wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein (Q584P5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSPILRVVRFIRTFNLKESCSSQPYLWYFSICGVFITWANYAQYKRLKPMYPNYDEYRKSEGGRMLEAKRQEFADVIRYNNMVNTMRSDMGARL
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (Q02776)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to direct preproteins in transit and direct them to the channel protein TIM23, and possibly facilitates transfer of the translocating proteins from the TOM complex to the TIM23 complex. Does not act as a structural subunit of the TIM23 complex but plays a dynamic role in protein import. Has no phosphatase activity.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:12437924, ECO:0000269|PubMed:12437925, ECO:0000269|PubMed:14562095}; Single-pass membrane protein {ECO:0000269|PubMed:12437924, ECO:0000269|PubMed:12437925, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM21
- Mitochondrial import inner membrane translocase subunit TIM17
- Mitochondrial import inner membrane translocase subunit TIM23
- Mitochondrial import inner membrane translocase subunit TIM44
- Mitochondrial import inner membrane translocase subunit TIM14
- Mitochondrial import inner membrane translocase subunit TIM16
- Presequence translocated-associated motor subunit PAM17
- Import motor subunit, mitochondrial
- GrpE protein homolog
- Mitochondrial import receptor subunit TOM40
Sequence:
MLSILRNSVRLNSRALRVVPSAANTLTSVQASRRLLTSYSSFLQKETKDDKPKSILTDDMLFKAGVDVDEKGQGKNEETSGEGGEDKNEPSSKSEKSRRKRQTSTDIKREKYANWFYIFSLSALTGTAIYMARDWEPQESEELKKDIDNGYTLSLMYKRFKARFNSMFTYFQEPPFPDLLPPPPPPPYQRPLTLVITLEDFLVHSEWSQKHGWRTAKRPGADYFLGYLSQYYEIVLFSSNYMMYSDKIAEKLDPIHAFVSYNLFKEHCVYKDGVHIKDLSKLNRDLSKVIIIDTDPNSYKLQPENAIPMEPWNGEADDKLVRLIPFLEYLATQQTKDVRPILNSFEDKKNLAEEFDHRVKKLKDKFYGDHKSGGNWAMTALGLGNSLGGSTKFPLDLIHEEGQKNYLMFMKMIEEEKEKIRIQQEQMGGQTFTLKDYVEGNLPSPEEQMKIQLEKQKEVDALFEEEKKKKKIAESK
Protein: Diguanylate phosphodiesterase (A6T8V8)
Organism: Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Interaction partners:
- Aerobic respiration control sensor protein
- Sensory box/GGDEF family protein
- diguanylate cyclase
- diguanylate cyclase
- diguanylate cyclase
- diguanylate cyclase
- diguanylate cyclase
- diguanylate cyclase
- diguanylate cyclase
- diguanylate cyclase
Sequence:
MLTTLIYRSQVHPDRPPVDLDALVHRASSKNLPLGITGILLFNGLQFFQVLEGTEEALESLFSEIQSDPRHRDVVELMRDYSAYRRFHGTGMRILDLRLFETDGALEEILRFSTFGVTEPVNDRMFRLLSAFIADGGRYCLPEPLQPSRWMMMPASGTAAPQHLPGQPCQFALQAIVEPAKKRVSSFEALIRSPTGGSPVEMFAAIAAEDRYRFDLESKAYAFALAGQLPLGKHQLAINLLPGSLYHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRPCLNGIGEICWPVARQAMDL
Protein: DNA polymerase Y family protein (Q6MQS5)
Organism: Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100)
Interaction partners:
- Error-prone DNA polymerase
- RecA protein
- Beta sliding clamp
- DNA polymerase I
- DNA ligase
- LexA repressor
- DNA-3-methyladenine glycosylase II
Sequence:
MVLSPRVQYRFPHYIFVDIGSTQHLMGGEIGCLEKALQIAAKFAPDASAAIADTPAGAQMLAKWRPSHISLRGKEQESFKGLGLDALKDLEGLSPWAQKKPVEHMIAFFHTLGVYGLEGVLNFRLNSLRERWGDFGVLLWNRLHSQDSQVISPLVPRDPLVGYGYLDDPLGSAPLLMNRLKVHLDILFARLQGLARHAQRLDVVLHCEYSDKRYNLSIEPVSPTRDQELFEDLLFKKLEQQVLENPIREFEITLFDVPEKIQQLDFFEPRDNTEDRWRRLISFAKQSQCEMGFLQMEASHFPEQSFRLVTDWPEDFKPQDLVERQDEALQIKSVYAKALASSPRPSLLLEKPQALSAGEVQKLRFVSSLPSERIESAWWQISVQDLKNRDYYFALSHQGQLLWVFKDRINSQVYLHGYFD
Protein: Tripartite motif-containing 24 (A0A8I6AI80)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEVAVEKAAAAAALAGAPAAAAPSGENEAESRQGPDSESGGEVSRLNLLDTCAVCHQNIQSRVPKLLPCLHSFCQRCLPAPQRYLMLTAPSLGSAETPPPAPVPAPAPGSPAGGPSPFATQVGVIRCPVCSQECAERHIIDNFFVKDTTEVPSSTVEKSNQVCTSCEDNAEANGFCVECVEWLCKTCIRAHQRVKFTKDHTVRQKEEVSPEAVGVTSQRPVFCPFHKKEQLKLYCETCDKLTCRDCQLLEHKEHRYQFIEEAFQNQKVIIDTLITKLMEKTKYIKYTGNQIQNRIIEVNQNQKQVEQDIKVAIFTLMVEINKKGKALLHQLESLAKDHRMKLMQQQQEVAGLSKQLEHVMHFSKWAVSSGSSTALLYSKRLITYRLRHLLRARCDASPVTNNTIQFHCDPSFWAQNIINLGSLVIEEKESQPQMPKQNPVVEQSSQPPGGLPSNQLSKFPTQISLAQLRLQHIQQQVMAQRQQVQRRPAPVGSPNPRMQGPIQQPSISLQHPPPRLINFQNHSPKPNGPVLPPYPQQLRYPPSQNIPRQAIKPNPLQMAFLAQQAIKQWQISSGQATPTTASSSSSTPSSPTITSAAGYDGKAFSSPMIDLSAPVGGSYNLPSLPDIDCSSTILLDNIARKDTSVDPGQPRPPSNRTVQSPNSSVPSPGLAGPVTMTSVHPPIRSPSASSVGSRGSSGSSSKPAGADSTHKVPVVMLEPIRIKQENSGPPENYDFPVVIVKQESDEESRPQNTNYPRSILTSLLLNSSQSSASEETVLRSDAPDSTGDQPALHHENSPNGKSEWPDASQKSPVHVGETRKEDDPNEDWCAVCQNGGELLCCEKCPKVFHLTCHVPTLTHFPSGEWICTFCRDLSKPEVEYDCDAPSHNSDKRKSEGLTKLTPIDKRKCERLLLFLYCHEMSLAFQDPVPLTVPDYYKIIKNPMDLSTIKKRLQEDYCMYTKPEDFVADFRLIFQNCAEFNEPDSEVANAGIKLESYFEELLKNLYPEKRFPKLEFRHDVEDCKFSDDSDDDFVQPRKKRLKSMEDRQLLK
Protein: Basic leucine zipper (bZIP) transcription factor atfB (A0A0F0IP79)
Organism: Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
Function: Transcription factor that acts as a key player in the regulatory circuit that integrates secondary metabolism and cellular response to oxidative stress. Regulates the genes involved in development, stress response, and secondary metabolism through direct binding to their promoters. Particularly involved in the resistance to oxidative stress in asexual conidiospores. Binds aflatoxin gene promoters carrying the cAMP-response element (CRE1) under aflatoxin-inducing conditions.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- BZIP transcription factor
