wanglab/gogpt-training-data huggingface dataset:
Protein: Glycerophosphodiester phosphodiesterase domain containing 3 (Glycerophosphodiester phosphodiesterase domain-containing 3a) (Lysophospholipase D GDPD3a) (Q6P2T3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Ectonucleotide pyrophosphatase/phosphodiesterase 2
- Glycerophosphocholine cholinephosphodiesterase ENPP6
- Lysophosphatidylcholine acyltransferase 4
- Glycerophosphodiester phosphodiesterase domain-containing 1
- Glycerophosphodiester phosphodiesterase domain-containing 3b.
- lysoplasmalogenase
- Protein yippee-like 3
- Aspartate beta-hydroxylase domain-containing protein 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase.
- Double C2-like domain-containing protein alpha isoform X2
Sequence:
MASCLYYLLPAVGGYALTSLYFLRNPQILHKMKQTAFRCTHISHRGGSGERIENTIEAFTHAVEVGTEMLELDCHLTKDGFVMVSHDENLLRQTGQDVSISSLNLEDLPPYKETLEVTFKTGHFSTGSDRKLALLEDVFRKFPHTAVNIEVKENNIVLIEKISELVKQYNREGISVWASVDSTIMENCRKINSSMPYMFSQKRGLQLLLLYYTGLLPFVPLGESFLQFYFPPIFNKAYIPDTEILKSRLVIFLIERLTMRKALFKHLRERGIQIHLFVCNEEQDIDAAFAAGATGVMTDYPTLLSNYIRRRKQAT
Protein: FI20063p1 (IGF-II mRNA-binding protein, isoform J) (E1JJM0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASELDQFADLELSKEDREQIFDPPLDRQQLEGAGTSRAAVGLNGVEFEGSKLHAEQLDKNQRRSQRNQRNPYPGMPGPGRQADFPLRILVQSEMVGAIIGRQGSTIRTITQQSRARVDVHRKENVGSLEKSITIYGNPENCTNACKRILEVMQQEAISTNKGELSPECSEICLKILAHNNLIGRIIGKSGNTIKRIMQDTDTKITVSSINDINSFNLERIITVKGLIENMSRAENQISTKLRQSYENDLQAMAPQSLMFPGLHPMAMMSTPGNGMVFNTSMPFPSCQSFAMSKTPASVVPPVFPNDLQETTYLYIPNNAVGAIIGTRGSHIRSIMRFSNASLKIAPLDADKPLDQQTERKVTIVGTPEGQWKAQYMIFEKMREEGFMCGTDDVRLTVELLVASSQVGRIIGKGGQNVRELQRVTGSVIKLPEHALAPPSGGDEETPVHIIGLFYSVQSAQRRIRAMMLSTNPPPITKKQKAAKEQLQQQQQSLAGAASSGSQQQQPQSPSQQQALPPQLHHQPVSSASSSSTPPAHHQQQASTAATSHQLQQQQPSPPPPGNATAAAAQQQQQLASSQQ
Protein: Cohesin subunit SCC3 (Irregular cell behavior protein 1) (P40541)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the MCD1/SCC1 subunit of the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750, ECO:0000269|PubMed:9990856}. Chromosome {ECO:0000269|PubMed:9990856}. Chromosome, centromere {ECO:0000269|PubMed:9990856}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin except at centromeres, where cohesin complexes remain. At anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.
