wanglab/gogpt-training-data huggingface dataset:
Protein: MAPKKK cascade protein kinase regulator Ste50 (AFU_orthologue AFUA_2G17130) (Q5AWS8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- mitogen-activated protein kinase kinase kinase
- Membrane anchor Opy2 N-terminal domain-containing protein
- High osmolarity signaling protein sho1
- CD42_CHICK Cell division control protein 42 homolog
- Mitogen-activated protein kinase kinae kinase bck1
Sequence:
MSLHTSYHADSDADDEYERSVITSPHLATDSEGSASESEFPSAEPTPTFAHNEDNSKIPDTIITEWTAEECASFVASLGLRQYCQAFIENGIVGEALIALRHDELKEMGIASVGHRLTILKSVYEMKVKQDIPLDADHYIPLSADQSMNESATQEDIARLIQSIRLRDEKIMTVETELRRVLEDYRRLREELLPVFKMAKDKSQPLPPPTAVSSSDGYYDDRLSGSTLTGQQSGITILDRSGSILSRNLSKRVHGGTTPKNNSPTHIPPSIHENRAYNDGTNLDPSAAAVAASSHLSTMNGKSQLSPNLPSPTSPSNHYGAPQTLASRAYTQPGSARNPHDHYDDNPQSQSRSDRLNTTSSSATRSEIPSRSESRAGGETPSVEIFKSFRVSVDDPCYKVLPAALKKYNINGDWKQYALYIVYGDQERCLGLEERPLILFKQLEKEGRKPMFMLRKQQQAPESTTAYPPSGGSAPNSAGFEPRQAQINLPGGVL
Protein: Endoplasmic reticulum aminopeptidase 1 (EC 3.4.11.-) (ARTS-1) (Adipocyte-derived leucine aminopeptidase) (A-LAP) (Aminopeptidase PILS) (Puromycin-insensitive leucyl-specific aminopeptidase) (PILS-AP) (VEGF-induced aminopeptidase) (Q9EQH2)
Organism: Mus musculus (Mouse)
Function: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Tapasin
Sequence:
MPSLLPLVLTFLSVSSPSWCQNSDIESLKASNGDSFPWNNMRLPEYMTPIHYDLMIHANLSTLTFWGKTEVEIIASRPTSTIIMHSHHLQISKATLRRGAGEMLSEEPLKVLEYPAHEQVALLAAQPLLAGSLYTVIIDYAANLSESFHGFYKSTYRTQEGEMRILAATQFEPTAARMAFPCFDEPALKASFSIKIKRDPRHLAISNMPLVKSVNVAEGLIEDHFDITVKMSTYLVAFIISDFKSVSKMTKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFNIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESSLLYDKEKSSASSKLGITMIVSHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVTVTHPELKVEDYFFGKCFNAMEVDALNSSHPVSTPVENPAQIREMFDDVSYEKGACILNMLRDYLSADTFKRGIVQYLQKYSYKNTKNEDLWNSMMHICPTDGTQTMDGFCSRSQHSSSTSHWRQEVVDVKTMMNTWTLQKGFPLITITVSGRNVHMKQEHYMKGSERFPETGYLWHVPLTFITSKSDSVQRFLLKTKTDVLILPEAVQWIKFNVGMNGYYIVHYADDGWASLSGLLKEAHTTISSNDRASLINNAFQLVSIEKLSIEKALDLTLYLKNETEIMPIFQALNELIPMYKLMEKRDMIEVETQFKDFLLKLLKDLIDKQTWTDEGSVSERMLRSQLLLLACVRNYQPCVQRAERYFREWKSSNGNMSIPIDVTLAVFAVGAQNTEGWDFLYSKYQSSLSSTEKSQIEFSLCTSKDPEKLQWLLDQSFKGEIIKTQEFPHILTLIGRNPVGYPLAWKFLRENWNKLVQKFELGSSSIAHMVMGTTDQFSTRARLEEVKGFFSSLKENGSQLRCVQQTIETIEENIRWMDKNFDKIRLWLQKEKPELL
Protein: Signal transducer and activator of transcription (A0A0D9RIE1)
Organism: Chlorocebus sabaeus (Green monkey) (Simia sabaea)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
- Interferon regulatory factor 9
- Signal transducer and activator of transcription
- Signal transducer and activator of transcription
- Tyrosine-protein kinase
- Tyrosine-protein kinase
- Interferon alpha/beta receptor 1
- Interferon gamma receptor 1
- Interferon alpha/beta receptor 2
- histone acetyltransferase
- Protein inhibitor of activated STAT 1
Sequence:
MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYNCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLNPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPYFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKFLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNAV
Protein: Transcription factor CRF1 (Corepressor with FHL1 protein 1) (Q04930)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor, corepressor with FHL1 of ribosomal protein genes. May be involved in the blocking of the spread of silencing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15620355}. Nucleus {ECO:0000269|PubMed:15620355}. Note=The nuclear location is negatively regulated by the TOR pathway.