- NrfG
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase mpkC
- Basic leucine zipper
- DUF1857-domain-containing protein
- Mitogen-activated protein kinase
Sequence:
MSVDQTLYSRARAAMADPTCAGPATFTAAGAFSQPDLMAFSLPEEEPIWGFDTIAPSMASWQGKMEQQTFCNPNMERGLKNTHVRNGQPTPPPFDDKKLQTPMGEMYPVAQYAFNSSPPEYAPPKHRSSLSEQSQTDGYGVSTRRRKASAVDQSEQQQDREKREKFLERNRLAASKCRQKKKEHTKLLETRFREVSSKKGELESEIEHLRSEVLNLKNEMLRHAQCGDEAIKIHLAQMVRLITSKDTPNRDLVSPMRSPEQMTASTPHGLSFGFDGPMQLPSEMGSPLDQRRDSEQSIMTESSYTFSTDDSFEELINV
Protein: RNA-binding protein 9, isoform J (M9PBZ2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- DNA-directed RNA polymerase II subunit Rpb4
- GEO13361p1
Sequence:
MVEGQTAVQQQQQQPSGAGGASGVGSTTGSAGGPATANNVTNSQAQTNGGTTATTTAAAGAGSTTNAAVGQATANNAASNNNNNNNNTNNNNNNNATANNNNNNEPDPKTNLIVNYLPQTMSQDEIRSLFVSFGEVESCKLIRDKVTGQSLGYGFVNYVKQEDAEKAINALNGLRLQNKTIKVSIARPSSESIKGANLYVSGLPKNMTQSDLESLFSPYGKIITSRILCDNITGLSKGVGFIRFDQRFEADRAIKELNGTTPKNSTEPITVKFANNPSSNKNSMQPLAAYIAPQNTRGGRAFPANAAAGAAAAAAAAAIHPNAGRYSSVISRYSPLTSDLITNGMIQGNTIASSGWCIFVYNLAPDTEENVLWQLFGPFGAVQSVKVIRDLQSNKCKGFGFVTMTNYEEAVLAIQSLNGYTLGNRVLQVSFKTNKNKQTXLLTKLAAVVNANAAAAALAANGLVLHNHHHHSNIGSINNNSNNSNGCSAAAFPLGKYVNHSSNNRQHNINNSTSNTSKQKPASTSNKQQSMAPPKRLASSTAATTGDLAATAATNSSSSSHSASSGDAGATGTAASSSSSSSSTNNNILKTSTKFIYNKPQNQYELLQQQLQLQQEFAQFLTNVANSAATPSSNGSANSTNQRNGGGTIGMGLGMSANSAGGGSGNKNSNGNNGYMPTWSNWFF
Protein: Phosphatidylethanolamine N-methyltransferase (PEAMT) (PEMT) (EC 2.1.1.17) (EC 2.1.1.71) (Phospholipid methyltransferase) (PLMT) (D3YTC7)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03216}. Mitochondrion membrane {ECO:0000256|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03216}. Note=Found in endoplasmic reticulum where most PEMT activity is generated and in mitochondria. {ECO:0000256|HAMAP-Rule:MF_03216}.
Interaction partners:
Sequence:
MKRSGNPGAEADFCVMTRLLGYVDPLDPSFVAAVITITFNPLYWNVVARWEHKTRKLSRAFGSPYLACYSLSVTILLLNFLRSHCFTQAMLSQPRMESLDTPAAYSLGLALLGLGVVLVLSSFFALGFAGTFLGDYFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIISPAPAGAVGSEARQPHGPAPDGAGGPHLHSGSPIRRALHR
Protein: RecBCD enzyme subunit RecC (Exonuclease V subunit RecC) (ExoV subunit RecC) (Helicase/nuclease RecBCD subunit RecC) (P9WIQ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit recognizes the wild-type Chi sequence, and when added to isolated RecB increases its ATP-dependent helicase processivity.