Interaction partners:
- Structural maintenance of chromosomes protein 1
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein 1
- Sister chromatid cohesion protein PDS5
- Meiotic recombination protein REC8
- Sister chromatid cohesion protein 2
- Protein RAD61
- N-acetyltransferase ECO1
- Separin
- Structural maintenance of chromosomes protein 4
Sequence:
MTAVRRSTRIRTKSQVIEEDYDDEQNTSAQHVESDKITAKTQHEEEEEQDTGESEESSSEDDYEDQDDDDYVDTATAKRKSRKRKPKSASNTSSKRQKKKPTSAQKSAVSHAPAYHRSKKDQDQYLEIAKDFQPTELFDILSTSEDVSIEELLREWLETYSENRDKFLQEFINLLLNCCGSVARVEDHDVHSNESSNETIGEIQLLFQRQKLHEFYLLISKENKKRKNFKMGPLYQNFAEFMTKLLEVANDLQLLYVESDEDDTQIVTGNLVLDLLTWLSSFSVCKIRCFRYISTLTLYLFQDYLTQQAVNLEKNYLAKLSKQLSLEEKKKRPNNKTLEKLESTIAETQGSKVVIDSIIDNIVKLCFVHRYKDVSDLIRSESMLHLSIWIKNYPEYFLKVTFLKYFGWLLSDNSVSVRLQVTKILPHLIIQNHNSKSTDNSAIRQVFERFKTKILEVAIRDVNLDVRIHSIQVLTEASSLGYLDDSEILIISSLMFDEEFDPFKTSSFNKRSKFLSTVAKFLARVIKEKFDEFIKTHEDLPKEVDGLEVGPVVQVGIFIKILNDSLIYHLKDCAEVDSRTKIRMLTQAAEFLSPYISTHLKTICNLLISDTESNELIQKLQNSANNNSDDEDVDDEELDITPLFPIDRNSTILYLNVFHGLCAGANNPKIQTKDSVKEIVLPLFYDLLNAASIESADILCPLLESFITFSLDDWISIGYETELKKITDKTIKAFMDSTIGNSKVDMKYDIFAKFIHHIHHFEKKELQEKFLNQIATLKIHLKKFLQEKMDPNNSRDDYKDLTCSLYELYINKLTILGRDYPIEVDEELLQLFLNNFVSRIPIMFQDFDDSTAQEINFKMLVLLATWNLEKWREIIEKVRDYENSISKDLRSVWKPIAAIIGRLNTLVISLAATNETFENINSLFYLKWSACTSLMDIIVAIKIFELKLPADATTWRYSMSEQFPFYLHDNASKVLLKIFLYLESLFAKQVDVQLERVADEDANLNDLPETGFFENIETEFLLFTVKLKGLMKLNILDERFASRVALNKEKLGPLFKKIVDDTIMENPEPNKKNIQKAKSNQTQREKAPLQPNSERETDHANTENNDPDIPMTIDLEPIEESSQNNSELAPIEEHPTVVDAIDNSDEITQD
Protein: Uncharacterized protein, isoform C (M9NED4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDVPDDNFGPSKPCDKQPLAGNSSSATNSSSHTGGNGNVDSAFESSTAAGPSSGANQSSTGGAIDEQGSIGEQSAGVGQNIIEGDLLVLNANSTNVDLSTHRDGSSFKDSNTEQGKKSTMIKTSKTLNDKSQFERRRRRGRQRERHREPSTHRDDLEPCDLGLMGWTGEFPKLTPISNIESNSDKEPLVEDKKEDTTKKQAEADHTLHKSLKDARIVKRSMSTHSPPEHSRRSVRFSSHTPLTDETNIMKETSTETSLKVIFERLKQTGVERDLFIPSSENPRPRSNGSPVPKVAEMEHVAVVKCKTVAKQGAVVKGKAGLANPSNVMPQTPALTVTGKRVSKPKVPKGASPPSEGWTSTRAVKGNSRADYTNSSSCGSPIGNTNIRRRRAHAKAAPDKSKPCVRCAASVHPSGPKLCKKCIYEKGYANKKWMKKTGGNEDHYDDDDDSDFSMIEVTLENEISVQQAEKKQLENVNKQTVIKEQEVVVIGGRKAIAIIADPIGCNLKVIPNRQNLAGLKKISKDKCSSSLVQSLGDCHIGCQIVMAVMKIMTMKDRVNMAQVCKTWAMISQDKSVWRTVMLRDTHISNWPRFIRELANNCTRELDMLGVILPNPPDILATLDISVLKALRVLRTCPVDDQFLFKVFRELPQLLELRAICYSPTFNFLNLARQWSKIRVLQILMTDHRSKVESLDSLGDLVHLTELNIRGVNYIGSQDFRFLKKLVNLKVLVLSSCQGMDTEEFGQQVLPFLTSLRRLRLENKHMINTTFPLYHIMCGVAAACSVQQLELVNVEVDDLLTSLIGMCTTVTHLLLVPKCLQNSANVIYSVMRAVRENASQLRVFRLGLVTQLLSATGELYRGSKKDVIPVERPVPGIPLDDDLNYCAPDDRCIETDHTECVTFLPAKRLLMILRDVAPTTFVTFVKVNMFNSTMVTFLKRPQLKNK
Protein: Non-classical arabinogalactan protein 31 (Hydroxyproline-rich arabinogalactan protein 31) (Q9FZA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proteoglycan that may contribute to the strengthening of cell walls.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:17885091}.
