wanglab/gogpt-training-data huggingface dataset:
Protein: High mobility group nucleosome-binding domain-containing protein 4 (Non-histone chromosomal protein HMG-17-like 3) (Non-histone chromosomal protein) (O00479)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
Sequence:
MPKRKAKGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPRPKKASAKKGEKLPKGRKGKADAGKDGNNPAKNRDASTLQSQKAEGTGDAK
Protein: Rap1 GTPase-activating protein 2 (Rap1GAP2) (GTPase-activating Rap/Ran-GAP domain-like protein 4) (Q5SVL6)
Organism: Mus musculus (Mouse)
Function: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ras-related protein Rap-1b
- Ras-related protein Rap-1A
- 14-3-3 protein zeta/delta
- 14-3-3 protein beta/alpha
Sequence:
MLAGLKVKKQELANSSDVTLPDRPLSPPLTAPPTMKSAEFFEMLEKMQGIKLEEQRPGPQKNKDDYIPYPSIDEVVEKGGPYPLIILPQFGGYWIEDPENVGTPTSLGSSVYEEEEEDSLSPNTFGYKLECRGEARAYRRHFLGKDHLNFYCTGSSLGNLILSIKCEEAEGMEYLRIILRSKLKTVHERIPLAGLSKLPSVPQIAKAFCDDAVGLKFNPVLYPKASQMIVSYDEHDVNNTFKFGVIYQKARQTLEEELFGNNEESPAFKEFLDLLGDTITLQDFKGFRGGLDVTHGQTGVESVYTTFRDREIMFHVSTKLPFTDGDTQQLQRKRHIGNDIVAIIFQEENTPFVPDMIASNFLHAYIVVQADNPGTETPSYKVSVTAREDVPAFGPPLPSPPVFQKGAEFREFLLTKLTNAENACCKSDKFAKLEDRTRAALLDNLHDELHTHTQVMLGMGPEEDKFENGGHGGFLESFKRAIRVRSHSMETMVGSQRKLHGGNLPGSLSGGIVHNSMEVTKTTFSPPVAAATAKNQSRSPIKRRSGLFPRLHSGSEGQGDSRTRCDSASSTPKTPDGGHSSQEIKSETSSNPSSPEICPNKEKPFIKLKENGRANISRSSSSTSSFSSTAGEGEAMEECDSGSSQPSTTSPFKQEVFAYSPSPSSESPSLGAAATPIIMSRSPTDAKSRNSPRSNLKFRFDKLSHASSSAGH
Protein: Diguanylate cyclase TpbB (DGC) (EC 2.7.7.65) (Q9I4L5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:20300602}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic di-GMP phosphodiesterase RocR
- Negative regulator YfiR
- Outer-membrane lipoprotein YfiB
- cyclic-guanylate-specific phosphodiesterase
- cyclic-guanylate-specific phosphodiesterase
- EAL domain-containing protein
- Dual specificity protein phosphatase TpbA
- Cyclic di-GMP phosphodiesterase PA2567
- Cyclic di-GMP phosphodiesterase PA4781
- FimX
Sequence:
MNRRRRYTGSNPSLRRVLYRAHLGVALVAVFTAGLAVTLVGLLTLRAYADPNQQLIARSISYTVEAAVVFGDAQAAEESLALIASSEEVSSAIVYDRQGQTLASWHRESTGPLHLLEQQLAHWLLSAPTEQPILHDGQKIGSVEVKGSGGSLLRFLLTGFAGMVLCLLLTALGAFYLSRRLVRGIVGPLDQLAKVAHTVRRERDFEKRVPEAGIAELSQLGEDFNALLDELESWQARLQDENASLAHQAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARLGGDEFAVLLAPLASGADALRIADNIIASMQAPIRLSDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQARGSRRLAELNDPRILQEEKEIDSATPEAPPK
Protein: E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp1 (EC 2.3.2.27) (Meiotically up-regulated gene 140 protein) (RING finger protein 1) (RING-type E3 ubiquitin transferase rfp1) (O13826)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mediates ubiquitination and subsequent desumoylation/degradation of sumoylated proteins and proteins containing SUMO-like domains. Involved in maintaining genome stability where it acts in the cellular response to DNA damage. Has a role in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17762864, ECO:0000269|PubMed:17762865}.
