wanglab/gogpt-training-data huggingface dataset:
Protein: Calpain small subunit 1 (CSS1) (Calcium-activated neutral proteinase small subunit) (CANP small subunit) (Calcium-dependent protease small subunit) (CDPS) (Calcium-dependent protease small subunit 1) (Calpain regulatory subunit) (P04632)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Essential for embryonic development (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon calcium binding. {ECO:0000250}.
Interaction partners:
- Calpain-1 catalytic subunit
- Calpain-2 catalytic subunit
- Calpastatin
- Calpain-6
- Calpain-5
- Calpain small subunit 2
- Calpain-7
- Calpain-10
- Calpain-15
- Cytochrome b-c1 complex subunit 1, mitochondrial
Sequence:
MFLVNSFLKGGGGGGGGGGGLGGGLGNVLGGLISGAGGGGGGGGGGGGGGGGGGGGTAMRILGGVISAISEAAAQYNPEPPPPRTHYSNIEANESEEVRQFRRLFAQLAGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKRWQAIYKQFDTDRSGTICSSELPGAFEAAGFHLNEHLYNMIIRRYSDESGNMDFDNFISCLVRLDAMFRAFKSLDKDGTGQIQVNIQEWLQLTMYS
Protein: Pericardin (Q9VTR6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Viking, isoform A
- Collagen alpha-1
- Laminin subunit alpha
- Lonely heart, isoform A
Sequence:
MLPFRLGLLLGAVLFVASANGAAIENEVSSLNDLQREKRSGRGYSRGQTQSQYLNFGKPEEDGKAEAEATENGSRSTVSGTHGMGQAQSQFSSGDCNGCSGYQTDYPSSGRILDASGSGGIGRPDSIISLPGGVGGQTGAGQAGYGSQLGVGAQAGAGQPGYGDQPGVGTQPGVGQPGYGSQPGIGGQTGAGQPGYGSQPGIGGQTGAGQPGYGSQPVVGAQTGTGQPGYGAQPGVGTQTGAGQPGYGSQPGIGGQTGARQPGYVTQPGVGAQTGIGQPGYGAQPGILGQTGAGQPGYGSQPGIGGQTGAGQPGYGTQPGVGAQTGTGQPGYGAQPGVGTQTGAGQPGYGSQPGIGGQTGAGQPGYGTQPGVGAQTGAGQPGYGAQPGVGAQTGAGQPGYGSQPGIGGQTGAGQPGYGSQPGIGGQTGARQPGYGSQPGVGAQTGAGQPGYGAQPGVGAQTGAGQPGYGSQPGIGGQTGAGQPGYGSQPGVGAQTGAGQPGYGAQPGVGAQTGAGQPGYGSQPGIGGQTGAGQPGYGTQPGVGAQTGTGQPGYGAQPGVGTQTGAGQPGYGSQPGIGGQTGAGQPGYGTQPGVGAQTGTGQPGYGAQPGVGTQTGAGQPGYGSQPGYGTQPGVGAQTGTGQPGYGAQPGVGGQTGAGQPGYGTQPGIGGQTGAGQPGYGSQPGIGGQTGGGQPGYGSQIGGQTGAGQPSYGSQPGVGAQNGAGQPGYGTQPVIGGQTGAGQPGYGGQTGVGGSPGFLTQPGIGGISGPIGGKLGGGQSEAAKPGYWAQPGIGGPSRYGSQPGIGDQTGTGQSGYGGQPGISGQTGGGQPGYGGQATISGLPGYGTQPGIGALTAVPGGHYGYETQPGIGGQTGTNQPGFGGQPGIGGQTGAGQPGYGFIGQPGIGGQTGTSGRQPGYGTQPGIGGQTAAGQPGYGSQTGVGGQIGAGQPGYGSQPGIGGQTGAGQPGYGAQPGFGGQPGYGNQPGVGGQTGAGQPGYGSQPGIGGQTGAGQPGYGAQPGFGGQLGYGNQPGVGGQTGAGQPGYGSQPGVGGQTGAGQPGYGVIPGFGGQPGIGGQTAAGKPGYGGQPGIGGSPVYGTQQGTGGQSGISGGQPGYGTQPGQTGAGQPGYGSLPGTGGQATAGQPGYGPGSQPGIGGQTVGGHGGYGSQPGIGGAPVYGTQPGGGGQTGVIGGQPGQIGDRVGQPGYGTQTGQIGAPGRYTDGSQTVPGAVGTGGVVAAGTSGADDAFSQAESSIGDGQASASAQGKKNGGTAKTQVSGTYSSGGTFSASAMTSDADRAASAQVTGNADGAVSQSQGSGGPAQSQAQVQVAKDGGTKASSQSGGIIQQSQSEVHANDKGGLADAQSSGPGQTSSQAQIGFRPGQEANPIAANGGGQASSSSGTHSSQSSSQIHGTSSFGVSYHGAAQSASGTKEQVATYREANRELFNTISQFGNNANAVTDRADAVYSGPALTDESDRVPEAQLKSTKPKEEAEQVVSKLDHPEPVQYDDEDEADPDEYDEDEYYEEKPVKLEESPKSSTIVAPTEATPRPKTYNQSSPTQSQQTVVVPVPGEKYQVVQKQNGKATINAEPSTTEAIPPGFRGTVNVEKKFHTKALELHAPKGVEITPDTSDEGPVRGDKPLRRAPDSYVTVTKSVTGSMDNTKNPPQENKNFQSTYYTKSSTCGYFTFSCNIVYGANGRSKICRPKAPTNGKC
Protein: 21S rRNA pseudouridine(2819) synthase (EC 5.4.99.43) (Pseudouridine synthase 5) (Pseudouridylate synthase PUS5) (Uracil hydrolyase PUS5) (Q06244)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Pseudouridylate synthase responsible for the pseudouridine-2819 formation in mitochondrial 21S rRNA. May modulate the efficiency or the fidelity of the mitochondrial translation machinery.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10756195}.
Interaction partners:
- Multisubstrate pseudouridine synthase 7
- tRNA pseudouridine
- tRNA pseudouridine
- tRNA pseudouridine
- tRNA pseudouridine
- tRNA pseudouridine synthase 4
- Bifunctional protein RIB2
- tRNA pseudouridine synthase 1
- tRNA modification GTPase MSS1
- H/ACA ribonucleoprotein complex subunit CBF5
Sequence:
MSLKKQIPIIFENTHYFIVNKPPGIPSQPPDCRTWGRTHPNLDPTPLLERFKAIYYSHREVELCRTVHRLDHCVTGGMLIAKTKDGSVKFSRFLQKGGNNGYKLQRKYVAIVESSGRFNKPNNYEIKYGPKYNFLISHGGREITKFKEVDENCIVLQLVTGKKHQIRNHVSQILNQPILNDKRHGSTVNFPELFNDQIALHSACIITKIGLQTKTHLIPMEHNNTGQLWSRKYVNEEGEFTLPIKEVLLENWDQ
Protein: RNA polymerase I termination factor (NTS1 silencing protein 1) (Q12457)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-binding protein that recognizes sequence-specific replication termini (Ter sites) within rDNA. Binds to rDNA terminator elements and mediates efficient RNA polymerase I transcription termination. Required for rDNA silencing at the non-transcribed spacer 1 (NTS1). Promotes the association of SIR2 with NTS1 and contributes to maintenance of rDNA stability.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22362748}.