Interaction partners:
- Classical arabinogalactan protein 9
- Leucine-rich repeat extensin-like protein 6
- Hydroxyproline-rich glycoprotein family protein
- Classical arabinogalactan protein 1
- Lysine-rich arabinogalactan protein 19
- Extensin-3
- Fasciclin-like arabinogalactan protein 16
- Fasciclin-like arabinogalactan protein 15
Sequence:
MGFIGKSVLVSLVALWCFTSSVFTEEVNHKTQTPSLAPAPAPYHHGHHHPHPPHHHHPHPHPHPHPPAKSPVKPPVKAPVSPPAKPPVKPPVYPPTKAPVKPPTKPPVKPPVSPPAKPPVKPPVYPPTKAPVKPPTKPPVKPPVYPPTKAPVKPPTKPPVKPPVYPPTKAPVKPPTKPPVKPPVSPPAKPPVKPPVYPPTKAPVKPPVSPPTKPPVTPPVYPPKFNRSLVAVRGTVYCKSCKYAAFNTLLGAKPIEGATVKLVCKSKKNITAETTTDKNGYFLLLAPKTVTNFGFRGCRVYLVKSKDYKCSKVSKLFGGDVGAELKPEKKLGKSTVVVNKLVYGLFNVGPFAFNPSCPK
Protein: Gametocyte-specific factor 1-like (Protein FAM112A) (Q9H1H1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEPEAFEICPYDPHHRIPLSRFQYHLASCRRKNPKKAKKMATCKYNACHVVPIKNLEEHEAVCVNRSAVEEEDTENPLKVSPPSSEQNDDTQQVSPCLPSPDIWNVDGANCQHVFVLKTFFPQKVVCENDTKESARETSPQKILRPGQ
Protein: T-cell-specific guanine nucleotide triphosphate-binding protein 1 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb5) (Q62293)
Organism: Mus musculus (Mouse)
Function: Involved in innate cell-autonomous resistance to intracellular pathogens, such as Toxoplasma gondii. During avirulent type II T. gondii infection, recruited to the parasitophorous vacuole (PV) membrane, leading to PV vesiculation and rupture, and subsequent digestion of the parasite within the cytosol. Not recruited to virulent type I T. gondii PV membrane. May confer an antiviral state for vesicular stomatitis virus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19285957}. Endoplasmic reticulum {ECO:0000269|PubMed:19285957}. Golgi apparatus {ECO:0000269|PubMed:19285957}. Note=In astrocytes stimulated with IFNG or TNF, diffuse cytoplasmic localization decreases and the protein partially relocalizes to the endoplasmic reticulum and Golgi apparatus (PubMed:19285957). Due to sequence similarity with Tgtp2, it is impossible to assign unambiguously experimental data published in the literature to Tgtp1 or Tgtp2 gene (Probable). {ECO:0000269|PubMed:19285957, ECO:0000305|PubMed:22892676}.
