-5
Sequence:
MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS
Protein: UPF0742 protein SPAC977.02 (P0CU07)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to cytoplasmic dots and the nuclear envelope. {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSASSKFRSFTFGCVVVYHNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISR
Protein: ADP-ribosylation factor-like protein 6-interacting protein 6 (ARL-6-interacting protein 6) (Aip-6) (Phosphonoformate immuno-associated protein 1) (Q8N6S5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus inner membrane {ECO:0000250|UniProtKB:Q8BH07}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSFAESGWRSALRRRGPGTPGPVARPSYSSFTQGDSWGEGEVDEEEGCDQVARDLRAEFSAGAWSEPRKRSVLPPDGNGSPVLPDKRNGIFPAAAGSRAQPRRWPVQVLSILCSLLFAILLAFLLAIAYLIVKELHAENLKNEDDVDTGLLGFWTLLIISLTAGFSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKLTGHSFHMGYSMAILNGIVAALTVAWCLM
Protein: Zinc finger protein ZFPM2 isoform X1 (Zinc finger protein ZFPM2a isoform X1) (Zinc finger protein, FOG family member 2a) (F1R4T3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- GATA-binding protein 4.
- Estrogen-related receptor gamma b
Sequence:
MSRRKQSNPRQIKRPLDGGLEEEEEECISDANELAAKEEFSAEENFPADFEPDNLTCEDMEYFCGKGEENGNREMGETEMETDSEKTRHPPLEPEEWDGPRELDLFNKDGERRIHSRQQLPVGTTWGPFEGKIELNTDAQKTKPHVPLVLNAGPRWLLDVTWQGTDDNKNNCVVYSKGGQLWCTTTKNMMEGEELVAFAVDFDSRLQAVNHMSLGEGMYPARLLDTIQLLPQQAAMASILPTAIVNKDIFPCKACGIWYRSERNLQAHLMYYCSGRQREPDNVPEETDAISHQTPSICPFPQCNKSFSNPRALEMHLSSHSSVKMEETLPPGTSLKCTICNFTADSLLTFQHHILSHLSQAAFRCNHCHISFQNHRELLQHQDLHGHSGKIHRESDSENSPRGGEDSLQAARAELSGRKDIVMQSPKNTPNKANSPDGELERPEKKPTLGLQKGDSHPGSKASFSYTRIKSEPSSPRLASSPVQHNMGPTFPMGPFLSQFAFSQDISVVPQASEILAKMSELVHRRLRHGGNSYPPVIYSPLMPKGATCFECNITFNNLDNYLVHKKHYCNSRWQHMTKSPDFSSVPDKVSDAISPNSGHTSVGMLPGCLPSDTDSHVVTTACLNSSVLDIMNAGGKVPEKELTGQVKKVTTPTGVEERLGGKQPEVKSPSTSLVDGDSDPNKTTCEACNITFSRHETYMVHKQYYCATRHDPPMKRMSAKVPAMQRTMRTRKRRKMYEMCLPEDQRQPMGPQPGFLSLHTLGNPCTSQETVENLADRFHPRCDIFPGLVPKHLDASLTITKSILAPKGNTVADPQELDAPIDLSKKCSPLPDKSCNSPKRLLDYHECTVCKISFNKVENYLAHKQNFCPVTAAHGEVGNLEQPIFPGMKTEGNNADDVYDKSSVKCEKNGGNKLMQNGGMFPPHLGSAPDLKAFADAQLMSSKDENKNMFLPHSLYPGAIKKVKGTEQISPYFGIKSGDYMAGSLVVQAEAAEQEQSSNGAGEPGTESLAANGCPHPNKDPLPLLPKNRSMVIVNGGHKEDRQTPATPQQENQPHNTSLPEEQTSPTWGAENPPDPNENVSPTSKSPVEDSAPAGKGINGSASPAGSGKYCRLCDIQFNNLSNFITHKKFYCSSHAAEHVK