Interaction partners:
- E3 ubiquitin-protein ligase complex slx8-rfp subunit slx8
- E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp2
- Ribosome biogenesis protein erb1
- ATP-dependent RNA helicase has1
- Cullin-4
- ATP-dependent RNA helicase dbp9
- Chromatin modification-related protein rik1
- GTPase grn1
- Ribosome production factor 2 homolog
- Brix domain-containing protein C1B9.03c
Sequence:
MQFNGSNGIDESSVIDLTRSPSPPVETSISSTNIIDLDAIPDDSFPSSPVLSPRRRRMNRRRNERSRNFPSNHLSYLEDMIYLGPQVSTRRSSSRRDLMGMIARTFPEFSSVNSLSPSLFQLIVNRMRFDAIHPEWTNGSDDEYFSNHFEESYDDFTSSLENIKQSYKPPGPPKSGFTRSFNNDTLMVCPRCQEPLGTSKSKEKSALWATKCGHVYCGSCAKVLKTSKRSQSKCLVNDCGRYLNTKNAMWELFY
Protein: Mas-related G-protein coupled receptor member B8 (Q7TN50)
Organism: Rattus norvegicus (Rat)
Function: Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDSSIPDPEADLIQLNGSYHTETSPCVIESRVMILLSIIIAFFGLAGNAMVLWLLAFRMRRNVFSVYILNLAGANFLFLCTHTAFSLEKIIVLFHSVHIHIPLLFYTLSTLAYLAGVSMVTAISAEYWLSGIWPYWYQGQRLKHTTTVICTGLWGLALLLSLLEGKSCGFLGSTYNQDVCWKLDFIIVAWLLVLFAVLSRSIQVLLVRIFCGSQRTPVTKLHVTIVLTALVLVICGFPFGIIFYLLYWTTEVYYIMPCNSFHETILLLSYINSCANPIICLLVGSIRHCRFQCGTLRLLLHRAMQDIPEEEGEELEEVVGERVQNSIP
Protein: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (MECDP-synthase) (MECPP-synthase) (MECPS) (EC 4.6.1.12) (P62617)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). Also converts 4-diphosphocytidyl-2-C-methyl-D-erythritol into 2-C-methyl-D-erythritol 3,4-cyclophosphate and CMP.
Interaction partners:
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- 1-deoxy-D-xylulose-5-phosphate synthase
- tRNA pseudouridine synthase D
- Farnesyl diphosphate synthase
- Isopentenyl-diphosphate Delta-isomerase
- tRNA
Sequence:
MRIGHGFDVHAFGGEGPIIIGGVRIPYEKGLLAHSDGDVALHALTDALLGAAALGDIGKLFPDTDPAFKGADSRELLREAWRRIQAKGYTLGNVDVTIIAQAPKMLPHIPQMRVFIAEDLGCHMDDVNVKATTTEKLGFTGRGEGIACEAVALLIKATK
Protein: Protein TUNICAMYCIN INDUCED 1 (Q84JN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of pollen surface morphology, probably by modulating the secretion of proteins and/or lipids during pollen development.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:20944397}.