Interaction partners:
- Guanylate-binding protein 7
- Guanylate-binding protein 2
Sequence:
MAWASSFDAFFKNFKRESKIISEYDITLIMTYIEENKLQKAVSVIEKVLRDIESAPLHIAVTGETGAGKSTFINTLRGVGHEEKGAAPTGAIETTMKRTPYPHPKLPNVTIWDLPGIGTTNFTPQNYLTEMKFGEYDFFIIISATRFKENDAQLAKAIAQMGMNFYFVRTKIDSDLDNEQKFKPKSFNKEEVLKNIKDYCSNHLQESLDSEPPVFLVSNVDISKYDFPKLETKLLQDLPAHKRHVFSLSLQSLTEATINYKRDSLKQKVFLEAMKAGALATIPLGGMISDILENLDETFNLYRSYFGLDDASLENIAQDLNMSVDDFKVHLRFPHLFAEHNDESLEDKLFKYIKHISSVTGGPVAAVTYYRMAYYLQNLFLDTAANDAIALLNSKALFEKKVGPYISEPPEYWEA
Protein: Bromodomain-containing protein C631.02 (Q9HGP4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Histone H4
- Transcription initiation factor TFIID subunit 7
- Putative JmjC domain-containing histone demethylation protein 1
- SWR1-complex protein 4
- Histone acetyltransferase mst1
- Histone H3.1/H3.2
- Helicase swr1
- Uncharacterized protein C530.07c
- Putative transcription initiation factor TFIID 111 kDa subunit
- Transcription initiation factor TFIID subunit 2
Sequence:
MTPVQVPNLDVSVTSSLITTAPVTGNAATISTFTPGSPEPSMNGEEKESSYFPISENDDGTLDLFGDSELEKEQKGDNQETDYSSQYLHPTPPYTNFDDESPSSPTHPSVSNITVDGDSKKHSLQLQEEEKSSESLDSHTHPPKRVRNEDDSLTFSKTSPVSPSSLKDGASNTVTNDASNKIKSEASESASPSALQALDSTAAGSSKEHSSPHDETVKKEENDKDQYPPMTKEQHKYIHAMLRQLRRGRDSIPFRAPVDPVKQNIPDYPTIIKNPIDLGTMQKKFSSGVYSSAQHFIDDMNLMFSNCFLYNGTESPVGVMGKNLQATFERQLKQLPSAYVTSYSRPGRRPRSMTAPKGGARTRRQAAMYSNSSSGIRETMYDLKPHRRKDAAEMKFCQSVLKELLKKQHEAYAYPFYKPVNPTACGCPDYFKVIKHPMDLGTMQNKLNHNEYASMKAFEADMVLMFKNCYKFNSAGTPVHLMGKKLESIFQKLWANKPDFDSETYMGMSSVNTDYYYGDNEVFDSGDEFLEDDGEEFEAVNRQIHKLQSTLQAMKSRARSSSVSRRSRSRSLSVDIYPPITYEMQNELAEQCNYLSADQLSHVAEILRAALPHLRNTDEIEIDVSAMPPDVFYKVYYYVCKGDEIGAEALATASHTHQEKKKGRALSETEQAEKIRQLRAQLDRFSGIAQNKNTVTGNIAAYNTKSLGSDDSSSEDDGESSESSDSA
Protein: Flowering time control protein FPA (Q8LPQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in the regulation of flowering time in the autonomous flowering pathway by decreasing FLOWERING LOCUS C mRNA levels. Required for RNA-mediated chromatin silencing of a range of loci in the genome. Cotranscriptionally recognizes aberrant RNA and marks it for silencing. Controls alternative cleavage and polyadenylation on pre-mRNAs and antisense RNAs. Acts redundantly with FCA to prevent the expression of distally polyadenylated antisense RNAs at the FLC locus.
Subcellular location: Nucleus {ECO:0000269|PubMed:17916737}.