Protein: Odorant-binding protein 56g, isoform A (A1ZBQ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRATFALTLLLGCLSGILAQANIDSSVSKELVTDCLKENGVTPQDLADLQSGKVKAEDAKDNVKCSSQCILVKSGFMDSTGKLLTDKIKSYYANSNFKDVIEKDLDRCSAVKGANACDTAFKILSCFQAAN
Protein: Suppressor of variegation 2-10, isoform A (Zimp-A) (Q7KNF5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVQMLRVVELQKILSFLNISFAGRKTDLQSRILSFLRTNLELLAPKVQEVYAQSVQEQNATLQYIDPTRMYSHIQLPPTVQPNPVGLVGSGQGVQVPGGQMNVVGGAPFLHTHSINSQLPIHPDVRLKKLAFYDVLGTLIKPSTLVPRNTQRVQEVPFYFTLTPQQATEIASNRDIRNSSKVEHAIQVQLRFCLVETSCDQEDCFPPNVNVKVNNKLCQLPNVIPTNRPNVEPKRPPRPVNVTSNVKLSPTVTNTITVQWCPDYTRSYCLAVYLVKKLTSTQLLQRMKTKGVKPADYTRGLIKEKLTEDADCEIATTMLKVSLNCPLGKMKMLLPCRASTCSHLQCFDASLYLQMNERKPTWNCPVCDKPAIYDNLVIDGYFQEVLGSSLLKSDDTEIQLHQDGSWSTPGLRSETQILDTPSKPAQKVEVISDDIELISDDAKPVKRDLSPAQDEQPTSTSNSETVDLTLSDSDDDMPLAKRRPPAKQAVASSTSNGSGGGQRAYTPAQQPQQSGGNVFKKPQKAEELYKRVHLGVWLRPRKPKPESSRRPNVG
Protein: Proline-rich protein 15 (Q8IV56)
Organism: Homo sapiens (Human)
Function: May have a role in proliferation and/or differentiation.
Interaction partners:
Sequence:
MADSGDAGSSGPWWKSLTNSRKKSKEAAVGVPPPAQPAPGEPTPPAPPSPDWTSSSRENQHPNLLGGAGEPPKPDKLYGDKSGSSRRNLKISRSGRFKEKRKVRATLLPEAGRSPEEAGFPGDPHEDKQ
Protein: ESAT-6-like protein EsxI (Antigen Mtb9.9B) (P0DOA6)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Secreted {ECO:0000305|PubMed:19876390}. Note=Probably secreted via the ESX-5 / type VII secretion system (T7SS). {ECO:0000305|PubMed:19876390}.
Interaction partners:
- ESAT-6-like protein EsxJ
- ESAT-6-like protein EsxW
- ESAT-6-like protein EsxK
- ESAT-6-like protein EsxP
- ESAT-6-like protein EsxO
- 6 kDa early secretory antigenic target
- ESAT-6-like protein EsxN
- ESAT-6-like protein EsxL
- Probable cold shock protein A
- Large ribosomal subunit protein uL1
Sequence:
MTINYQFGDVDAHGAMIRAQAGSLEAEHQAIISDVLTASDFWGGAGSAACQGFITQLGRNFQVIYEQANAHGQKVQAAGNNMAQTDSAVGSSWA
Protein: Protein EFFECTOR OF TRANSCRIPTION 1 (AtET1) (F4JU69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator involved in the regulation of cell differentiation in meristems (By similarity). Binds DNA without sequence preference.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17991462}. Nucleus {ECO:0000269|PubMed:17991462}. Note=Localizes to the cytoplasm in non-differentiating cells and to the nucleus in differentiating cells. {ECO:0000269|PubMed:17991462}.