Interaction partners:
- DnaJ protein ERDJ3A
- Uncharacterized protein
- Uncharacterized protein
- Hydroxyproline-rich glycoprotein family protein
- Proline-rich family protein
- Zinc knuckle
- Heat shock 70 kDa protein BIP3
- bZIP transcription factor 60
- Zinc finger
- Endoplasmic reticulum oxidoreductin-1
Sequence:
MGHRVLVYVGALFLILFTIFPSSSALISSPDANPPYPKAISDLKESIVKGLGFQSEEVKVSGFDIRDALVGHSVSYEFDLEIDNKVLPFKLLEDVNRWEYVDLPIFQVEQPSENGLVPMRNKKTSSDDVLPVLAPFQLSGPMELWIQDANNMRLSLPYDVDAGVLKKVILADGAVVTVKGARSVSLRHPIDLPLPLNQSSNEFASGLLSLAEQLRRASTDQESPVLSLRIVGPTSLASTSQSPDNKLKLKRLAPGLVELSSMSKDKRSLSTIGANAMTTVLTPREFTTMWPITSINGSNANLLGFEKLLTSVLGPKAQEKGSFKVLKAKVAAQTFMKIGFGIEKKLKEADVEGLSFPEWRTKPETMRMHFEVLAKVDGENVIPENVMRVDPIPLEDTIAQNVITGNVTMSKLPIIESPPSPFTL
Protein: T. brucei spp.-specific protein (Q38FB5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLSTVCGSGAATMNNGRQKKVDHSRGLDFYLPPPDDREYRRGRIQRLRDQITAWKDPSRPFSVSGPNSMLGTKEFKWLSTQRSCSSGRTANSCGAAAGGATGSKCGKAAPQQPDNVYFHDHIVFCVPSGKGQTESRGGADGMCYGVTTNKESMAECEQGLQQTHVGQRSVSTRSIGANSVGISRADGDKQGTMRSDYRSCATSPTPVATLQSIKAQSVDLASSVHEARMQCRQGDFPTPHSSQQQLFMRTMELPIDWGEYTRNSKGTTCASRGDQSVPKFDTIHSCGPDVSSVCFVNTFTGSNASSLGLEGRATGIKGESTLRSAATLHNNARRPLRLYSIQLKDFHPSRTSTITPGADAPRNGIRVKLKS
Protein: cAMP-dependent protein kinase catalytic subunit (EC 2.7.11.11) (P40376)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- Adenylate cyclase
- Ras-like protein 1
- Mitogen-activated protein kinase spm1
- Serine/threonine-protein kinase ppk18
- Serine/threonine-protein kinase cek1
- Glucose receptor protein git3
- Guanine nucleotide-binding protein subunit beta
- Lysophospholipase NTE1
- Guanine nucleotide-binding protein alpha-2 subunit
Sequence:
MDTTAVASKGSTNVGSSTDTLSTSASLHPSMNAGSVNEYSEQQRHGTNSFNGKPSVHDSVGSDASVSNGHNNHNESSLWTSGIPKALEEATKSKKPDSLVSTSTSGCASAHSVGYQNIDNLIPSPLPESASRSSSQSSHQRHSRDGRGELGSEHGERRSAMDGLRDRHIRKVRVSQLLDLQRRRIRPADHTTKDRYGIQDFNFLQTLGTGSFGRVHLVQSNHNRLYYAIKVLEKKKIVDMKQIEHTCDERYILSRVQHPFITILWGTFQDAKNLFMVMDFAEGGELFSLLRKCHRFPEKVAKFYAAEVILALDYLHHNQIVYRDLKPENLLLDRFGHLKIVDFGFAKRVSTSNCCTLCGTPDYLAPEIISLKPYNKAADWWSLGILIFEMLAGYPPFYSENPMKLYENILEGKVNYPSYFSPASIDLLSHLLQRDITCRYGNLKDGSMDIIMHPWFRDISWDKILTRKIEVPYVPPIQAGMGDSSQFDAYADVATDYGTSEDPEFTSIFKDF
Protein: Transcription factor 24 (TCF-24) (Q7RTU0)
Organism: Homo sapiens (Human)
Function: Putative transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MDRGRPAGSPLSASAEPAPLAAAIRDSRPGRTGPGPAGPGGGSRSGSGRPAAANAARERSRVQTLRHAFLELQRTLPSVPPDTKLSKLDVLLLATTYIAHLTRSLQDDAEAPADAGLGALRGDGYLHPVKKWPMRSRLYIGATGQFLKHSVSGEKTNHDNTPTDSQP