Interaction partners:
- WD-40 repeat-containing protein MSI4
- Flowering locus K homology domain
- Protein FLOWERING LOCUS D
- 30-kDa cleavage and polyadenylation specificity factor 30
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- 25S rRNA
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
- At1g29530
- Inactive protein FRIGIDA
- Secreted protein
Sequence:
MALSMKPFRADDSGFQSNNLWVGSLTPETTESDLTELFGRYGDIDRITVYSSRGFAFIYYRHVEEAVAAKEALQGANLNGSQIKIEYARPAKPCKSLWVGGIGPNVSKDDLEEEFSKFGKIEDFRFLRERKTAFIDYYEMDDALQAKSMNGKPMGGSFLRVDFLRSQAPKKEQWAGSYDNRNGNMNHKPQYPHSYEDFKGDVQPSKVLWIGFPPTATQCNDEQILHNAMILFGEIERVKSYPSRNFALVEFRSAEEARQCKEGLQGRLFNNPRIKIMYSNDELPPEQDDTSFYSGMKRSRTDMFNNDPSFVSSPHSTGIPGSMRPLRGTNERSYNGAEYNDVVGKEPNWRRPSANGTGILPSPTGPGILPSPAQGTRRPMRSNPDSWEGYDPAQLVRESKRTRRDGSVDGFTPMGVDERSFGRGSVAARPIRGPPDSDHIWRGMIAKGGTPVCCARCVPMGKGIETKLPEVVNCSARTDLNMLAKHYAVAIGCEIVFFVPDREEDFASYTEFLRYLSSKDRAGVAKLDDGTTLFLVPPSDFLTDVLQVTRQERLYGVVLKLPPPAVPVTASYRQESQSNPLHYMDQARDSPANASHSLYPPRENYIRGAPEHLTAASKPSVSEPLRIPNNAAPQAGVSLTPELLATLASILPATSQPAAPESHQPMSGPSTVVSTAHQSNGLYNGEAPSQAWKRGPQTVHDASNQSFQQYGNQYTPAGQLPPPPSRYPPASNNPNYTSGMVHGNMQYQSQSVNMPQLSPLPNMPHNNYSMYTQGSSNHPVSQPMVQQYQPEASMPNQNYGPIPSYQQANFHGVTTNQAQNLNPSQFQAAMQPPADKANLEPQNQALRLQPMISGDGQGTTDGEVDKNQRYQSTLQFAANLLLQIQQKQQQQSSGTPAGQGP
Protein: Probable G-protein coupled receptor 34 (Q6XCC7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSSTESLQSFSSVWDNRSMWSNRSCPLEEEALRLPLAVLYSLIFLFGLLGNLLALWVFLFLHRRRNSVRVFLINVALADLVLLACLPFRVLYHALGNVWTLGPRMCRVVGNLFYMNMYVSITLLGLISLDRYLKIMGSHRGRRWLRGRSWSLVTCGLLWGLSVLMAVPMMALAEGNEEPGKCYQYKQRKHARGKAYFNLVMVAVFWLVFVVLLVSYGQIARRLLRASQDKPHLPNAARYARTARKSFVVPLLFTVCFVPYHAFRGFYVASQLQDISCETRRLMDRTNEAVLLLSALNSCLDPVMYFLLSGSVRRATLQALAQCLRLHAEPPATNSSTTELRRTSVSHASTTAVLDTSRCSLGNITTLRSQHTDLHPHSEPCVHRSGLSD
Protein: T. brucei spp.-specific protein (Q57Y43)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEDVNRQNHNDSQKRHEYPGRSGENEPSHNQSPLREGESGYRKALCRISLQQMITRPLLQNYNRREVSGNIDVYTYIYIYYIIQVARGDVLRGASQGAQSLQHGNRHINTSLCTYVCLLPPSLFTWNVFHHVRLFLQPLQYLNNILCVVTYLFSSFSFSLFLTMVAFFASMSVVAPNETIIGLR
Protein: ATP-dependent zinc metalloprotease FTSH 5, chloroplastic (AtFTSH5) (EC 3.4.24.-) (Protein VARIEGATED 1) (Q9FH02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of a complex that function as an ATP-dependent zinc metallopeptidase. Involved in the thylakoid formation and in the removal of damaged D1 in the photosystem II, preventing cell death under high-intensity light conditions. Not involved in the degradation of the light-harvesting complex of photosystem II (LHC II) or in thermotolerance.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:12167156, ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:18431481}; Single-pass membrane protein {ECO:0000269|PubMed:12167156, ECO:0000269|PubMed:14630971}; Stromal side {ECO:0000269|PubMed:12167156, ECO:0000269|PubMed:14630971}.