Interaction partners:
- Protein EFFECTOR OF TRANSCRIPTION 3
- Uncharacterized protein
- At4g31150
- B3 domain-containing protein At2g36080
Sequence:
MLVVLQIHSSINVKVFASRLRKHFFFTRRKITRIATCLSSSRCPLYPSHWNLCRWNNKQGGTEIGLLIGGLIVFRQTLKSDQETKREQKKRDWILVTAFPSPSCSPCSRETTTFELIMTPFFQSGRVSPDLCFCVNPFQKLQNSQDFCGLLLNFSRFRSKAKGANEKENFREGKDLVGRNRVQGAFQGLYELSHDHGRKDDVLVANLGQPESIRSRLRSYSRSFAHHDLLKQGLSQTILPTTQNKSDNQTEEKKSDSEEEREVSSDAAEKESNSLPSILRLSRSRPQPVSEKHDDIVDESDSASACGVLLEDGTTCTTTPVKGRKRCTEHKGKRLSRVSPGIHIPCEVPTVRECEETENICGVILPDMIRCRSKPVSRRKRCEDHKGMRVNAFFFLLNPTERDKAVNEDKSKPETSTGMNQEGSGLLCEATTKNGLPCTRSAPEGSKRCWQHKDKTLNHGSSENVQSATASQVICGFKLYNGSVCEKSPVKGRKRCEEHKGMRITS
Protein: LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 1.4 (EC 2.7.11.1) (Probable receptor-like serine/threonine-protein kinase LRK10L-1.4) (F4HQ17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P0C5E2}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Proteasome subunit beta type-3-B
- Proteasome subunit beta type-3-A
- Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' theta isoform
- Probable ethanolamine kinase
Sequence:
MYYPLSSSLMFFILFSLFYHLPCESSKCESLFQCGNITASFPFWGGDRHKHCGHPLLELRCDQNKSTSLFISDQEFFVLHVDQTSYSLTLARPDLLHSFCSLTFTNTTLPPEIFELSPAYKSVTFYHCYPVLPDLSNYTCPVIGPISVSGNPEDHETCFPNFAANVPTSFVTKEKKLNIANLESVLEKGFEVNMNVIMKACQACSYSNESCGFDENFPFEVKCKPHHSPTDTSLSIGAKAGIAVASVSGLAILLLAGLFLCIRRRRKTQDAQYTSKSLPITSYSSRDTSRNPTSTTISSSSNHSLLPSISNLANRSDYCGVQVFSYEELEEATENFSRELGDGGFGTVYYGVLKDGRAVAVKRLYERSLKRVEQFKNEIEILKSLKHPNLVILYGCTSRHSRELLLVYEYISNGTLAEHLHGNRAEARPLCWSTRLNIAIETASALSFLHIKGIIHRDIKTTNILLDDNYQVKVADFGLSRLFPMDQTHISTAPQGTPGYVDPEYYQCYQLNEKSDVYSFGVVLTELISSKEAVDITRHRHDINLANMAVSKIQNNALHELVDSSLGYDNDPEVRRKMMAVAELAFRCLQQERDVRPAMDEIVEILRGIKDDEKKRVLVKSPDVVDIECGGGDDVGLLRNSVPPPISPETDKWTSSSDTAASL
Protein: LP22668p (Roundabout 3, isoform A) (Q9VPZ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein slit
- Protein commissureless 1
- receptor protein-tyrosine kinase
- Protein son of sevenless
- Ephrin
- Rho GTPase-activating protein 39
- Syndecan
- Netrin-B
Sequence:
MDLRFVFIVFLLKWTHAQGSHPPRIVEHPIDTTVPRHEPATLNCKAEGSPTPTIQWYKDGVPLKILPGSHRITLPAGGLFFLKVVNSRRETDAGIYWCEAKNELGVARSRNATLQVAVLRDEFRLEPQNTRIAQGDTALLECAAPRGIPEPTVTWKKGGQKLDLEGSKRVRIVDGGNLAIQDARQTDEGQYQCIAKNPVGVRESSLATLKVHVKPYIIRGPHDQTVLEGASVTFPCRVGGDPMPDVLWLRTASGGNMPLDRVSVLEDRSLRLERVTIADEGEYSCEADNVVGAITAMGTLTVYAPPKFIQRPASKSVELGADTSFECRAIGNPKPTIFWTIKNNSTLIFPGAPPLDRFHSLNTEEGHSILTLTRFQRTDKDLVILCNAMNEVASITSRVQLSLDSQEDRPPPIIISGPVNQTLPIKSLATLQCKAIGLPSPTISWYRDGIPVQPSSKLNITTSGDLIISDLDRQQDQGLYTCVASSRAGKSTWSGFLRIELPTNPNIKFYRAPEQTKCPSAPGQPKILNATASALTIVWPTSDKAGASSFLGYSVEMYCTNQSRTWIPIASRLSEPIFTVESLTQGAAYMFIVRAENSLGFSPPSPISEPITAGKLVGVRDGSESTGTSQLLLSDVETLLQANDVVELLEANASDSTTARLSWDIDSGQYIEGFYLYARELHSSEYKMVTLLNKGQGLSSCTVPGLAKASTYEFFLVPFYKSIVGKPSNSRRMRTLEDVPEAPPYGMEAIQFNRTSVFLKWLPPQPNRTRNGILTSYNVVVKGLDVHNTTRIFKNMTIDAAAPTLLLANLTTGVTYYIAVAAATRVGVGPFSKPAVLRIDARTQSLDTGYTRYPISRDIADDFLTQTWFIVLLGSIIAIIVFLLGALVLFKRYQFIKQTSLGSLHGNHAIGTVRKFPTLPLNGGGAVGAGGSNSTAAAGQSGHGLWIDPTSGVWRQAAGGGNPGGVGSCTTKEQLPGYAQATAQQGQQPTLLPDYERLSPLNMPDYAEVACSTFKSPTHGAPPMGGGGGGQSASLYDSCGAYATTNVVANVKLYQNRYATKPNQSSGSNNNNHQGNDYQSTGMYSAPPSAHYGCLEPKQQQQQQQPNLMTTSTASTAILTNSPAKVKKINITENKMDQLEGKSERTNPFNQQQQLLLASNALKQGLGAYANTTLAAQMASGGGAGTLRRQRQPKTLYKSENNILGKSGLRQNTMNASVGAPSNGQMDFLTGGPPSEGGDFSGLGLCNSTNQLLNDWASSASIAAPGDYHFGSKQPSKQHLYVKAKDGTWSAVSSDAYQSFKHQQQHHPFLAGSGDNTKSLASVNSLAGDSKFLSSFGSSANV
Protein: Serine/threonine-protein kinase ppk18 (EC 2.7.11.1) (Q8TFG6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- mRNA stability protein mug134
- Serine/threonine-protein kinase cek1
- Serine/threonine-protein kinase sck1
- cAMP-dependent protein kinase catalytic subunit
- Serine/threonine-protein kinase tor2
Sequence:
MVMQERNSNEDNKVNHGIDNIYVLELDLDGSVLFASTNFSQITGISSLELTGKPAALLSSDQEIFNAAIEQLLDDDSHSVKIHTVISKLPSLEENVFVQDEEMELQSKSVELDCVGVLIRDPLTSRPSHTLWVLQPLKPTRITRQEIGQQLTETLGFGAQLLAQHLEKLQTVPSTDSLPPFETVLCRVCDHEIQNWYFEHHTELCLLIHHAEARAQEANDLLNEQRNALQSLLDSLDDQIEPDVSYLGVPLAAVLPSSITSSAKSNSRSSLSQKIRNYISNMLFDAISYTDSCLAIHLPFIPESTTREDNQPFSEIRLLSPASEVFNAKTLSWCLPHIDDPGLQLMFENTDALVKKKLDAINRLSNIIYYSERVRCEIEDQVQTIIEQSIQVDGYDEPLSTTTPTLIEPIQETLMTQSPIIECEPFNTVKPSVSPEEVHDISQFNHRNDPPITAASVDSSNSFSVHRSSTNHSSTNSGSPNLSRRNNLAIPIASRRKSVSAVNTLYGVGSSYTSESFPFSKLTVPVERNSFRETESPKPFLSRQIGISTLSSNISSGKGTPSIQDYEIIKPISKGTFGTVYLSRKNTTGEIYAIKVLRKVDMISKNQVANVKAERAVLMAQEESAFVAKLYYAFQSRDYLYLVMEFMNGGDCASLLKSLYTIPESWAKIYIAEVALGLEHLHRLGIIHRDIKPDNILMSITGHLKLADFGLSQLGLTTRQLRLQKGKNNILSPPSFQSPTALGDPGDNIASSPLILPTSVSAFSYDEKSQKQKTELATFTTYKEDDTTTTTRTSIDSISSKYLESPVDSQKVNRTPNLQSVPFFRQPDAPKRFVGTPDYLAPETLRGSTQDDMVDWWALGCVLFEFLFGYPPFHAETPEKVFENILANNIAWPDLEMYPCSEEALDLINGFLQPNPERRLGFSDINEIKEHPFFNGINWDDIFSHEAPFIPAPETPLDTAYFDSRGAGAAESNMSSSVNSGEEVSKDNNVSQERGSQFLRSSHGRSRERSTSARRSRRFSEANSEFDEFGPFSYKNLSVLERANRNAIEKIRSEIAGKLHISPPDPHIGYTPGSDMPSAKLYDQQLTLSPSLMTNQGSNFSSTDSTPRKSINSSDVESRSKTDGPKSMHDLIKQLHMRKHSSHTNQSTGSSESDDLFNLDLPISNLETSYPFKIEEGQASPLSSPLSKTPPFFSSSVPLKALICVSKLNLFSELIKLLKSYKFQVSIVTDEDKMLRTLMADEKFSIIFLQLDLTRVSGVSILKIVRSSNCANRNTPAIALTPTRIDINAAIPRMFDGRLYLPINAFLLRGYIARLCNK
Protein: COG-1A (Homeobox domain-containing protein) (G5EGE2)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- LIM/homeobox protein lim-6
- C2H2-type domain-containing protein
- Nuclear hormone receptor family member nhr-67
- Protein lin-11
- Transcription factor che-1
Sequence:
MSLIMSEPPQLTTPDDKDVENRKHSSTYSISNLLLEKKESSPSGSSSEDDSASSNDDDQRSPSATSSFIFPPASSSSSSESATSPTQIMAQLMANGGAVDPGLQAYFFLLQSQLNSQSMMNRVTQENVSRALTSFNLLNNLPGALPSLSPMGRLQHSMQLSPNSLNMQKKQSRPTFTGHQIYQLERKFEQTKYLAGADRAQLAQELNMSESQVKVWFQNRRTKWRKKEAADNALVKRGASGDKSPCSLSPFLSAGI
Protein: Disintegrin and metalloproteinase domain-containing protein 1 (ADAM 1) (EC 3.4.24.-) (Fertilin subunit alpha) (P70505)
Organism: Rattus norvegicus (Rat)
Function: May be involved in sperm-egg fusion.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 2
- Calmegin
Sequence:
MSVAASASRSASTLCSPQIQQGALKEAKVPPHIWAARHWNLGLRLVPGHASVRAGILVLLIFLPSTLCDLGSVYDSSYETVIPERLPGQGSDDPGGKVSYVLLMQGQKQLLHLEVKGHYSERNFPVYSYHHGILGQEVPLLSQACHYEGHIEGVPGSFVSVSICSGLRGVLIKEETAYGIEPLLFSTDFEHILYTMAHQPVVLCNVTPTDSLGDSSQRQGSSKTDELLALSDLWSHAKYVEMFVVVNHQRFQMWGSDVNTTVQAVVDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQATLRNFNLWRQEKLMGRVRHDVAHLIVGHRPGANEGQAFLDGACSGGFAAAVEAFHHEDVLLFAALMAHELGHNLGIRHDRPGCTCGPKHLCLMHETISKTSGFSNCSSDHFLRFLHDHRGACLLDRPWHQSHKRRDAHCGNGVVEESEECDCGNACDSHPCCEPTCTLKVGAQCSEGLCCYKCTFKKKGTLCRPAEDVCDLPEYCNGITGECPANSYMQDGTQCDRIYYCSGGLCKNPDKQCARIYGYPARSAPEECYISVNTKANRFGNCGHPTSANLKYEACSNEDIFCGKLVCTDVRYLPQVKPLHSLLQIPYGDDWCWSMDAYNVTDIPDYGDVQGGTYCAPKKVCMESICTGHATLQYDCHPQEMCHGNGVCNNFKHCHCDAGFSPPDCSSGGNGGSVDSGPVGKPADRNLSLFGVGESPDSRMEDEEINLKVVVLVVPIFLIVLLCCLMLIAYLWSEVQEAVSPGSSSTTSSSESESD