Protein: At2g16630 (Pollen Ole e 1 allergen and extensin family protein) (Q8RWG5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F28N24.16 protein
- Pollen-specific protein-like At4g18596
- AT1g27100/T7N9_16
- RING-type E3 ubiquitin transferase
- At5g45880
- Allergen, putative
- Cyclin-dependent protein kinase inhibitor SMR10
- Probable methyltransferase PMT4
- Allergen-like protein BRSn20
- At5g55620
Sequence:
MDPNHNNLLIFVAFFVLCLATNGVTGYATVTGSVFCDQCKDGERSLFDFPVSGIKISVTCADENGQVYMSREETTNWLGGYVMRFDGTPDLSNCYAQVSDNGVQQDPSSCSIASGPAQKLKLMFSFFGIETFAADALLAQPVQPSSFCPKPPTAPVMPPPQVPVMPPPQVPVKPHPKVPVISPDPPATLPPPKVPVISPDPPTTLPPPLVPVINLPPVTSPPQFKLPPLPQIPPMPFVEPSACSHQLWMKPEYRCYWRAIGPDTKVAVAFGLVAGRIYGTDMTVREALDGRGEAYKTLLREATTALLNSYNSLGFPYNSVAVITYTNLALLGNSEHDVLMTAIRFIKANSGTCRFTVCN
Protein: Apolipoprotein A-I (E3TE55)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Apolipoprotein A-I-1
- Apolipoprotein A-I-2
- Apolipoprotein Bb, tandem duplicate 1 isoform X1
- Apolipoprotein B-100
Sequence:
MKVVALALTLLLALGCHARTLQAEALDQVEHFKSAAAVYLSQVKDQAYKALENLDGGDYEQYKLKLTESLDNLQKYAESTSTSLKPYATQVVEGTQTVREYILKEMDDLHAKVEPHRAELRQAIEKHLEEYGERLIPIFRDYMADNQKELESLRQKLQPALEDLKAKVETNFEETKTKLAPIVEAVSGRLNERLQNLKDLANPVAEEYKEHVLKAVEDVKEKLVPHTAQLQGQIEPYVETLRAKFMSIYETVSQAIQA
Protein: HTH-type transcriptional regulator EbgR (Ebg operon repressor) (P06846)
Organism: Escherichia coli (strain K12)
Function: Repressor for beta galactosidase alpha and beta subunits (ebgA and ebgC). Binds lactose as an inducer.
Interaction partners:
- Evolved beta-galactosidase subunit alpha
- HTH-type transcriptional regulator IdnR
- Inner membrane transporter YgjI
- HTH-type transcriptional regulator GntR
- Maltose regulon regulatory protein MalI
- Evolved beta-galactosidase subunit beta
- Catabolite repressor/activator
Sequence:
MATLKDIAIEAGVSLATVSRVLNDDPTLNVKEETKHRILEIAEKLEYKTSSARKLQTGAVNQHHILAIYSYQQELEINDPYYLAIRHGIETQCEKLGIELTNCYEHSGLPDIKNVTGILIVGKPTPALRAAASALTDNICFIDFHEPGSGYDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIREVAFAEYGRLKQVVREEDIWRGGFSSSSGYELAKQMLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLVYEKARDGRALPLLVFVPSKLKLRGTTR
Protein: FBL protein (Q96BS4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
GGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKVKN
Protein: Paramyosin (Putative myosin heavy chain) (Q8LPK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Zinc finger CCCH domain-containing protein 64
- Cystatin/monellin superfamily protein
- Zinc finger CCCH domain-containing protein 17
- Protein CROWDED NUCLEI 3
- Protein CROWDED NUCLEI 2
- COP1-interactive protein 1
- Beta-adaptin-like protein B
- Subtilisin-like protease SBT1.8
- Protein CROWDED NUCLEI 1
- GDSL esterase/lipase At2g24560
Sequence:
MANGADEDAVLSDVESDEPAPVVLKDSPREEASDERITELIAELDREKKAREAAESSKSELQVSFNRLKALAVEAIKKRDESKRERDEALKEKENLTNELENVNKGKDEMSKKLDEALRSRDGLKAEIENSSHMLVSGIEKISGKVSSFKNFSNGGLPKSQKYTGLTSVAYGVIKRTNEIVEELVRQIDTTAKSRNEAREQMDQRNYEIAIEVSQLESAISNLRLEVAEKASIVDDLERGVSEKEKRIAELEKGNLEKVSLLEGEVVELKQLVDEYDGKLKTMELKMVAQRPLLMDQLNLVSRIHDQLYEVVRIVDGNSSEQSDLSESFFMPQETEMEENIRASLAGMESIFELTKVVSGKAQSLVEEKSHELKNLNETVGLLVKEKEHIGTLLRSALSKRVIGEQPSQKRELFQAAENGLRDGGTDSKFAKLLKDGKVQDSRSDNTHDHSKEDNEIYSLASTLENIVKASQLEIVELQHLLEASREETSSLRKQLDTQTKELNQRMRQIEELKEKERIANENVEGLMTDIAAAEEEITRWKVAAEQEAAAGGAVEQDFTSQLYVLKEELEEAKQAIIESEKKLKFKEETAAAAMGARDAAERSLRLADNRATKLRERIQELNRKVEELETHRDMNTSNRARYACWPWQLLGIDFVGSRRIESGQESANEMELAEPLL
Protein: Serine/threonine-protein kinase Nek1 (EC 2.7.11.1) (Never in mitosis A-related kinase 1) (NimA-related protein kinase 1) (P51954)
Organism: Mus musculus (Mouse)
Function: Phosphorylates serines and threonines, but also appears to possess tyrosine kinase activity. Involved in DNA damage checkpoint control and for proper DNA damage repair. In response to injury that includes DNA damage, NEK1 phosphorylates VDAC1 to limit mitochondrial cell death (By similarity). May be implicated in the control of meiosis. Involved in cilium assembly (By similarity).
Subcellular location: Nucleus {ECO:0000305|PubMed:16267153}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16267153}. Note=Associated with the pericentriolar material (By similarity). Localizes to centrosome during interphase and mitosis (PubMed:16267153). {ECO:0000250|UniProtKB:Q96PY6, ECO:0000269|PubMed:16267153}.
Interaction partners:
- Alsin
- Cytoplasmic dynein 2 heavy chain 1
- Kinesin-like protein KIF3A
- Coiled-coil-helix-coiled-coil-helix domain containing 10
- Protein fantom
Sequence:
MEKYVRLQKIGEGSFGKAVLVKSTEDGRHYVIKEINISRMSDKERQESRREVAVLANMKHPNIVQYKESFEENGSLYIVMDYCEGGDLFKRINAQKGALFQEDQILDWFVQICLALKHVHDRKILHRDIKSQNIFLTKDGTVQLGDFGIARVLNSTVELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYELCTLKHAFEAGNMKNLVLKIISGSFPPVSPHYSYDLRSLLSQLFKRNPRDRPSVNSILEKGFIAKRIEKFLSPQLIAEEFCLKTLSKFGPQPLPGKRPASGQGVSSFVPAQKITKPAAKYGVPLTYKKYGDKKLLEKKPPPKHKQAHQIPVKKMNSGEERKKMSEEAAKKRRLEFIEKEKKQKDQIRFLKAEQMKRQEKQRLERINRAREQGWRNVLRAGGSGEVKASFFGIGGAVSPSPCSPRGQYEHYHAIFDQMQRLRAEDNEARWKGGIYGRWLPERQKGHLAVERANQVEEFLQRKREAMQNKARAEGHVVYLARLRQIRLQNFNERQQIKAKLRGENKEADGTKGQEATEETDMRLKKMESLKAQTNARAAVLKEQLERKRKEAYEREKKVWEEHLVARVKSSDVPLPLELLETGGSPSKQQVKPVISVTSALKEVGLDGSLTDTQEEEMEKSNSAISSKREILRRLNENLKAQEDEKEKQHHSGSCETVGHKDEREYETENAISSDRKKWEMGGQLVIPLDAVTLDTSFSATEKHTVGEVIKLDSNGSPRKVWGKNPTDSVLKILGEAELQLQTELLENTSFKSEVYAEEENYKPLLTEEENLQCISKEINPSATVDSTETKSPKFTEVSPQMSEGNVEEPDDLETEVLQEPSSTHTDGSLPPVLNDVWTREKEAAKETELEDKVAVQQSEVCEDRIPGNVDQSCKDQRDPAVDDSPQSGCDVEKSVQPESIFQKVVHSKDLNLVQAVHCSPEEPIPIRSHSDSPPKTKSKNSLLIGLSTGLFDANNPKMLRTCSLPDLSKLFRTLMDVPTVGDVHQDSLEIDELEDEPIKEGPSDSEDTVFEETDTDLQELQASMEQLLREQPGDEYSEEEESVLKSSDVEQTARGTDAPDEEDNPSSESALNEEWHSDNSDAETTSECEYDSVFNHLEELRLHLEQEMGFEKFFEVYEKVKAIHEDEDENIEICSTIVENILGNEHQHLYAKILHLVMADGAYQEDNDE
Protein: PMS1 homolog 1, mismatch repair system component (D4A651)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- DNA mismatch repair protein Msh2
- DNA mismatch repair protein
- DNA mismatch repair protein Mlh1
- DNA mismatch repair protein
- Mismatch repair endonuclease PMS2
- MutS protein homolog 4
- MutL homolog 3
- MutS protein homolog 5
- Exonuclease 1
- DNA polymerase delta catalytic subunit
Sequence:
MKQLPAATVRLLSSSQTITSVVSVVKELIENSLDAGANSIDVKLENYGFDKIEIRDNGAGIKAVDVPVMAVKYYTSKISSHEDLQTLTTYGFRGEALGAICNVAEVVVTTRTAADDFSTQYVLDGSGHILSQKPSHLGQGTTVTVLKLFKNLPVRRQFYSTPKKCKDELKNVQDLLISYAVLKPDLRITFVHNKAVIWQKSRVPDHRMALMSVLGTAVMGNMESVERYCEDSQIHLRGLFPKHDADHNSTSLSTPERSFIFINSRPVHQKDILKLIRHYYNLKCLKESTRLYPIFFLKIDVPSAEVDINLTPDKSQVLLQNKESVLIALENLLMTCYGPLPTTESYENNRVDVSSANVVISETTETDVLFNKMESSGNKYPNADTLAIPFQNDESRKNTDHHLNEQINIGHCDGHFSGEYSHINKDTFQNIPRNNLSSEANQSKHSETHSAGSIEHIQGENGRSGTGENGEDGKKTLPEKALEICVDDWSKGNVFNSMGENIEPVKILVPQKSLSCKVTNSHPNPEPENLSVGPGSRTSNVIDNRPGQLTAYDLISSRAVKKPMSACALFIQDHRTQFLAENPKTGLEDVTAQIKAQWETLSEEEKHKYEEKAKKDLERYNNQMKKAIEQEAQVSLKDGRKKLRATGAWGCTQRHKVKDLSNQPKLDELFQSQNEKKSENIKITKIPFSMENLKVNFNKQKEVDLEEKDEICLIHSLKFPDAWLVTSRADVMLLNPYRVEEALLFKRLLENHKFLAEPLEKPIVLTESLFNGSDYLEVLHKMSTVEERCRGSVYLCDPRLTANGFKIRLTPGVSSAENYLEIEGMAKCLPFYGVMDLKEILNAIVNKNAKEIYECRPRKVINYLEGEAVRLSRQLPMYLPQEDVQDLIYKMKHQFGKEIKGCVHGRPFLHHLIHLPGTS
Protein: Trypsin-5 (EC 3.4.21.4) (Testicular-specific serine protease 4) (Trypsinogen 9) (T9) (Q9QUK9)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:10506205}.