Interaction partners:
- RecBCD enzyme subunit RecB
- RecBCD enzyme subunit RecD
- ATP-dependent DNA helicase RecG
- DNA ligase C
- Uncharacterized protein Rv2311
- DNA ligase B
- DNA polymerase I
Sequence:
MALHLHRAERTDLLADGLGALLADPQPDPFAQELVLVAARGVERWLSQRLSLVLGCGPGRADGVCAGIAFRNPQSLIAEITGTLDDDPWSPEALAWPLLAVIDASLDEPWCRTLASHLGHFATTDAEAELRRGRRYSVARRLAGLFASYARQRPGLLAAWLDGDLGELPGDLAWQPPLWRALVTTVGADPPHVRHDKTIARLRDGPADLPARLSLFGHTRLACTDVQLLDALAVHHDLHLWLPHPSDELWRALAGFQGADGLLPRRQDTSRRAAQHPLLETLGRDVRELQRALPAARATDEFLGATTKPDTLLGWLQADIAGNAPRPAGRSLSDADRSVQVHACHGPARQIDVLREVLLGLLEDDPTLQPRDIVVMCPDIDTYAPLIVAGFGLGEVAGDCHPAHRLRVRLADRALTQTNPLLSVAAELLTIAETRATASQLLNLAQAAPVRAKFGFADDDLDTITTWVRESNIRWGFDPTHRRRYGLDTVVHNTWRFGLDRILTGVAMSEDSQAWLDTALPLDDVGSNRVELAGRLAEFVERLHHVVGGLSGARPLVAWLDALATGIDLLTACNDGWQRAQVQREFADVLARAGSRAAPLLRLPDVRALLDAQLAGRPTRANFRTGTLTVCTMVPMRSVPHRVVCLVGLDDGVFPRLSHPDGDDVLAREPMTGERDIRSEDRQLLLDAIGAATQTLVITYTGADERTGQPRPPAVPLAELLDALDQTTSAPVRERILVTHPLQPFDRKNVTPGALLGAKPFTFDPAALAAAQAAAGKRCPPTAFISGRLPAPPAADVTLADLLDFFKDPVKGFFRALDYTLPWDVDTVEDSIPVQVDALAEWTVGERMLRDMLRGLHPDDAAHSEWRRGTLPPGRLGVRRAKEIRNRARDLAAAALAHRDGHGQAHDVDVDLGDGRRLSGTVTPVFGGRTVSVTYSKLAPKHVLPAWIGLVTLAAQEPGREWSALCIGRSKTRNHIARRLFVPPPDPVAVLRELVLLYDAGRREPLPLPLKTSCAWAQARRDGQDPYPPARECWQTNRFRPGDDDAPAHVRAWGPRAPFEVLLGKPRAGEEVAGEETRLGALAARLWLPLLAAEGSV
Protein: Protein-glutamine deamidase Cif (EC 3.5.1.44) (Cycle-inhibiting factor) (P0DUW5)
Organism: Escherichia coli
Function: Protein-glutamine deamidase effector that inhibits the host cell cycle and other key cellular processes such as the actin network and programmed-cell death. Acts by mediating the side chain deamidation of 'Gln-40' of host NEDD8, converting it to glutamate, thereby abolishing the activity of cullin-RING-based E3 ubiquitin-protein ligase complexes (CRL complexes). Inactivation of CRL complexes prevents ubiquitination and subsequent degradation of the cyclin-dependent kinase inhibitors CDKN1A/p21 and CDKN1B/p27, leading to G1 and G2 cell cycle arrests in host cells. Also able to catalyze deamidation of 'Gln-40' of host ubiquitin in vitro; however, NEDD8 constitutes the preferred substrate in vivo (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:15292151, ECO:0000269|PubMed:19308257, ECO:0000269|PubMed:20688984, ECO:0000305|PubMed:14651638}. Host nucleus {ECO:0000269|PubMed:20941356}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:14651638, ECO:0000269|PubMed:15292151, ECO:0000269|PubMed:19308257, ECO:0000269|PubMed:20688984}.
Interaction partners:
Sequence:
MKDITLPPPTSASCLTGAISVNTEAVLSPMQHTSALHVRDFASLCSQNLKANVLLNSDDHEVPIHQKNPAAIMQNIDSNIKQMATDWGMSIEEVEVIIGREKGIVEPSCGVTANAIMKLFLDKDGFSYCFENEQTLSLEQLQERLSCMPECKSFVLRVNDGALGHAYIVDIPKGENSCRPAFLYQSDLGEGVTRKLRFEDWMTHKALTPILLDDICNYFSCMSQNKTDLEQIATLFDIDGNVKMLRKENIQYQKHDNFSFQLFEYDTDNIEKNIEIIKSLCS
Protein: Growth hormone (Q0QBG8)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MMAAGPRTSLLLAFTLLCLLWTQVVGALPAMSLSRLFANAVLRAQHVHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTSKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDVTPRAGQILKQTYDKFDTNMRSDDALLKNYSLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: GPI ethanolamine phosphate transferase 3, putative (Q8I5R4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MKIKNNIKKKNDNLHHFISNHTLIFSIILLINLLIFFSFINGYFYARQKLEEKSENLELFSRKVFGDEYVESLKKKKNTFSIINAPYDKVVILLIDSLRFDFTLYDTNYEKEFIGKEKNTDIYNNISSEKKNISNDGEKKNSLFFLNNMINVHHILQNEKNNTLLFRFDADAPTITTSRIKSIFMGTIPNYMEVNENFSPTTSVEDNFFEQLHLNNKKVIAIGDNTITHLMKHFSKELVYESFNVFDFYSLDIAAKKHFYEEYESNDWDIMYIHMLGVDHIGHIKTPNSKIMGDALKDFDTFIYDIINKIKLDNLKNISTEEKEKMKIIKKKIYKTYRNGHHIQNENDHIIDNIQNENDHIIDNIQNENDHTIDNIQSENDHTIDNIQNENDHTIEDIQIDNDHTIEDIENQSEQKNDDKKTLFIFFGDHGQLDTGDHGGYSLDETHSALFAYSPLNFISLDNDIIQNNFVLYDKDKLKKNVNTLNEENNNNENIDNYKKYHSYLKDRNKKYSYHYNVKYTKQVNLMSTLSLLIGSTLPYGNIGNIIMDFIPNAYIKNNNKKKNNNNNNNNNNSSLPNEQTNLYYDLLNLHYIAELNYANLWQLNRYLNEYEKKYNIIKNEDYHFIKSSWHIIQKDKKELFFQPNKKFIKNDILLKKEKESYIEFINEMTTLMDITQKYFYYIFNIKEKYFLILSIVLNIFLLLFLKHFYYYSKLNYYHKLIKGSKILLCMSLFLNIIVTFNDFNKNIYLLLCICALLLYFFIFCLSIKEYKDIFRIFSHAKIIFISNNIDMIIPSIKNYHMSAKRNMNITNNDTYHTSHKDRKSFTNKEEKQNNTLMNIFYNIIYFLRIIRKKIVQYIIFIHLTIYNLTIGNIIFILFKLFPKIITNSFQILRSNYFLLFVIIWSCCEMSFNYIDKERYYIHYILIVYVIFGMLKWKYHRVFNILKAFILLVLLIINALYSHTPEYFDHGKEKIYLKESVLKSVFPISSYILSLILINSGINNLLKKRIKIIITQIWTLQYILVFLFLNNIYHRYIQFITPPSIYFLTISTFIFILLSKNILNEKEKLQDSLDKIYEVCITLFLIIITSIPLSFIIYSNTNLGVLFLFYMTFLFFYFILISSNCSENMIQMNDITSTWINENIHNRNDPIITKGNLENKEKCTSCNTSIKEKFYYKLMIEKFKLLNTCSVLNEEEIMGIQIYKLIRDISYFYINETDFYILSCVLLIYSFFITGHKFILNNLPLVSGYVGLYKYVWPISQFYIFNHIFFPFFFSLFFIIYIYNIRRIKIINSFKQFDLYYFYVYPLMNFSFKASFLFCCKFIISVWVSYYLNLHIMLYDYFLPKMFYLFAIHLIFIIFCLLVFLMTKHIFLR
Protein: Epididymis secretory sperm binding protein (A0A384P5S9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDPSGVKVLETAEDIQERRQQVLDRYHRFKELSTLRRQKLEDSYRFQFFQRDAEELEKWIQEKLQIASDENYKDPTNLQGKLQKHQAFEAEVQANSGAIVKLDETGNLMISEGHFASETIRTRLMELHRQWELLLEKMREKGIKLLQAQKLVQYLRECEDVMDWINDKEAIVTSEELGQDLEHVEVLQKKFEEFQTDMAAHEERVNEVNQFAAKLIQEQHPEEELIKTKQDEVNAAWQRLKGLALQRQGKLFGAAEVQRFNRDVDETISWIKEKEQLMASDDFGRDLASVQALLRKHEGLERDLAALEDKVKALCAEADRLQQSHPLSATQIQVKREELITNWEQIRTLAAERHARLNDSYRLQRFLADFRDLTSWVTEMKALINADELASDVAGAEALLDRHQEHKGEIDAHEDSFKSADESGQALLAAGHYASDEVREKLTVLSEERAALLELWELRRQQYEQCMDLQLFYRDTEQVDNWMSKQEAFLLNEDLGDSLDSVEALLKKHEDFEKSLSAQEEKITALDEFATKLIQNNHYAMEDVATRRDALLSRRNALHERAMRRRAQLADSFHLQQFFRDSDELKSWVNEKMKTATDEAYKDPSNLQGKVQKHQAFEAELSANQSRIDALEKAGQKLIDVNHYAKDEVAARMNEVISLWKKLLEATELKGIKLREANQQQQFNRNVEDIELWLYEVEGHLASDDYGKDLTNVQNLQKKHALLEADVAAHQDRIDGITIQARQFQDAGHFDAENIKKKQEALVARYEALKEPMVARKQKLADSLRLQQLFRDVEDEETWIREKEPIAASTNRGKDLIGVQNLLKKHQALQAEIAGHEPRIKAVTQKGNAMVEEGHFAAEDVKAKLHELNQKWEALKAKASQRRQDLEDSLQAQQYFADANEAESWMREKEPIVGSTDYGKDEDSAEALLKKHEALMSDLSAYGSSIQALREQAQSCRQQVAPTDDETGKELVLALYDYQEKSPREVTMKKGDILTLLNSTNKDWWKVEVNDRQGFVPAAYVKKLDPAQSASRENLLEEQGSIALRQEQIDNQYHSLLELGEKRKGMLEKSCKKFMLFREANELQQWINEKEAALTSEEVGADLEQVEVLQKKFDDFQKDLKANESRLKDINKVAEDLESEGLMAEEVQAVQQQEVYGMMPRDETDSKTASPWKSARLMVHTVATFNSIKELNERWRSLQQLAEERSQLLGSAHEVQRFHRDADETKEWIEEKNQALNTDNYGHDLASVQALQRKHEGFERDLAALGDKVNSLGETAERLIQSHPESAEDLQEKCTELNQAWSSLGKRADQRKAKLGDSHDLQRFLSDFRDLMSWINGIRGLVSSDELAKDVTGAEALLERHQEHRTEIDARAGTFQAFEQFGQQLLAHGHYASPEIKQKLDILDQERADLEKAWVQRRMMLDQCLELQLFHRDCEQAENWMAAREAFLNTEDKGDSLDSVEALIKKHEDFDKAINVQEEKIAALQAFADQLIAAGHYAKGDISSRRNEVLDRWRRLKAQMIEKRSKLGESQTLQQFSRDVDEIEAWISEKLQTASDESYKDPTNIQSKHQKHQAFEAELHANADRIRGVIDMGNSLIERGACAGSEDAVKARLAALADQWQFLVQKSAEKSQKLKEANKQQNFNTGIKDFDFWLSEVEALLASEDYGKDLASVNNLLKKHQLLEADISAHEDRLKDLNSQADSLMTSSAFDTSQVKDKRDTINGRFQKIKSMAASRRAKLNESHRLHQFFRDMDDEESWIKEKKLLVGSEDYGRDLTGVQNLRKKHKRLEAELAAHEPAIQGVLDTGKKLSDDNTIGKEEIQQRLAQFVEHWKELKQLAAARGQRLEESLEYQQFVANVEEEEAWINEKMTLVASEDYGDTLAAIQGLLKKHEAFETDFTVHKDRVNDVCTNGQDLIKKNNHHEENISSKMKGLNGKVSDLEKAAAQRKAKLDENSAFLQFNWKADVVESWIGEKENSLKTDDYGRDLSSVQTLLTKQETFDAGLQAFQQEGIANITALKDQLLAAKHVQSKAIEARHASLMKRWSQLLANSAARKKKLLEAQSHFRKVEDLFLTFAKKASAFNSWFENAEEDLTDPVRCNSLEEIKALREAHDAFRSSLSSAQADFNQLAELDRQIKSFRVASNPYTWFTMEALEETWRNLQKIIKERELELQKEQRRQEENDKLRQEFAQHANAFHQWIQETRTYLLDGSCMVEESGTLESQLEATKRKHQEIRAMRSQLKKIEDLGAAMEEALILDNKYTEHSTVGLAQQWDQLDQLGMRMQHNLEQQIQARNTTGVTEEALKEFSMMFKHFDKDKSGRLNHQEFKSCLRSLGYDLPMVEEGEPDPEFEAILDTVDPNRDGHVSLQEYMAFMISRETENVKSSEEIESAFRALSSEGKPYVTKEELYQNLTREQADYCVSHMKPYVDGKGRELPTAFDYVEFTRSLFVN
Protein: Cytochrome b-c1 complex subunit 7 (Q4VBV1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 8
- NADH dehydrogenase iron-sulfur protein 4
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Ubiquinol-cytochrome c reductase core protein 2a
- Ubiquinol-cytochrome c reductase core protein 1.