Interaction partners:
- ATP-dependent zinc metalloprotease FTSH 8, chloroplastic
- Zinc finger protein VAR3, chloroplastic
- Protease Do-like 1, chloroplastic
- Translation initiation factor IF-2
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- AT5g02160
- Protease Do-like 5, chloroplastic
- Protease Do-like 8, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 3, chloroplastic
- Protein THYLAKOID FORMATION 1
Sequence:
MATTSSNPLLLSSNFLGSQIIISAPTPKTTTKSLPFSVISRKRYQISQSEKLMKSLPSQAALAALLFSSSSPQALAVNEPVQPPAPTITAEAQSPNLSTFGQNVLMTAPNPQAQSSDLPDGTQWRYSEFLNAVKKGKVERVKFSKDGSVLQLTAVDNRRATVIVPNDPDLIDILAMNGVDISVSEGEGGNGLFDFIGNLLFPLLAFGGLFYLFRGGQGGAGGPGGLGGPMDFGRSKSKFQEVPETGVTFGDVAGADQAKLELQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISDALERIIAGPEKKNAVVSEEKKRLVAYHEAGHALVGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERLESGLYSRSYLENQMAVALGGRVAEEVIFGDENVTTGASNDFMQVSRVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADVVDAEVRELVEKAYVRAKEIITTQIDILHKLAQLLIEKETVDGEEFMSLFIDGQAELYVS
Protein: Pentatricopeptide repeat-containing protein At2g17670 (Q84J71)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGKVPSSFRSMPANLLVRKTTPSPPAPPRDFRNRTAVGGDSAKLPQNTQAPREPSLRNPFKSPNLSDAKSLFNSIAATSRIPLDLKFHNSVLQSYGSIAVVNDTVKLFQHILKSQPNFRPGRSTFLILLSHACRAPDSSISNVHRVLNLMVNNGLEPDQVTTDIAVRSLCETGRVDEAKDLMKELTEKHSPPDTYTYNFLLKHLCKCKDLHVVYEFVDEMRDDFDVKPDLVSFTILIDNVCNSKNLREAMYLVSKLGNAGFKPDCFLYNTIMKGFCTLSKGSEAVGVYKKMKEEGVEPDQITYNTLIFGLSKAGRVEEARMYLKTMVDAGYEPDTATYTSLMNGMCRKGESLGALSLLEEMEARGCAPNDCTYNTLLHGLCKARLMDKGMELYEMMKSSGVKLESNGYATLVRSLVKSGKVAEAYEVFDYAVDSKSLSDASAYSTLETTLKWLKKAKEQGLVP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (B3KNX7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVSEDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHSSRL
Protein: Multiplexin, isoform L (E1JIE2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRVLQGVMFALAMICTLLVPVLGSFELVGQSIKDALAEYTLTDIMNNNQFAGIEFGEAEDGFPAFRFLQTADVKSPYRMLLPEKLYEFAILITFRQSSLKGGYLFSVVNPLDTVVQLGVHLSPVVKNSYNVSLVYTQADQNIGRKLASFGVAHVPDKWNSIALQVLSDKVSFYYDCELRNTTLVTREPIELVFDSASTLYIGQAGSIIGGKFEGYLEKINVYGNPDAINVTCMPPPKATIAPTTADDGSIFYEGSGENILFEDSTEANILSDDFWNTGDEGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAKYTGECTCNASDILEAIKDNESLRESLRGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLPGVMGPPGPPGPPGLPENYDESLMVNSMGAFRGTTQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPGGLDGLASANGTKGEKGEKGEKGMRGRRGGTGATGPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSGGREGLKGDKGDRGQDGRDGLPGPPGLPSTGGGDGDSGGVQYIPMPGPPGPPGPPGLPGLSISGPKGEPGVDSRSSFFGDASYYGRPEPPRQPGHSHKHEETLGLVDGEEPYFSASSSNMNMKIVPGAVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVPIATPAPPTTVAPSMRFDLQSKNLLNSPPPLLNTPTLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRDLPVVNTRGDVLFNSWKGIFNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKLIILCVEALSQDRKRKKREIGDGSSHGESESREFKTADEYAAHLENLLL