Interaction partners:
- Carboxypeptidase A1
- Carboxypeptidase B
- Chymotrypsin-like elastase family member 2A
- Anionic trypsin-2
- Chymotrypsinogen B
- Pancreatic triacylglycerol lipase
- Chymotrypsin-like elastase family member 3B
- Bile salt-activated lipase
- Pancreatic alpha-amylase 2a5
- Chymopasin
Sequence:
MNSLLFLALVGAAVAFPVDDDDKIVGGYTCRENSIPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKTRIQVRLGEHNINVLEGNEQFVNSAKIIKHPNFNSRTLNNDIMLIKLASPVTLNARVATVALPSSCAPAGTQCLISGWGNTLSFGVNNPDLLQCLDAPLLPQADCEASYPGKITNNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCALKDNPGVYTKVCNYVDWIQDTIAAN
Protein: Protein translocase subunit SecA (EC 7.4.2.8) (Q7WUF6)
Organism: Streptococcus parasanguinis
Subcellular location: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01382}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01382}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Note=Distribution is 50-50. {ECO:0000256|HAMAP-Rule:MF_01382}.
Interaction partners:
Sequence:
MEKIKQKRSFINTMKLRRLRKKLVKINALKETMSLLSDEELKQKTVEFRNRLHEGETLEDILIEAFAAIREADRRILGMFPFDVQVLGALALHEGTIVEMKTGEGKTLTATLPLYLNALEGKGTILVTTNDYLARRDAIDMGEVYRFMGLTVGVGVFDDDEEVDSNRKKKIYSSDILYTTSTALGFDYLIDNLAGNVEDKFLRSFNYVIVDEADAVLLDSAQTPLIIAGSPRVQSNLYDTADQFIRTLKKDQEFKFLKDEKFIFLTDEGIRYAEKYFNIPNLYSEEYFELNRHINLALRAHYLFKKDMDYVVTDDAVELLDNRTGRILEGTRLQSGIHQAIETKEKVKKSKDSRAIASVTYQSLFNMFPKLSGMTGTGKIAENELISTYGVSVVVLPTNTPIQRLDYSDKIYTTLPEKLLATLEFVKELHEKQQPILLISGTVDIAEIYSRMLLQEGIPHNVLTAKNIAKEALIIAEAGQKGAVTVATSLAGRGTDIKLGKGVAELGGLAVIGTERMPNSRIDWQLRGRAGRQGDPGLSQFFVSLEDDLIMNHANRRLKKYFEKQNSIDRKNYGKPLFSKRFSRIVTHAQQKSEDKSESARQNTIKFDESLKSQRKKIYHLRDQLIFGEVKLRDRLDKLISEYIEMYMENNRKFGLNQNDFKRFILENFTYQLRSLPKSLDLSNSRQVKDYLFYLYQLEMERKSKQLKTDSKVEEFIRLSILRAIDECWIQQVDHLQQLKTFVSMRQIAQRDSFNEYLRESLESYEEMSREVKHAIVKNVMLSTIEGKVDDGLSIYFV
Protein: p53-induced death domain-containing protein 1 (EC 3.4.21.-) (Leucine-rich repeat and death domain-containing protein) [Cleaved into: PIDD-N; PIDD-C; PIDD-CC] (Q9HB75)
Organism: Homo sapiens (Human)
Function: Component of the DNA damage/stress response pathway that functions downstream of p53/TP53 and can either promote cell survival or apoptosis. Associated with CRADD and the CASP2 caspase, it forms the PIDDosome a complex that activates CASP2 and triggers apoptosis. Associated with IKBKG and RIPK1, it enhances sumoylation and ubiquitination of IKBKG which is important for activation of the transcription factor NF-kappa-B.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16360037, ECO:0000269|PubMed:17159900, ECO:0000269|PubMed:39532532}. Nucleus {ECO:0000269|PubMed:16360037, ECO:0000269|PubMed:17159900}. Note=Enriched in the nucleus upon DNA damage. {ECO:0000269|PubMed:17159900}.