Interaction partners:
Sequence:
MLLSAPVNSTVRRKPHSPNKKKPKETGTAASFSSSSSTVVLSSNNDGSFDALWDPSISKASDFESSYISAKRLKPESSNRQKKKNSYKYSREENTNEVEEKTSLGSSSKTEADNIFNDQLTSAGNTTYVSNKRDVNFGANSAVVLLGLPTSKSESHRQYHSPSASTTNEDEEDIGVDILVDNHIDSCETVSINNNRGITHQYPETESDVDFDEAVILTPMDGTDKGVKNPRPLEKKYSSSCFEDRTPLNLDDGHFSECNHFSTLDVSSFFHLNEHVHKIDEVELDGPDRTFSLDNVAINTRKKDIDCLYNSSREDLSNLTCSSEGPRNDSYDSDYNIDEVTYRDDESTDEDESLPTPDRKRKKIGHKACEILDSKRIGIKVPKLYVWSLSDKPFSVIDGLCTKSLYPLSDDINTPESLSSCSSSVSSRENQKGDATFDNDAMIADLLNIGGLEVEKASNGHIELIGE
Protein: FRAS1-related extracellular matrix protein 1 (Protein QBRICK) (Q5H8C1)
Organism: Homo sapiens (Human)
Function: Extracellular matrix protein that plays a role in epidermal differentiation and is required for epidermal adhesion during embryonic development.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q684R7}. Note=Localizes at the basement membrane zone of embryonic epidermis and hair follicles. {ECO:0000250|UniProtKB:Q684R7}.
Interaction partners:
- FRAS1-related extracellular matrix protein 2
- Extracellular matrix organizing protein FRAS1
- Integrin alpha-8
- Nephronectin
- Integrin beta-1
- Glutamate receptor-interacting protein 1
Sequence:
MNSLSWGAANAVLLLLLLAWASPTFISINRGVRVMKGHSAFLSGDDLKFAIPKEKDACKVEVVMNEPITQRVGKLTPQVFDCHFLPNEVKYVHNGCPILDEDTVKLRLYRFTERDTFIETFILWVYLLEPDCNIIHMSNNVLEVPEFNGLSQAIDKNLLRFDYDRMASLECTVSLDTARTRLPAHGQMVLGEPRPEEPRGDQPHSFFPESQLRAKLKCPGGSCTPGLKKIGSLKVSCEEFLLMGLRYQHLDPPSPNIDYISIQLDLTDTRSKIVYKSESAWLPVYIRAGIPNQIPKAAFMAVFILEVDQFILTSLTTSVLDCEEDETPKPLLVFNITKAPLQGYVTHLLDHTRPISSFTWKDLSDMQIAYQPPNSSHSERRHDEVELEVYDFFFERSAPMTVHISIRTADTNAPRVSWNTGLSLLEGQSRAITWEQFQVVDNDDIGAVRLVTVGGLQHGWLTLRGGKGFLFTVADLQAGVVRYHHDDSDSTKDFVVFRIFDGHHSIRHKFPINVLPKDDSPPFLITNVVIELEEGQTILIQGSMLRASDVDASDDYIFFNITKPPQAGEIMKKPGPGLIGYPVHGFLQRDLFNGIIYYRHFGGEIFEDSFQFVLWDSHEPPNLSVPQVATIHITPVDDQLPKEAPGVSRHLVVKETEVAYITKKQLHFIDSESYDRELVYTITTPPFFSFSHRHLDAGKLFMVDSIPKVVKNPTALELRSFTQHAVNYMKVAYMPPMQDIGPHCRDVQFTFSVSNQHGGTLHGICFNITILPVDNQVPEAFTNPLKVTEGGQSIISTEHILISDADTKLDNIDLSLRELPLHGRVELNGFPLNSGGTFSWGDLHTLKVRYQHDGTEVLQDDLLLEVTDGTNSAEFVLHVEVFPVNDEPPVLKADLMPVMNCSEGGEVVITSEYIFATDVDSDNLKLMFVIAREPQHGVVRRAGVTVDQFSQRDVISEAVTYKHTGGEIGLMPCFDTITLVVSDGEAGPFVNGCCYNGPNPSVPLHASFPVYDLNITVYPVDNQPPSIAIGPVFVVDEGCSTALTVNHLSATDPDTAADDLEFVLVSPPQFGYLENILPSVGFEKSNIGISIDSFQWKDMNAFHINYVQSRHLRIEPTADQFTVYVTDGKHHSLEIPFSIIINPTNDEAPDFVVQNITVCEGQMKELDSSIISAVDLDIPQDALLFSITQKPRHGLLIDRGFSKDFSENKQPANPHQKHAPVHSFSMELLKTGMRLTYMHDDSESLADDFTIQLSDGKHKILKTISVEVIPVNDEKPMLSKKAEIAMNMGETRIISSAILSAIDEDSPREKIYYVFERLPQNGQLQLKIGRDWVPLSPGMKCTQEEVDLNLLRYTHTGAMDSQNQDSFTFYLWDGNNRSPALDCQITIKDMEKGDIVILTKPLVVSKGDRGFLTTTTLLAVDGTDKPEELLYVITSPPRYGQIEYVHYPGVPITNFSQMDVVGQTVCYVHKSKVTVSSDRFRFIISNGLRTEHGVFEITLETVDRALPVVTRNKGLRLAQGAVGLLSPDLLQLTDPDTPAENLTFLLVQLPQHGQLYLWGTGLLQHNFTQQDVDSKNVAYRHSGGDSQTDCFTFMATDGTNQGFIVNGRVWEEPVLFTIQVDQLDKTAPRITLLHSPSQVGLLKNGCYGIYITSRVLKASDPDTEDDQIIFKILQGPKHGHLENTTTGEFIHEKFSQKDLNSKTILYIINPSLEVNSDTVEFQIMDPTGNSATPQILELKWSHIEWSQTEYEVCENVGLLPLEIIRRGYSMDSAFVGIKVNQVSAAVGKDFTVIPSKLIQFDPGMSTKMWNIAITYDGLEEDDEVFEVILNSPVNAVLGTKTKAAVKILDSKGGQCHPSYSSNQSKHSTWEKGIWHLLPPGSSSSTTSGSFHLERRPLPSSMQLAVIRGDTLRGFDSTDLSQRKLRTRGNGKTVRPSSVYRNGTDIIYNYHGIVSLKLEDDSFPTHKRKAKVSIISQPQKTIKVAELPQADKVESTTDSHFPRQDQLPSFPKNCTLELKGLFHFEEGIQKLYQCNGIAWKAWSPQTKDVEDKSCPAGWHQHSGYCHILITEQKGTWNAAAQACREQYLGNLVTVFSRQHMRWLWDIGGRKSFWIGLNDQVHAGHWEWIGGEPVAFTNGRRGPSQRSKLGKSCVLVQRQGKWQTKDCRRAKPHNYVCSRKL
Protein: Uncharacterized protein YKR075C (P36155)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized globin-like protein YNL234W
- Hexose transporter HXT8
Sequence:
MTSLDDTIISYQNIMLLDNMTNYNKPAIDYFHHEFNDASLEISASWTLLLKMRKHKLLRLPSCSSEDVLDYNMYLVRLHHCLWRRWSINHYGLQNSKSNPLSINWNKETDVTVLYGPDLTNIDSNENEISPVQNQIDQKQTKNLKSALKKNTECWVTEEVDEINASIESNDNALVKLEDISCPSSVDSHTSSIFDQHSTCTKISSIDEDSEDLMNEKKEQFPRKLKFNQAVMKREIDSKGTIRESLININDIQHSRHHRRHHRRHHHHHHQNSSHSDETIKEAHYEFSNYTFGTMEEDIFYRNQVVF
Protein: FMRFamide-like neuropeptide 21 [Cleaved into: GLGPRPLRF-amide] (Q18234)
Organism: Caenorhabditis elegans