Protein: Transcription factor E2-alpha (Immunoglobulin enhancer-binding factor E12/E47) (Transcription factor 3) (TCF-3) (Transcription factor A1) (P15806)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator involved in the initiation of neuronal differentiation and mesenchymal to epithelial transition. Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation. Together with TCF15, required for the mesenchymal to epithelial transition. Dimers bind DNA on E-box motifs: 5'-CANNTG-3'. Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer (By similarity). Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region.
Subcellular location: Nucleus {ECO:0000269|PubMed:12200424}.
Interaction partners:
- Rhombotin-2
- T-cell acute lymphocytic leukemia protein 1 homolog
- LIM domain-binding protein 1
- Erythroid transcription factor
- Myoblast determination protein 1
- Protein lyl-1
- DNA-binding protein inhibitor ID-2
- Catenin beta-1
- Core-binding factor subunit beta
- Runt-related transcription factor 1
Sequence:
MMNQSQRMAPVGSDKELSDLLDFSMMFPLPVANGKSRPASLGGTQFAGSGLEDRPSSGSWGSSDQNSSSFDPSRTYSEGAHFSDSHSSLPPSTFLGAGLGGKGSERNAYATFGRDTSVGTLSQAGFLPGELSLSSPGPLSPSGIKSSSQYYPSFPSNPRRRAADGGLDTQPKKVRKVPPGLPSSVYPPSSGDSYSRDAAAYPSAKTPSSAYPSPFYVADGSLHPSAELWSTPSQVGFGPMLGDGSSPLPLAPGSSSVGSGTFGGLQQQDRMGYQLHGSEVNGSLPAVSSFSAAPGTYSGTSGHTPPVSGAAAESLLGTRGTTASSSGDALGKALASIYSPDHSSNNFSPSPSTPVGSPQGLPGTSQWPRAGAPSALSPNYDAGLHGLSKMEDRLDEAIHVLRSHAVGTASDLHGLLPGHGALTTSFTGPMSLGGRHAGLVGGSHPEEGLTSGASLLHNHASLPSQPSSLPDLSQRPPDSYSGLGRAGTTAGASEIKREEKEDEEIASVADAEEDKKDLKVPRTRTSPDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLSSEKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSGVVGDPQLALSAAHPGLGEAHNPAGHL
Protein: Cytoplasmic dynein 1 intermediate chain 2 (Cytoplasmic dynein intermediate chain 2) (Dynein intermediate chain 2, cytosolic) (DH IC-2) (Q62871)
Organism: Rattus norvegicus (Rat)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11340075}. Cytoplasm {ECO:0000250|UniProtKB:O88487}. Note=Detected in the cytoplasm of pachytene spermatocytes. Localizes to the manchette in elongating spermatids. {ECO:0000250|UniProtKB:O88487}.