Interaction partners:
- DNA replication fork-blocking protein FOB1
Sequence:
MDSVSNLKSTNFQNNNDPKESVEEAVLRYVGVDLKNHIKKTKKKLKKQKKRKHGSKMSHEDEDTDMDWYLKTSGSKDLRKVDDIEPNSVAVAAVAAAYNSSMREKDKRSCHKKSSNSRSERKKHRKRKSSKERKAKIKMVLDPQLTTLDDGITTTAFLPDDLIAETAFDKYVDTEKAYLAKHPSKSLEVNEDDKENNFNNNSSTLVRIYTDLEGIPNDGSYIKRTPKIPEKDVKSDDLILAPEENNGDTALLRSDIVKASVIDGAITKSIGKKFTPSEENALDQFIEEYMKIRGLDRRQMCERIWSTDGVIRDGFWANISKVLPYRTRSSIYKHIRRKYHIFEQRGKWTPEEDQELARLCLEKEGHWTEVGKLLGRMPEDCRDRWRNYMKCGSKRGSKRWSKEEEELLTTVVNEMIEEAHQYQRMKALEAANKNDRYNQMYSRGPKGKRISDNPTFKDMINWTVVSERMSGTRSRIQCRYKWNKLVTDEAARSMLSIPVSERKWLLERLKQLPKTSYSNIDWNSIATYKPGYPRTGLELRLCYEQMREKIHDFKGRSTAEIIDSLLEQIN
Protein: LD24460p (Q95TT8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSIFKARVKEFEDVLAGPQDLIDLKQLRKLAFNGVPDVQSFRALSWKLLLGYLGPRRSSWTTTLAQKRALYKQFIEELVLPPGHSSNRASVDGGDGDKVDSGGVGLQDHPLSEGPESAWNTFFNDNEFLLQIDKDVRRLCPDISFFQQPTDYPCEIVVHSKGEHGRRLHERVVPAVLSSANVERKGLGMTKINLITKRSVENYAAMEEGQEAHWEVVQRILFIYAKLNPGQGYVQGMNEIVGPIYYVMASDPDLTYRAHAEADCFFCFTALMSEIRDFFIKTLDDAEGGIKFMMARLSNMLKSKDLSIYELLRSQELHPQYYSFRWLTLLLSQEFPLPDVLRIWDSVFADEQRFDFLIKICCSMILIQKEAILENDFASNVKLLQNYPPIDINVVIAHAGSLA
Protein: Kazal-like domain-containing protein (Q8BM23)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKTATVPMLLTLAFYLTQDAAGEKGNQDPCMKFQAQMKNGTLTCPKGNNSSQSLNDIIFQSECILCKRALEQGAPTKIMNVKVLSRANRATDPAKLNCESFKQRRKDGDFICPSDTSSVCGTDGKTYRSRCELCAENAKSQNHVDVKSEGECGSSHLETDMCSDFRAYVQDGRLGCTRESDPILGPDGRTHGNRCAMCAELFLKEAKENATRNRESRIRRDAEKELCKEFENQVRNGRLFCTRESDPIRGPDGKMHGNKCALCAEIFMRQFTEEKGKAEKNQKDAEERAKAKMEIQKRCSEFQDRARNGTLFCTRENDPIRGLDGKTHGNLCSMCQAFFKTEAEEKKAEAGSRNRRGSEESETYAKLCDEYRKARKNGQLYCTRENAPIRGPDGKIHGNTCSMCQAFFIQEDKARAKVKREAAKEMCSEFRNQARNGMLMCTRENDPVVGPDGKRHSNKCAMCASVFLLEEEEKKKDDKTEKVDAGKAKKEAVQELCRKYHTQLRNGPLRCTRRNNPIEGLDGKMYKNACFMCWAFFQQEAKKSGAGFRPKVKREVKVDCSEYLALSKRGEIFCTRENDPVRGPDGKTHGNKCAMCKAVFKKENEERKRKEGENQRITSGESSSGGNPKAKDECAQYRESMKHGQLSCTRESDPVRGVDGEHYNNKCVMCKELLQKEMEETNKNSASRSNGTGSATGKDVCDQFRSQM
Protein: Uncharacterized protein C1B3.20 (Q9Y7I1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MSSNSNTDHSTGDNRSKSEKQTDLRNALRETESHGMPPLRGPAGFPVNPRPFSHGGNANLDRLNLKEPVDLEGPKDEQ
Protein: Conserved oligomeric Golgi complex subunit 5 (Q381A1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 6