Function: FMRFamide-like neuropeptide. Involved in modulating locomotion quiescence during the sleep-like state called lethargus which occurs during molting between larval and adult stages, acting via the G-protein coupled receptor npr-1. Plays a role in modulating social and feeding behavior.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Neuropeptide receptor npr-1
- FMRFamide-like neuropeptide 18
- G-protein coupled receptors family 1 profile domain-containing protein
- FMRFamide-like neuropeptides 5
- FMRFamide-like neuropeptides 2
- Neuropeptide receptor 3
- G-protein coupled receptors family 1 profile domain-containing protein
- FMRF-Like Peptide
- FMRFamide-like neuropeptides 11
- FMRFamide-like neuropeptides 19
Sequence:
MRLFILLSCLLAWVLAAPYIDQEDALRVLNAYLEQFGPGSDRVYYVAEDDHGSMKRGLGPRPLRFG
Protein: Lac1p (A0A1D8PKA5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Alkaline dihydroceramidase
- 3-ketodihydrosphingosine reductase TSC10
- Sphingolipid delta
- Sphingosine hydroxylase
- Sphinganine kinase
- Sphinganine kinase
- Sphingosine N-acyltransferase
- orotate phosphoribosyltransferase
- serine C-palmitoyltransferase
Sequence:
MSSGSIATTTIPSTPMSIESIEDHQYHNSFLAMVERNQIPLSRNLLIILYLSHLLLQNNNTTITPYTSKFIHIQNCVGIDEFTGKSIYDIDINDTYFVIHSLVIVTFLRSFLMKWCFEPFASKFCHIHSKKAKTRFAEQSWSFVYYSISFIFGVVLYWDSPYYNNLDQVYINWPNHYMSWEFKTYYLVSMGFWLQQIFVLNVEKPRKDHYQMFSHHIITCLLIIGSYYYYYFRIGHLILMIMDSVDIFLAAAKMLKYAGFSNACDAMFLLFLVSWIVLRHGVYNYIFYHAWYKSVDLMKNGQCVEGLMQKRCWTPVVIDTFLGLLGGLQIITCIWMYLILKVAYKVVTGSGAEDVRSDEDDTDIELEEEEKEEEEEEEVGQPIFVEKKEEEVVLEIEEDKYSFERDSFSSSSESTLDEKKDIRKRKV
Protein: G kinase-anchoring protein 1 (cGMP-dependent protein kinase-anchoring protein of 42 kDa) (Q9JMB0)
Organism: Mus musculus (Mouse)
Function: Regulates insulin-dependent IRS1 tyrosine phosphorylation in adipocytes by modulating the availability of IRS1 to IR tyrosine kinase. Its association with IRS1 is required for insulin-induced translocation of SLC2A4 to the cell membrane. Involved in TNF-induced impairment of insulin-dependent IRS1 tyrosine phosphorylation.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:10671526}.