Protein: Serine/threonine-protein kinase atg1 (EC 2.7.11.1) (Autophagy-related protein 1) (Q86CS2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Serine/threonine protein kinase involved in autophagy. Involved in the control of autophagic vacuolar cell death. Required for normal survival when exposed to pathogenic bacteria S.typhimurium by promoting autophagic degradation of intracellular S.typhimurium.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
Interaction partners:
- Autophagy-related protein 8
- Autophagy-related protein 9
- Autophagy protein 5
- Ubiquitin-like protein atg12
- Autophagy-related protein 18
- Autophagy-related protein 13 N-terminal domain-containing protein
- Autophagy-related protein 3
- Probable autophagy-related protein 17
- Beclin-1-like protein A
- Protein raptor homolog
Sequence:
MKRVGDYILDKRIGWGAFAQVYKGFSIKTNEPFAIKVVDVCRLADKNSKLTENLNYEIRILKELSHTNIVRLYDVLNEETDPTFIYMIMECCEGGDFSKYIRTHKKLTEEKALYFMKQLANGLKFLRQKQIVHRDLKPQNLLLSDDSEHPILKIGDFGFAKFIDPFSLSDTFCGSPLYMAPEILHRKNYTVKADLWSVGIILYEMLVGEPAYNSGSVPDLLNQLQNKKIKLPSHISSDCQNLIYSLLQIDVEKRISWEDFFNHKWLNLNNNDSYKNNSGNYFNNNNINNNNNNNTNNNNNNISYPISINSNNTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNYYNNNNSPPNVYHASSLPYDFNNNNNNNNSNNYNNNTNVPNSLPFAYNNNIYSSPTEAIPQPTTLNKSKSLENTGNTIRAHPFKDDKKSTTIQQPQQQQQQQQQQQQQQQQQQQQQQQQQQQNRQLSNLSTDFERDLVILDGEELESMERVFNRAVAIAELGDLRQNEPLECVPLYILALKLMKSKIPNDPSSSPDKFINTFTEYKRKLVHIFSTSNTSVKNQDHHSSFSPNRFIYENALEFGKKGAVEELYNNYPTSLQFYTDGTLLLEYLSSIVIDSDDQEIIKKYLNAFEVRTQICKKNYENSKNTVLNTNSIQNNT
Protein: Very long chain fatty acid elongase 2 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL2) (ELOVL fatty acid elongase 2) (ELOVL FA elongase 2) (Elongation of very long chain fatty acids protein 2) (Very long chain 3-ketoacyl-CoA synthase 2) (Very long chain 3-oxoacyl-CoA synthase 2) (Q9NXB9)
Organism: Homo sapiens (Human)
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA), acting specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA. May participate in the production of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:20937905}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03202}.