- COG4 transport protein middle alpha-helical bundle domain-containing protein
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 7
Sequence:
MFTDSILMSPDFDEEGYLRYAIHASSCKTEQSRLTSCSAAVREEMHNILTENVEDMLRQVTAASCAQRDAAAVRQAAATLMHSASRLRHTIYEPYHLIKGSITKLRNTNVTLNTLRSVIRFINLTTRLKGLLPDDIARAARTMREVEELLQAANIAAIDVVRSRMDVVERSATVIRSRAQDMLRRADSRDASNVTTALQCFVALGSASRVISGFMTEQKREVMKTLMRELDIQVIANEINDECTATTSDFDYVGSRTCEVLASHLQAALRATATHTGSVIALWRVLVKKADPVTQIPYLSAVDNPTSVLGDYWHFVTDKLRERLQAIQKRPNFFYAMAGDILRYRSLLVTFLDDVVELLELLDQLMGLDASSNGRPNTSGGGGAGACLPSGVEQLRCMWLSHVTREVNERFGAQIMDRHRERLHGVISRLNSIIPSGGNKPLPNLSVDLQRPQVPAIAHVLDVRSYATLAMRDVMEYQRDPQTLSTVLACTLQCLAGFMQRVTETSMRWPLPPLPSVSSDVNTLQMLHICISNACTQLSMDFAVMLASLPEGEEDEDRGEFVGGRDDMWQSSGGGCDGAGGACCDESAVSTRKLVAERQRKLLEVTINLKKISEKVVRPFFRSVSVLLLDSVSMCVDGACGQEAAGISQLQSQTVHFMSHYYYLFDPQTPTLVDSVRRITDSLIVRLMVAVTLVYPFTKEVREHLTVCLHQVPRVAISFGPSTQGAMGRSTMVLKGQLHQLAMWYNASEEALETPEGVSRAALATLPLVVSRLLLLQRVFRPSAAVGGPSAVMGVTPECFIETIEAAVLDQLCVGNVPEGDLAKRVADNSHAAERLGQVMDAVERCFLMAIEALSGDAAQEATVRWVKQLWVLLDHRQVGK
Protein: Nucleoprotein (Nucleocapsid protein) (NC) (Protein N) (P10527)
Organism: Bovine coronavirus (strain Mebus) (BCoV) (BCV)
Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04096}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04096}. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. {ECO:0000255|HAMAP-Rule:MF_04096}.
Interaction partners:
Sequence:
MSFTPGKQSSSRASFGNRSGNGILKWADQSDQSRNVQTRGRRAQPKQTATSQLPSGGNVVPYYSWFSGITQFQKGKEFEFAEGQGVPIAPGVPATEAKGYWYRHNRRSFKTADGNQRQLLPRWYFYYLGTGPHAKDQYGTDIDGVFWVASNQADVNTPADILDRDPSSDEAIPTRFPPGTVLPQGYYIEGSGRSAPNSRSTSRASSRASSAGSRSRANSGNRTPTSGVTPDMADQIASLVLAKLGKDATKPQQVTKQTAKEIRQKILNKPRQKRSPNKQCTVQQCFGKRGPNQNFGGGEMLKLGTSDPQFPILAELAPTAGAFFFGSRLELAKVQNLSGNLDEPQKDVYELRYNGAIRFDSTLSGFETIMKVLNENLNAYQQQDGMMNMSPKPQRQRGQKNGQGENDNISVAAPKSRVQQNKSRELTAEDISLLKKMDEPYTEDTSEI
Protein: LD28220p (Uncharacterized protein, isoform B) (Q8IMP2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTDDLLVRRERSEDSQSSSVSIPVTPTTGGAAPAPSAPTSSLDRLRNTFRRTESISSQIFSHISTQFSNAAAAAASSEVIDGTTTYPYPDEPAPPVVPVAPDTVASASASSPSPSKLKAKRLKRARDTAEIERSNLVNICKLVVKELLEQSLRYGRMLDSDHLPLQHFFIVIEHVLGHGLRPKKGLLGPRKELWDLLQSVEHYCPEAQDITASVRDLPTVRTHIGRARAWLRIALMQKKLSDYLQALIEHREDSLFDYYEPHALMMSDEIVVIMGILVGLNVIDCNLCVKEEDLDSQQGVIDFSLYLRSSSRNADAAPEDSAPPALLDATGQGNMIAVLDQKNYIEELNRHLNATVGNLQAKVESLTTTNALMKEDLAIARNSLLALQAENQAMRQSTSAGDNNSTGSGGSSDKDKEKASEELVEERRKNSELEKELKLQVSLKAESDMAMKLLEKDIHEKQDTIVSLRRQLDDIKQINLEMYRKLQDCKASLTHKTELMTKLEVQKEDMASTIDQLEKKWSHDKSNLGEILKTTSQTLTTQVTASEERAARAEAESRIEREWRISLQEKELKLKEKIANLQGCLKELSEEKERNGKLKADLDKVRTQWSEAQTTLEELGIQLSVSKLKVSEMQDQERRQRQLLSGSAQSLQAMPEAVGSPGIWAPDSIATHCTACEREFNLTRRKHHCRSCGEIFCKACSEHTLPLLNAQGQPGKPVRVCDNCYAAK
Protein: Charged multivesicular body protein 4c (Chromatin-modifying protein 4c) (CHMP4c) (SNF7 homolog associated with Alix 3) (SNF7-3) (hSnf7-3) (Vacuolar protein sorting-associated protein 32-3) (Vps32-3) (hVps32-3) (Q96CF2)
Organism: Homo sapiens (Human)
Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: upon phosphorylation by AURKB, together with ZFYVE19/ANCHR, retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ANCHR and VPS4 and subsequent abscission. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan.
Subcellular location: Cytoplasm, cytosol. Late endosome membrane {ECO:0000305|PubMed:14583093}; Peripheral membrane protein {ECO:0000305}. Midbody, Midbody ring {ECO:0000269|PubMed:22422861}. Note=Localizes to the midbody during late cytokinesis. During its recruitment, localizes initially to the midbody arms, before being directed to the central region, the midbody ring, also called Flemming body. Phosphorylation at Ser-210 by AURKB triggers localization to midbody ring. {ECO:0000269|PubMed:22422861}.
Interaction partners:
- Programmed cell death 6-interacting protein
- Charged multivesicular body protein 5
- Charged multivesicular body protein 2a
- Vacuolar protein sorting-associated protein 4A
- Vacuolar protein sorting-associated protein 4B
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 3
- Charged multivesicular body protein 7
- Charged multivesicular body protein 4b
- Charged multivesicular body protein 1b
Sequence:
MSKLGKFFKGGGSSKSRAAPSPQEALVRLRETEEMLGKKQEYLENRIQREIALAKKHGTQNKRAALQALKRKKRFEKQLTQIDGTLSTIEFQREALENSHTNTEVLRNMGFAAKAMKSVHENMDLNKIDDLMQEITEQQDIAQEISEAFSQRVGFGDDFDEDELMAELEELEQEELNKKMTNIRLPNVPSSSLPAQPNRKPGMSSTARRSRAASSQRAEEEDDDIKQLAAWAT
Protein: Probable transcriptional regulator (Q9HTN1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Lipoprotein
- Neutral ceramidase