Interaction partners:
Sequence:
MASAVLSSVLTTASRFALLQVDSGSGSDSEPGKGKGRSNGKSQTLGNKATSNEKKREKRRKKKEQQQSEANELRNLAFKKIPQKSSHSICNVQHELSSPNPAQKESREENWQEWRQKDEQLTSEMFEADLEKALLLSKLEYEEHKQDYENAETASTQTKGINKKDKRKNHQGKDKPVTVSLKDFQCEDHISKKAEESNSAQTLSHDGGFFNRLEDDVHKILIREKRREQLTEHNGTDNSPAPEHNQEVGLKDGRIERLKLELERKDAEIQKLKAVITQWEAKYKEVKARNGQLLKMLQEGEMKDKAEILLQVDESQSIKNELTVQVSSLHAALEQERSKVKVLQAELAKYQGGRKGKRNFEPDHCR
Protein: Protein 4.1 (Band 4.1) (Erythrocyte membrane protein band 4.1) (A0A8I6A4E3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTEKSLAAEAENSQHQKEEGEGATNSGQQESQLEEASQAAAAEGSNQGEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLLSSFLKRPKSQVSEEEGREVESEREKGEGEQKETELGTSLDEDVILKAPIAAPEPELKTDPSLDLHSLSSIETQPAQEEHREDPDSETKEGEGIEECSGTEVKEDPESRAEREPETSQKPIRRHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAVWDSTTSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTVQSELGDYDPELHGVDYVSDFKLAPNQTRELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEHYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTLPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAESTDRSPRPTSAPAIAQSQVMEGPGAPAKKAPKEAVKVEEKRGEEPAEPEPEPTEAWKDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQVPTGDGPPLVKTQTVTISDTANAVKSEIPTKDVPIVHTETKTITYEAAQTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEISEE
Protein: Respiratory nitrate reductase 1 beta chain (EC 1.7.5.1) (Nitrate reductase A subunit beta) (Quinol-nitrate oxidoreductase subunit beta) (P11349)
Organism: Escherichia coli (strain K12)
Function: The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.
Subcellular location: Cell membrane; Peripheral membrane protein.
Interaction partners:
- Nitrate reductase molybdenum cofactor assembly chaperone NarJ
- Respiratory nitrate reductase 2 alpha chain
- Respiratory nitrate reductase 1 alpha chain
- Respiratory nitrate reductase 1 gamma chain
- Nitrate/nitrite antiporter NarK
- Respiratory nitrate reductase 2 gamma chain
- Probable nitrate reductase molybdenum cofactor assembly chaperone NarW
- Respiratory nitrate reductase 2 beta chain
- Nitrate/nitrite transporter NarU
- Nitrite reductase large subunit
Sequence:
MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENQEKYKGGWIRKINGKLQPRMGNRAMLLGKIFANPHLPGIDDYYEPFDFDYQNLHTAPEGSKSQPIARPRSLITGERMAKIEKGPNWEDDLGGEFDKLAKDKNFDNIQKAMYSQFENTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADAIERAASTENEKDLYQRQLDVFLDPNDPKVIEQAIKDGIPLSVIEAAQQSPVYKMAMEWKLALPLHPEYRTLPMVWYVPPLSPIQSAADAGELGSNGILPDVESLRIPVQYLANLLTAGDTKPVLRALKRMLAMRHYKRAETVDGKVDTRALEEVGLTEAQAQEMYRYLAIANYEDRFVVPSSHRELAREAFPEKNGCGFTFGDGCHGSDTKFNLFNSRRIDAIDVTSKTEPHP
Protein: Huckebein (RE60512p) (Q9VN10)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein tailless
- Zygotic gap protein knirps
- Protein hunchback
- Segmentation protein fushi tarazu
- Segmentation protein even-skipped
- Protein groucho
- Fork head domain transcription factor slp1
- Homeotic protein bicoid
Sequence:
MSTINLHPPQTYSRLFRPWDTQRQAATSAAPRTVKQEPEAITIKTELASSSFGHDCDGDFSSASSSASSSSNSSKSCYEEALNHSSYTRTSTPLLDAAPHPVFSHPQSSPLDTHAAATASLAPPNQHAPFLSAASDLYYAAAAAAAAAASTPTAVPGFGMDPFTMGLMEQEYARVMAEDAQLKALNSRKQRPKKFKCPNCDVAFSNNGQLKGHIRIHTGERPFKCDVNTCGKTFTRNEELTRHKRIHTGLRPYPCSACGKKFGRRDHLKKHMKTHMPQERQLGPSIFVPMYSYLYGY
Protein: Uncharacterized endoplasmic reticulum membrane protein YMR122W-A (Q3E842)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YDR524C-B
Sequence:
MASSTSTSASASSSIKTNSALVSNNVVAASSVSATSTASSSAAKNTTSSSKNAAPGMVANPVSSKYGIIMAAFAAVSFVLGTGI