- Cytochrome b-c1 complex subunit 6
- Complex III subunit 9
Sequence:
MAARAPVAASGRFVDVFRKWYYNACGFNKLGLMRDDTIDEGSDVKEAVRRLPEPLYNERVFRLKRAMDLSMKHQILPKDQWTKFEQDVKYLEPYLQEVIRERKEKEEWDKK
Protein: Testis-specific Y-encoded-like protein 2 (TSPY-like protein 2) (Cell division autoantigen 1) (Cutaneous T-cell lymphoma-associated antigen se20-4) (CTCL-associated antigen se20-4) (Differentially-expressed nucleolar TGF-beta1 target protein) (Nuclear protein of 79 kDa) (NP79) (Q9H2G4)
Organism: Homo sapiens (Human)
Function: Part of the CASK/TBR1/TSPYL2 transcriptional complex which modulates gene expression in response to neuronal synaptic activity, probably by facilitating nucleosome assembly. May inhibit cell proliferation by inducing p53-dependent CDKN1A expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:11318608, ECO:0000269|PubMed:11395479}. Cytoplasm {ECO:0000250}. Note=Enriched in transcriptionally active regions of chromatin in neurons. {ECO:0000250}.
Interaction partners:
- Testis-specific Y-encoded-like protein 1
- MYND-type zinc finger-containing chromatin reader ZMYND8
- Zinc finger protein 687
- T-box brain protein 1
- X-box-binding protein 1
- Cyclin-dependent kinase 1
- Lysine-specific demethylase 5C
Sequence:
MDRPDEGPPAKTRRLSSSESPQRDPPPPPPPPPLLRLPLPPPQQRPRLQEETEAAQVLADMRGVGLGPALPPPPPYVILEEGGIRAYFTLGAECPGWDSTIESGYGEAPPPTESLEALPTPEASGGSLEIDFQVVQSSSFGGEGALETCSAVGWAPQRLVDPKSKEEAIIIVEDEDEDERESMRSSRRRRRRRRRKQRKVKRESRERNAERMESILQALEDIQLDLEAVNIKAGKAFLRLKRKFIQMRRPFLERRDLIIQHIPGFWVKAFLNHPRISILINRRDEDIFRYLTNLQVQDLRHISMGYKMKLYFQTNPYFTNMVIVKEFQRNRSGRLVSHSTPIRWHRGQEPQARRHGNQDASHSFFSWFSNHSLPEADRIAEIIKNDLWVNPLRYYLRERGSRIKRKKQEMKKRKTRGRCEVVIMEDAPDYYAVEDIFSEISDIDETIHDIKISDFMETTDYFETTDNEITDINENICDSENPDHNEVPNNETTDNNESADDHETTDNNESADDNNENPEDNNKNTDDNEENPNNNENTYGNNFFKGGFWGSHGNNQDSSDSDNEADEASDDEDNDGNEGDNEGSDDDGNEGDNEGSDDDDRDIEYYEKVIEDFDKDQADYEDVIEIISDESVEEEGIEEGIQQDEDIYEEGNYEEEGSEDVWEEGEDSDDSDLEDVLQVPNGWANPGKRGKTG
Protein: GATA transcription factor 9 (O82632)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. May be involved in the regulation of some light-responsive genes (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Auxin response factor 30
- C2H2-like zinc finger protein
Sequence:
MEKIAPELFLVAGNPDSFVVDDLLDFSNDDGEVDDGLNTLPDSSTLSTGTLTDSSNSSSLFTDGTGFSDLYIPNDDIAELEWLSNFVEESFAGEDQDKLHLFSGLKNPQTTGSTLTHLIKPEPELDHQFIDIDESNVAVPAKARSKRSRSAASTWASRLLSLADSDETNPKKKQRRVKEQDFAGDMDVDCGESGGGRRCLHCATEKTPQWRTGPMGPKTLCNACGVRYKSGRLVPEYRPASSPTFVMARHSNSHRKVMELRRQKEMRDEHLLSQLRCENLLMDIRSNGEDFLMHNNTNHVAPDFRHLI
Protein: Interferon-induced 35 kDa protein (IFP 35) (Ifi-35) (P80217)
Organism: Homo sapiens (Human)