- Alanine racemase N-terminal domain-containing protein
- Probable transcriptional regulator
- Uncharacterized oxidoreductase PA3106
- Probable transcriptional regulator
- Probable acyl-CoA dehydrogenase
- DUF2804 domain-containing protein
- Probable cytochrome c
Sequence:
MHNNAADARYELAQVSTFLLQTLAEVVEGHGVDPARLCRGLGFTVEDLQDPTQRISYRQAVSMIQRALQALPERGLGLWVGHQNVLGTLGLLGHVLSLCRTLRDAFDIGVRYQHSSGGIVTSSVYQQGDTFFVEVECHLPSSEVQVFAIEEFFASLLVYGRALVSPAFEPLGIELIHAAPPYAGEYLRLLGPQVRFGCLHNRMAIASHWLDMRLPNHNLPALRQALALLEQESTQVHRKLDLVQAVERAIARDLSLGSQIERISAELNMSSRTLRRRLAEHGLTFEALLEQVRRGRAMSLLGNPGMSIERITEEVGYRDIRSFRRAFKRWTGVSPATFRSEGTSPLDQVFTLAARR
Protein: FERM domain-containing protein (G5EF18)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAEVSVAIVRLKISALSDKAIPSAQDFEICVKEEPSTAKNFGPVKHDYNIKKRVTVGGHTIGADVFKLPNFSFEPSKVSTLEDMIHDYFKRTGNIIRRSVRIPLHDDLHQPSSSTKPFVGHVPGLSLVCVPVFNKESVEVANSRYENLQKMVNLCHNQPEMFDIHTKNMILILERWLIDSQTFDSYFLSHFFMKESSRTRIKTCVHNPAFIDLQEQCIRHMSHSVRSNVSSASADLDDRVHVANIAKIAMLRYNKFTISVINPAFNPNFASEDSSCVYFYPGIKQCRAQRAASSTSQDMRSRLYPLHKAAEDGNAEEIRRFLKIGMDSNLRDDDSWTPLHYACFHGHLEVVHELLNSPQMTAINAQNKGGATALQYAVINGNEYLVEILTSHASIDVNIQNNEGYRPIDYCGNHPAIQKILELQIFKSKINVDTSIGSFSIKSRSPEEATVGEVLDRLAEETQLNREQMNCFALFVYSESMSLQLQPDSLIDGKLKVDKWNTTIRKLVGDIPFETPRLKLKRNAYATARMEIVTKVDNNSFAWSTILDEAIHSYLAGHLIANSKEEITKFAAIVCRTMHGRDFKPSSKNLSNLYPQYMLDNHDRGKLADRLKAQLRKNETQNDMQLEAEFISMARGLVTYGASFFDVDVFTKKVRK
Protein: Probable serine/threonine-protein kinase gdt2 (EC 2.7.11.1) (Growth-differentiation transition protein 2) (Q55CZ1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Regulates the transition between growth and differentiation.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MNYILYILLILIIFSINNTFSIGSFVYTPDGYYNLYRINKFENFSKIPTKANSVNVEPHELYYPDICDSALKNKNSNEFSIDNFPGSPFLKANIKITKGSNMTLDPLLSIHPSYINILCIEGSFTAGSQQTLTLGGIIVLPGGNFHCNNCVLQFVDLSSTIIKIDPFGFLPGILSLGGSISLIGSQRILYSAKPIEDNVLEVNDISTLDPFNGFNVSIVSDSFPNVRTSRFTYNKNKLEMQDLTIPTTDLNIKLFFNDSGSLKFGGISTRTKSSIYITGDTKLHIENYLLDSIGKTSNKEYDDTKLTFSSDNPNNVTDIIIGKNQRFRNSLYIEFSNSVTIKNSVIIGNTGSSRSSLVFFQSNVNISGNLIVGTAGSSMIAQYGTEYIESSNNYFSLVLPNEFPTSPAFMDYGHEGNGIYSLSPNIFSTNDIFNGQKILYNFNFISRENVTGFDKDCFAPCDINSIVVPSLSQEPIDFSKNLVNPISINPVDYFLIVNSDEELKNTFFTIKDSTISSKIIVNLKGSGLVLKNIIGVNNFKLTGQVKRLDIYDSFFGSSTTPSLGDNGIKSSAVIIKNSSFYIDDFQLQNNQIYGSSIVPYLYELLNVDEFILVDSIFPTSQYQIPVGGKLDLIVKLVIISPVISRITCELESDNETITSSAISESVNKECKFPLTFKNDGSVNLKVTVKLKNVGDSEIMYIINFPKITIFSNYSFYSGWSMENSTENGIISVDGNSFKKGCSISSNDNSNNCTISNNIKYITNLPKLNISNDLNELFLNGITSINSNELVTITTRIDSETKYYQIQLFFIHQPIDDQPTPLSIYIENQPVFLLEPLESNSAPIFKNLTFNFDNINSLENINISFATRGNTYLTSMAIYSSLVIEYPIPVEKINLLPIIVPICVTVLVLLSILIVFFGARYYKHKKRRRLEIAVFGVELYSKKPSNNKSPVPSTPLIINSNQEQSSSNHISITVNRNSDIQTQSENNNLEPTTVETTTTTTTTAAGAILQTNVTLEMENLEIKPIINNNEPFFEDYSDEYDDSSDGAELNEDDVEDYINIIRGGNIKIEAEGELFVRQFERNTFDQEFFEYKKSKIPSPHLVPSLAHGDFIENPLNIIDILLDPVTNEIPLEHYLKTYKNRNGQSGKYRTNTQTHVLIADTIFQHCNDPDLPVSVSPYICDFGMNGRKSDLGEVCHDTITFKNKLSEPLYALFLFPEGDDSSITSSPFQSIELKPNVETSISLSVTLFSTTKYNEKVIVRFETLDVKQSWSTFVFLRLESELTNIIDFNEIIIKNYISEGTFGIVYRGIWRSSPVAVKLLKNEYVDHDEIEKEISLLERLRHPNILLYVGRFIFSGIHGIVTDYCSKGCLSKYIHENKYKITIIQKIRILIDISKACAYLHRNGITHRDLKPENILITSLNPKSLVCAKVSDFGTSKETNERYNLQTRRGTVAYMSNEILSQGSYTKSTDIYSFGMLCYELFSERIPYYSEPHWRIRELVLKNERPSLDQEIFKDTDISDIVTRCWSKNPSQRPTFDYLSKYLKHLLKKYDINNIIYDKDKKNKKKNKNNNNNNNNNNNNNNNNNNNNNNNDDHDDNNNNINDSDCDNNKNNNNNNNNNNNNNNNNNNNNNNNNNNNN
Protein: Annexin A7 (Annexin VII) (Annexin-7) (Synexin) (P20073)
Organism: Homo sapiens (Human)
Function: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.
Interaction partners:
- Sorcin
- Galectin-3
- Annexin A11
- Vacuolar protein sorting-associated protein 26A
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
Sequence:
MSYPGYPPTGYPPFPGYPPAGQESSFPPSGQYPYPSGFPPMGGGAYPQVPSSGYPGAGGYPAPGGYPAPGGYPGAPQPGGAPSYPGVPPGQGFGVPPGGAGFSGYPQPPSQSYGGGPAQVPLPGGFPGGQMPSQYPGGQPTYPSQINTDSFSSYPVFSPVSLDYSSEPATVTQVTQGTIRPAANFDAIRDAEILRKAMKGFGTDEQAIVDVVANRSNDQRQKIKAAFKTSYGKDLIKDLKSELSGNMEELILALFMPPTYYDAWSLRKAMQGAGTQERVLIEILCTRTNQEIREIVRCYQSEFGRDLEKDIRSDTSGHFERLLVSMCQGNRDENQSINHQMAQEDAQRLYQAGEGRLGTDESCFNMILATRSFPQLRATMEAYSRMANRDLLSSVSREFSGYVESGLKTILQCALNRPAFFAERLYYAMKGAGTDDSTLVRIVVTRSEIDLVQIKQMFAQMYQKTLGTMIAGDTSGDYRRLLLAIVGQ
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit (DDOST 48 kDa subunit) (Oligosaccharyl transferase 48 kDa subunit) (Q641Y0)
Organism: Rattus norvegicus (Rat)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q29381}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q29381}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Serine/threonine-protein kinase Chk1.