Protein: Uncharacterized protein C167.05 (P87132)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- GYF domain-containing protein mpd2
- Uncharacterized protein C18G6.09c
Sequence:
MTSALYSGGGKSAGSLESALDEERLEVLRWMKEREEKKHRQLALQYDPIVRDYCLVKHGDSGYRMDSSLMTSLPHSRNPPIFEAIQGEQPSDIDTLNLKKVKSGPTSPSSIDRLSSPNAKAGDILASSLFSSGSPPDTTRRNSTSNLSSVSTNSDKSRTIGSNYNMLQSTKSTASQRRMSDSSTPSTTKSKEKIFSPKALSSPTQGASSNVTPESPPEKPIPSFVLSPPPVSATNEANKLSDIQTSSPSQDIPAKHLEPLHLNRSLSSSPSSEDSDLSLSSDSDDDEKKQPSKSEKTSSMSVSIKPPKIIRKGSKEQNRIAKEKASGAPLTKSKSHNDTSTEYDSNSLRRSRSNPAFANDDTVHPNTSFVSSNINNWYGSDLEELEQDVKTAKSMKVDIGPTRWIPTANRTIRCIRRGDFQTAASSSKRNCTYFLTLDLSSESLHAAEWAVGILLRNGDTLIIVDVIECDDPSARAVKDRMESEQLETLEKITKYILKLLSKTVLEVEVNIEVIHHEKAKHLIIEMIDYIEPSLVVMGSRGRSHLKGVLLGSFSNYLVNKSSVPVMVARKKLKKNKQRLGNQSRLANNLSDAIVDEVGRTP
Protein: General transcription and DNA repair factor IIH subunit TFB4 (TFIIH subunit TFB4) (RNA polymerase II transcription factor B 34 kDa subunit) (RNA polymerase II transcription factor B p34 subunit) (RNA polymerase II transcription factor B subunit 4) (Q12004)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- General transcription and DNA repair factor IIH helicase subunit XPD/RAD3
- RNA polymerase II transcription factor B subunit 3
- Cyclin CCL1
- General transcription and DNA repair factor IIH subunit TFB2
- General transcription and DNA repair factor IIH subunit SSL1
- General transcription and DNA repair factor IIH subunit TFB5
- Serine/threonine-protein kinase KIN28
- Transcription initiation factor IIE subunit alpha
- Transcription initiation factor IIE subunit beta
- General transcription and DNA repair factor IIH subunit TFB1
Sequence:
MDAISDPTFKHARSRKQVTEESPSLLTVIIEIAPKLWTTFDEEGNEKGSIIKVLEALIVFLNAHLAFNSANKVAVIAAYSQGIKYLYPESTSALKASESENKTRSDLKIINSDMYRRFRNVDETLVEEIYKLFELEKKQIEQNSQRSTLAGAMSAGLTYVNRISKESVTTSLKSRLLVLTCGSGSSKDEIFQYIPIMNCIFSATKMKCPIDVVKIGGSKESTFLQQTTDATNGVYLHVESTEGLIQYLATAMFIDPSLRPIIVKPNHGSVDFRTSCYLTGRVVAVGFICSVCLCVLSIIPPGNKCPACDSQFDEHVIAKLKRKPVVPRLKAKKKVTKP
Protein: Nucleoside triphosphatase NudI (EC 3.6.1.9) (Nucleotide diphosphatase NudI) (Pyrimidine deoxynucleoside triphosphate diphosphatase) (dCTP diphosphatase) (EC 3.6.1.12) (dTTP diphosphatase) (EC 3.6.1.-) (dUTP diphosphatase) (EC 3.6.1.23) (P52006)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP).
Interaction partners:
- Phosphatase NudJ
Sequence:
MRQRTIVCPLIQNDGAYLLCKMADDRGVFPGQWAISGGGVEPGERIEEALRREIREELGEQLLLTEITPWTFSDDIRTKTYADGRKEEIYMIYLIFDCVSANREVKINEEFQDYAWVKPEDLVHYDLNVATRKTLRLKGLL
Protein: Damage-specific DNA-binding protein 2 (A0A087X0X5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAPKKRPETQKTSEIVLRPRNKRSRSPLELEPEAKKLCAKGSGPSRRCDSDCLWVGLAGPQILPPCRSIVRTLHQHKLGRASWPSVQQGLQQSFLHTLDSYRILQKAAPFDRRATSLAWHPTHPSTVAVGSKGGDIMLWNFGIKDKPTFIKGIGAGGSITGLKFNPLNTNQFYASSMEGTTRLQDFKGNILRVFASSDTINIWFCSLDVSASSRMVVTGDNVGNVIL
Protein: Tectonic (dTectonic) (Q9VMH0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable component of the tectonic-like complex (also named MKS complex), a complex localized at the transition zone of primary cilia. Has a role in ciliary structure and function.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27646273}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:27646273}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme (PubMed:27646273). Co-localizes with the tectonic-like complex (PubMed:27646273). {ECO:0000269|PubMed:27646273}.