Interaction partners:
- Acyl-CoA
- Very-long-chain 3-oxoacyl-CoA reductase
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Very-long-chain enoyl-CoA reductase
- Acyl-CoA wax alcohol acyltransferase 1
- Diacylglycerol O-acyltransferase 2
- Acyl-CoA 6-desaturase
Sequence:
MEHLKAFDDEINAFLDNMFGPRDSRVRGWFMLDSYLPTFFLTVMYLLSIWLGNKYMKNRPALSLRGILTLYNLGITLLSAYMLAELILSTWEGGYNLQCQDLTSAGEADIRVAKVLWWYYFSKSVEFLDTIFFVLRKKTSQITFLHVYHHASMFNIWWCVLNWIPCGQSFFGPTLNSFIHILMYSYYGLSVFPSMHKYLWWKKYLTQAQLVQFVLTITHTMSAVVKPCGFPFGCLIFQSSYMLTLVILFLNFYVQTYRKKPMKKDMQEPPAGKEVKNGFSKAYFTAANGVMNKKAQ
Protein: Golgin A2 (B7ZC06)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWPQPRLPPRPAMSEETRQSKLAAAKKKLREYQQRNSPGVPTGAKKKKKIKNGSNPETTTSGGCHSPEDTPKDNAATLQPSDDTVLPGGVPSPGASLTSMAASQNHDADNVPNLMDETKTFSSTESLRQLSQQLNGLVCESATCVNGEGPASSANLKDLELAVALDSSYVTNKQLNITIEKLKQQNQEITDQLEEEKKECHQKQGALREQLQVHIQTIGILVSEKAELQTALAHTQHAARQKEGESEDLASRLQYSRRRVGELERALSAVSTQQKKADRYNKELTKERDALRLELYKNTQSNEDLKQEKSELEEKLRVLVTEKAGMQLNLEELQKKLEMTELLLQQFSSRCEAPDANQQLQQAMEERAQLEAHLGQVMESVRQLQMERDKYAENLKGESAMWRQRMQQMSEQVHTLREEKECSMSRVQELETSLAELRNQMAEPPPPEPPAGPSEVEQQLQAEAEHLRKELEGLAGQLQAQVQDNEGLSRLNREQEERLLELERAAELWGEQAEARRQILETMQNDRTTISRALSQNRELKEQLAELQSGFVKLTNENMEITSALQSEQHVKRELGKKLGELQEKLSELKETVELKSQEAQSLQQQRDQYLGHLQQYVAAYQQLTSEKEVLHNQLLLQTQLVDQLQQQEAQGKAVAEMARQELQETQERLEAATQQNQQLRAQLSLMAHPGEGDGLDREEEEDEEEEEEEAVAVPQPMPSIPEDLESREAMVAFFNSAVASAEEEQARLRGQLKEQRVRCRRLAHLLASAQKEPEAAAPAPGTGGDSVCGETHRALQGAMEKLQSRFMELMQEKADLKERVEELEHRCIQLSGETDTIGEYIALYQSQRAVLKERHREKEEYISRLAQDKEEMKVKLLELQELVLRLVGDRNEWHGRFLAAAQNPADEPTSGAPAPQELGAANQQGDLCEVSLAGSVEPAQGEAREGSPRDNPTAQQIMQLLREMQNPRERPGLGSNPCIPFFYRADENDEVKITVI
Protein: Protein GAM-1 (Gallus-anti morte protein) (Gam1) (Q64770)
Organism: Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian adenovirus gal1 (strain Phelps))
Function: Early protein essential for viral replication. Strong and global transcriptional activator of both viral and cellular genes. Activates transcription by blocking host retinoblastoma protein (RB) and inhibiting the SUMO pathway. Inhibition of host RB leads to the activation of E2F1-dependent transcription and, in particular, of E2F1-regulated S-phase genes. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. Blocks the SUMO pathway by targeting the E1 enzyme (SAE1/UBA2 heterodimer) to the ubiquitin-proteasome machinery. Mediates SAE1 degradation possibly through the formation of complexes with either CUL2-elongin BC complex-RBX1 or CUL5-elongin BC complex-RBX1. The degradation of UBA2 is probably a consequent effect of SAE1 disappearance. Inhibits HDAC1 sumoylation, thereby interfering with histone deacetylation mediated by HDAC1, leading to activation of transcription. Mediates induction of heat-shock response. Seems to have an antiapoptotic function.
Subcellular location: Host nucleus {ECO:0000269|PubMed:9060680}.
Interaction partners:
Sequence:
MARNPFRMFPGDLPYYMGTISFTSVVPVDPSQRNPTTSLREMVTTGLIFNPNLTGEQLREYSFSPLVSMGRKAIFADYEGPQRIIHVTIRGRSAEPKTPSEALIMMEKAVRGAFAVPDWVAREYSDPLPHGITHVGDLGFPIGSVHALKMALDTLKIHVPRGVGVPGYEGLCGTTTIKAPRQYRLLTTGVFTKKDLKRTLPEPFFSRFFNQTPEVCAIKTGKNPFSTEIWCMTLGGDSPAPERNEPRNPHSLQDWARLGVMETCLRMSRRGLGSRHHPYHSL