Function: Acts as a signaling pathway regulator involved in innate immune system response. In response to interferon IFN-alpha, associates in a complex with signaling pathway regulator NMI to regulate immune response; the complex formation prevents proteasome-mediated degradation of IFI35 and correlates with IFI35 dephosphorylation. In complex with NMI, inhibits virus-triggered type I interferon/IFN-beta production. In complex with NMI, negatively regulates nuclear factor NF-kappa-B signaling by inhibiting the nuclear translocation, activation and transcription of the NF-kappa-B subunit p65/RELA, resulting in the inhibition of endothelial cell proliferation, migration and re-endothelialization of injured arteries. Beside its role as an intracellular signaling pathway regulator, also functions extracellularly as damage-associated molecular patterns (DAMPs) to promote inflammation when actively released by macrophage to the extracellular space during cell injury and pathogen invasion. Macrophage-secreted IFI35 activates NF-kappa-B signaling in adjacent macrophages through Toll-like receptor 4/TLR4 activation, thereby inducing NF-kappa-B translocation from the cytoplasm into the nucleus which promotes the release of pro-inflammatory cytokines.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10779520, ECO:0000269|PubMed:10950963, ECO:0000269|PubMed:8288566}. Nucleus {ECO:0000269|PubMed:10950963, ECO:0000269|PubMed:26342464, ECO:0000269|PubMed:8288566}. Secreted {ECO:0000269|PubMed:29038465}. Note=Cytoplasmic IFI35 localizes in punctate granular structures (PubMed:10950963). Nuclear localization increased is stimulated by IFN-alpha (PubMed:10950963, PubMed:8288566). Extracelullar following secretion by macrophage (PubMed:29038465). {ECO:0000269|PubMed:10950963, ECO:0000269|PubMed:29038465, ECO:0000269|PubMed:8288566}.
Interaction partners:
- Ubiquitin-like protein FUBI
- N-myc-interactor
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL36
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL33
Sequence:
MSAPLDAALHALQEEQARLKMRLWDLQQLRKELGDSPKDKVPFSVPKIPLVFRGHTQQDPEVPKSLVSNLRIHCPLLAGSALITFDDPKVAEQVLQQKEHTINMEECRLRVQVQPLELPMVTTIQMSSQLSGRRVLVTGFPASLRLSEEELLDKLEIFFGKTRNGGGDVDVRELLPGSVMLGFARDGVAQRLCQIGQFTVPLGGQQVPLRVSPYVNGEIQKAEIRSQPVPRSVLVLNIPDILDGPELHDVLEIHFQKPTRGGGEVEALTVVPQGQQGLAVFTSESG
Protein: Pre-mRNA-splicing factor CWC25 homolog (Coiled-coil domain-containing protein 49) (Spliceosome-associated protein homolog CWC25) (Q9NXE8)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as component of the spliceosome.
Subcellular location: Nucleus {ECO:0000269|PubMed:29301961}.
Interaction partners:
- Splicing factor YJU2
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Cell division cycle 5-like protein
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-processing factor 19
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor CWC22 homolog
- Protein BUD31 homolog
- Pre-mRNA-splicing factor ISY1 homolog
Sequence:
MGGGDLNLKKSWHPQTLRNVEKVWKAEQKHEAERKKIEELQRELREERAREEMQRYAEDVGAVKKKEEKLDWMYQGPGGMVNRDEYLLGRPIDKYVFEKMEEKEAGCSSETGLLPGSIFAPSGANSLLDMASKIREDPLFIIRKKEEEKKREVLNNPVKMKKIKELLQMSLEKKEKKKKKEKKKKHKKHKHRSSSSDRSSSEDEHSAGRSQKKMANSSPVLSKVPGYGLQVRNSDRNQGLQGPLTAEQKRGHGMKNHSRSRSSSHSPPRHASKKSTREAGSRDRRSRSLGRRSRSPRPSKLHNSKVNRRETGQTRSPSPKKEVYQRRHAPGYTRKLSAEELERKRQEMMENAKWREEERLNILKRHAKDEEREQRLEKLDSRDGKFIHRMKLESASTSSLEDRVKRNIYSLQRTSVALEKNFMKR