Interaction partners:
- B9 domain-containing protein 1
- B9 domain-containing protein 2
- Coiled-coil and C2 domain-containing protein 2A
- Tectonic-like complex member Mks1
- Centrosomal protein Cep290
- Transmembrane protein 231
Sequence:
MKEVLPLVVLCLATYHTHSIKIGISHNYNATISPTASTTTEAPATTGAPSSETVSSISTLPEAEVTTTTPAITFPPRVQQKPKVAVASPTMSTALPLNSTEVNSTLSVSGDNTFYYCSCDLQAGRCDLNCCCDNDCPLETRQVFNCLPNSLLPQLESRLEDFQYTHGLPTCQINDGWLCVFRSNTKATKTQPPDMNIDTSQYRKWKDNLEYQESDYAQSRPSAGHYKFGQTLQLWQPETKQLATLELPAAYESPNCQLKQSVWHLQPIRHVCRMKDSAQLQESIWSLLNQTSNYEILSKPRDLEEPEVNGLIVQVCLRGANKSMRCLERGNDTQLDVIVDHVELQLIHNFTNILEAKLFLEEAKLAEDDNEPLWLRYNVEFVTLNESLTKPTSGPLGYLSGAPVILSRMLPQNSSEDKQLISYHSLNQNIKEFHWLSLPSRKPRGSSCQRALDHKEALRFGIDLLTRCELRHAAPLLQAHANHTEYCQGLQAQIWSLLLPHNCTQLEDVTKVFVSHLGRPQPDKWLPMEVRYPENVHEMPPPVQAVYDEMRQSLSCRNIFLSVGYEFHVAHLAMVEGRAPHQRVLQHARLVLGQRHDLEFDTSEIEVALPLSISAMFYRMQTKALSNGAAVGIAGHLVLVEMIYLGIIYLGSMQLCL
Protein: Focal adhesion kinase, isoform F (EC 2.7.10.-) (E1JGM8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNTAGATSQPPPTKNEINSEEYLIHVHMPNKSFKAVRFNVKETVFHVIRRTVEDLGTDGRTPSIQRYACRMLNMITKEVIWLARSTSMQKVLSHILTPGCSNVDCPNNQSELDEVLLEHGRRITDNRVWRVELRVRYVPNNIQELFEEDKATCFYYFNQVKEDFIQANVTAIDTEVAVQLCCLGIRHYFKNITVKAPDKKQHIDYIEKEIGFKSFLPQSVIATSKPKNLKKLIQVGYKKVYNYNDIEYLTRFFDLLKNIYLTNFEQFSVTLSSAWNISGILHVGPHIGISYQTHPQASLKNVAQFKDVVSIKTCTLPKEKLSKSGENTTEPELQNFNCNCQKIKTQIKISASNNVEDLVITCNGINTAESIADLIDGYCRLLSKDLEFTIWHRETNASNEDSAKALPNDATLGSNKSTSSQGKPMLTDDYAEIGLLEGEGDYSTPTVRNYELDRALITPSAKIGVGQFGDVYVGTYTLPKLGKGKNLAGNGKNSNSDQRNADSRPDVIQVAIKTCKANDDPEKTENFLAEAYIMQKFDHPHIIRLIGICSVMPIWIVMELAKLGELRAYLKTNSERLSHGTLLKYCYQLSTALSYLESKKFVHRDIAARNVLVSSPTCVKLADFGLSRWVSDQSYYHSTPTVALPIKWMSPESINFRRFTTASDVWMFGVCIWEILMLGVKPFQGVKNSDVILKLENGERLPLPPNCPPRLYSLMSQCWAYEPLKRPNFKRIKETLHEILIEDSINSSETLKREQRKVASMSWIGSDDIDIPPSKPSRVMHDPDITGLMPETTGLPQTYIIAQNPAVLAKLMMENQKRGINPAAYTTPASGIHNVLGEKLRQQQKDSNSDSEWLIQEELLRSCSIPQGSLNDHQAQMFKLDFMSAGPSSLPDCSNSSSRPMTPNANLSSLKSNHSSADHLSSLTSAEEQMGSNARNLGSAVPSRPPNRADDEVYCATTLVVKSIMALSQGVEKANTEGYLELVKNVGVKLRNLLTSVDKISIIFPAQALKEVQMAHQVLSKDMHELVSAMRLAQQYSDTTLDCEYRKSMLSAAHVLAMDAKNLFDVVDSIRQRYQHLFPPSATKETSCSSSFESTSGSIVAEPVNDLGGYIKTSTSGDLLQNTGIYDNDLHHSFNSQLQLQNPKASIDLSGGGSLQRGMSLGLDTTRSTNEPLRIVEETLGSPGEHMYCNTSALHGHA
Protein: PH domain-containing protein DDB_G0287875 (Q1ZXE2)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MEPPQKKILKVFDQDGLYKTMVIEPSSTTGEICEKFAKKLFLEDSEVVQFSLFIFEGGVRHQLKNTDFPFDYLIKYEKKDYKFFFLNPNGEFISFDKDKQVKKSQSASTSGSAPPKKEPPKPQELQQKQHISKGKSGWLLRKRPGRYDKLYSVSKADKYLRLYENEDTDNDPLYELSLENSIIELKQDLHLQLTLGNSERYIFTHESESEIVSWAQELQATMNYTPGSSSSGSKTNIIKNSSPMGGMLMGGGGGGGGYIPSTKDLGVKLQSKAENTTTLVSTLIQWVNHILEGKGIKVEETEVLSAFSDGIVFINLIEDLFNQTISYRKGKSVYEMQSNIDKCLDVLKTKCGCDYGKILSSDVSECKVAKIIVRILWSMFVGYFCNCEGKEFNMRDKLISWCSTIVLQESSKQIIVESPSSLRNPMVFAVLVNKFAGSTTLDFNALQKIKSKQDQAQQIIEAAFNYLSIPMVVDSSFWNDDQLDEKSFLIYLSFYYIYLSGQEEEKSKFLQSCINPRPSVEPEQTISIRDKQLKLMREKKEEEDRLKKEKEEKEKEEKEKLEKESSAAAAATSSIASTANSNSTEPPKPTTVPLKKTISKLPPRKLPPTVSSPTTTTTTTVPTTVPTTVTTTTTTTSPTTSPTLTPKQPIGTTIKKPATAPLKLKPVAKPLPQPTPSSSTSTTTTPTTTPSSPKPTPVPRTPQLEKEKQDRLEKARLEKEKAEKEEQEFLKQQQEEEEEEQRLLLEQQKQQQEGQERLRKEEEEQQQQRELEEKQRQIDEEEAEEEARIRELEEEARKSKERLEKARLDKLAKAQKEREDKEREEKEKKEKEERERKERKHDENDMDTFKLLEDIVSSSSSPTITPPQSLHSSQIIRTTIEEDDQTNSELEMFQNEYNRLQDEEEHINSFLKLGSSGSNNSNNNNNNNNNKSGASSVTESVTTNKHKSIDILSDNSSVLSSLDDIINSIDKKTSATTSDSFNLSTSSTSLSFLPSSPDLSTNSTFTTNNNNDDETKARSLTSKARKPLPTLTKEQQSIIDKQTGLVSKQSTNNESNEQQQQQQQQQQLQQQQSSQNSTTSISTVNPSNLSINNEEKEKESEPHKPPPKNTQGRVVVRICLEGFGDVLFCSFAIGYDTLCGTVRDMVIKKMKVSSTEEFEYSLHIVRDGLERVLDDDEILLEAEDKIDRFVFKKNDIDRRLLISNHRPVSSK