Interaction partners:
- Cytoplasmic dynein 1 heavy chain 1
- Cytoplasmic dynein 1 light intermediate chain 2
- Cytoplasmic dynein 1 light intermediate chain 1
- Dynactin subunit 1
- Dynein light chain roadblock-type 1
- Dynein light chain 2, cytoplasmic
- Dynactin subunit 2
- Dynein light chain 1, cytoplasmic
- Cytoplasmic dynein 2 light intermediate chain 1
- Dynein light chain LC8-type 1 like 1
Sequence:
MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAAVSVQEESDLEKKRREAEALLQSMGLTTDSPIVFSEHWVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRTLHWDTDPSALQLHSDSDLGRGPIKLGMAKITQVDFPPREIVTYTKETQTPVTAQPKEDEEEEDDVAAPKPPVEPEEEKILKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEEAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWSTKNNKPLYSFEDNSDYVYDVIGSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINASRADAEEEAATRIPA
Protein: Lysosome-associated membrane glycoprotein 2 (LAMP-2) (Lysosome-associated membrane protein 2) (CD107 antigen-like family member B) (LGP-110) (LGP-96) (Lysosomal membrane glycoprotein type B) (LGP-B) (CD antigen CD107b) (P17046)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live. Binds target proteins, such as GAPDH, and targets them for lysosomal degradation. Plays a role in lysosomal protein degradation in response to starvation. Required for the fusion of autophagosomes with lysosomes during autophagy. Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes. Required for normal degradation of the contents of autophagosomes. Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits. Is not required for efficient MHCII-mediated presentation of endogenous antigens (By similarity).
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:11082038, ECO:0000269|PubMed:1794981, ECO:0000269|PubMed:18644871, ECO:0000269|PubMed:2590192, ECO:0000269|PubMed:8662539}; Single-pass type I membrane protein {ECO:0000269|PubMed:11082038}. Endosome membrane {ECO:0000250|UniProtKB:P13473}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Cell membrane {ECO:0000250|UniProtKB:P13473}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P17047}. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane. {ECO:0000250|UniProtKB:P13473}.
Interaction partners:
- Lysosome-associated membrane glycoprotein 1
- CD63 antigen
- Ribonuclease pancreatic beta-type
- Heat shock cognate 71 kDa protein
- Cathepsin D
- Heat shock protein HSP 90-beta
- Microtubule-associated protein 1 light chain 3 alpha
- Early endosome antigen 1
- Heat shock protein HSP 90-alpha
- Ubiquitin carboxyl-terminal hydrolase isozyme L1
Sequence:
MRLLSPVTGSKLVLLFLFLGAVRSDALKLNLTDSKGTCLYAEWEMNFTITYEALKVNETVTITVPDKVTYNGSSCGDDKNGAKIMIQYGSTLSWAVNFTKEASQYFINNITLSYNTNDTKTFPGAVPKGILTVIIPVGSQLPLGVIFKCSSVLTFNLSPVVQHYWGIHLQAFVQNGTVSKHEQVCKEDKTATTVAPIIHTTVPSPTTTLTPTSIPVPTPTVGNYTISNGNATCLLATMGLQLNITEEKVPFIFNINPAITNFTGSCQPQTAQLRLNNSQIKYLDFIFAVKNEKRFYLKEVNVNMYLANGSAFHVSNNNLSFWDAPLGSSYMCNKEQVVSVSRTFQINTFNLKVQPFNVTKGEYSTAQDCSADEDNFLVPIAVGAALGGVLILVLLAYFIGLKRHHTGYEQF
Protein: Uncharacterized protein C922.04 (Q9URX2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Putative alpha,alpha-trehalose-phosphate synthase 100 kDa subunit
Sequence:
MKFFWVSSLLGLLGLSTAIPLSTEADALLDRKTIYFGMKAYDDVNCKGSTSYTISFNKCQAYPNINSINALTDGAVCTVYVYSSNNCTGEPVFQTDSDGIECINVDAFETGSWKFKC