- Tumor suppressor candidate 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1
- Oligosaccharyltransferase complex subunit OSTC
- Mannosyl-oligosaccharide glucosidase
Sequence:
MKMVPRLAVRAWPLCGLLLAALGCVCASGPRTLVLLDNLNVRDTHSLFFRSLKDRGFELTFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINVETISAFIDGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDVSDLGQHTLIVADTENLLKAPTIVGKSSLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGRNTLLIAGLQARNNARVIFSGSLDFFSDAFFNSAVQKAAPGAQRYSQTGNYELAVALSRWVFKEEGVLRVGPVSHHRVGETAPPNAYTVTDLVEYSIVIEQLSNGKWVPFDGDDIQLEFVRIDPFVRTFLKRKGGKYSVQFKLPDVYGVFQFKVDYNRLGYTHLYSSTQVSVRPLQHTQYERFIPSAYPYYASAFSMMAGLFLFSVVFLHMKEKEKSD
Protein: tryptophan--tRNA ligase (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (Q9U4Y1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADTKETVVEGVEALTLNGKPDAEPVETGTDAQAQEGATAPTEDVVDPWNVASSNDAGVDYDKLIKRFGSSKIDEELIARFEKITGKPAHHFIRRGMFFSHRDLHTILTLREQGKPFYLYTGRGPSSGSLHVGHLVPFIMTKWLQETFDVPLVIQLTDDEKTLWKDLKVEDAIKLGRENAKDIVAIGFDVNKTFIFNNLEFVGKCPAMYQNIIRIQKCVTFNQVKGIFGFGDSDIIGKIGFPAAQAAPAISSTFPFIFGNRKVHCLIPCAIDQDPYFRMTRDVAPRLGFPKCALIHSTFFPALQGAKTKMSASDQNSAVYLTDTPKQIKNKINKYAFSGGRVTVEEHRKLGGVPEVDVSYQLLKFFLEDDAKLEEVRVAYSKGEMLTGEIKKLAVETLTPIVEQHQAARKLITDEVLDKYFELRPLKFGS
Protein: Hypermethylated in cancer 1 protein (Hic-1) (Zinc finger and BTB domain-containing protein 29) (Q14526)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor. Recognizes and binds to the consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. May act as a tumor suppressor. Involved in development of head, face, limbs and ventral body wall (By similarity). Involved in down-regulation of SIRT1 and thereby is involved in regulation of p53/TP53-dependent apoptotic DNA-damage responses. The specific target gene promoter association seems to be depend on corepressors, such as CTBP1 or CTBP2 and MTA1. In cooperation with MTA1 (indicative for an association with the NuRD complex) represses transcription from CCND1/cyclin-D1 and CDKN1C/p57Kip2 specifically in quiescent cells. Involved in regulation of the Wnt signaling pathway probably by association with TCF7L2 and preventing TCF7L2 and CTNNB1 association with promoters of TCF-responsive genes. Seems to repress transcription from E2F1 and ATOH1 which involves ARID1A, indicative for the participation of a distinct SWI/SNF-type chromatin-remodeling complex. Probably represses transcription of ACKR3, FGFBP1 and EFNA1.
Subcellular location: Nucleus {ECO:0000269|PubMed:11554746}.
Interaction partners:
- C-terminal-binding protein 1
- C-terminal-binding protein 2
- NAD-dependent protein deacetylase sirtuin-1
- Methylated-DNA--protein-cysteine methyltransferase
- SUMO-conjugating enzyme UBC9
- DNA
- Ras association domain-containing protein 1
- 14-3-3 protein epsilon
- E3 SUMO-protein ligase PIAS2
- Catenin beta-1
Sequence:
MTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLNNQRTKGFLCDVIIVVQNALFRAHKNVLAASSAYLKSLVVHDNLLNLDHDMVSPAVFRLVLDFIYTGRLADGAEAAAAAAVAPGAEPSLGAVLAAASYLQIPDLVALCKKRLKRHGKYCHLRGGGGGGGGYAPYGRPGRGLRAATPVIQACYPSPVGPPPPPAAEPPSGPEAAVNTHCAELYASGPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPGAGGDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPESFGDNLYVCIPCGKGFPSSEQLNAHVEAHVEEEEALYGRAEAAEVAAGAAGLGPPFGGGGDKVAGAPGGLGELLRPYRCASCDKSYKDPATLRQHEKTHWLTRPYPCTICGKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLGGLPGVPGPDGKGKLDFPEGVFAVARLTAEQLSLKQQDKAAAAELLAQTTHFLHDPKVALESLYPLAKFTAELGLSPDKAAEVLSQGAHLAAGPDGRTIDRFSPT