Interaction partners:
- Death domain-containing protein CRADD
- Caspase-2
- Cellular tumor antigen p53
- BH3-interacting domain death agonist
- Receptor-interacting serine/threonine-protein kinase 1
- FAS-associated death domain protein
- Serine-protein kinase ATM
- NF-kappa-B essential modulator
- Tumor necrosis factor receptor superfamily member 10B
- DNA-dependent protein kinase catalytic subunit
Sequence:
MAATVEGPELEAAAAAGDASEDSDAGSRALPFLGGNRLSLDLYPGGCQQLLHLCVQQPLQLLQVEFLRLSTHEDPQLLEATLAQLPQSLSCLRSLVLKGGQRRDTLGACLRGALTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLGEASPDAPSSPVAALIPEMPRLFLTSDLDSFPVTPQGCSVTLACGVRLQFPAGATATPITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFTPPQARRCREVVVRTRNDNSWGDLETYLEEEAPQRLWAHCQVPHFSWFLVVSRPVSNACLVPPEGTLLCSSGHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGPPSFLQPVTVQLPLPSGITGLSLDRSRLHLLYWAPPAATWDDITAQVVLELTHLYARFQVTHFSWYWLWYTTKNCVGGLARKAWERLRLHRVNLIALQRRRDPEQVLLQCLPRNKVDATLRRLLERYRGPEPSDTVEMFEGEEFFAAFERGIDVDADRPDCVEGRICFVFYSHLKNVKEVYVTTTLDREAQAVRGQVSFYRGAVPVRVPEEAEAARQRKGADALWMATLPIKLPRLRGSEGPRRGAGLSLAPLNLGDAETGFLTQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAEEVRAVLELGRRKYQDSIRRMGLAPKDPALPGSSAPQPPEPAQA
Protein: Prohead protease (EC 3.4.21.-) (Q6QGD7)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Serine protease involved in capsid assembly and maturation. Cleaves the major capsid protein, the decoration protein, the portal protein to yield mature procapsids competent for DNA packaging (Probable). Acts as a trigger for assembly of the capsid protein.
Subcellular location: Virion {ECO:0000269|PubMed:24198424}. Note=Present in the prohead I. {ECO:0000269|PubMed:24198424}.
Interaction partners:
Sequence:
MTQAAIDYNKLKSAPVHLDAYIKSIDSESKEGVVKIRGFANTISKDRAGDVIPASAWKTSNALTNYMKNPIILFGHDHRRPIGKCIDLNPTEMGLEIECEINESSDPAIFSLIKNGVLKTFSIGFRCLDAEWDEATDIFIIKDLELYEVSVVSVPCNQDSTFNLAKSMNGHDYTEWRKSFTAISSKAVPAQERNLSELEKLAIALGYVKE
Protein: Dynein, 70 kDa intermediate chain, flagellar outer arm (IC69) (IC70) (P27766)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: May play a role in regulating dynein heavy chain (DHC) activity. May function in holding IC78 to the DHC, or in stabilizing the entire dynein complex.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme.
Interaction partners:
Sequence:
MEIYHQYIKLRKQFGRFPKFGDEGSEMLADIRPNEDHGKEYIPRNPVTTVTQCVPEMSEHEANTNAVILVNKAMSHVEGGWPKDVDYTEAEHTIRYRKKVEKDEDYIRTVVQLGSSVEDLIKQNNAVDIYQEYFTNVTMDHTSEAPHVKTVTVFKDPNNIKRSASYVNWHPDGSVPKVVVAYSILQFQQQPAGMPLSSYIWDVNNPNTPEYEMVPTSQICCAKFNLKDNNLVGAGQYNGQLAYFDVRKGNGPVEATPIDISHRDPIYDFAWLQSKTGTECMTVSTDGNVLWWDLRKMNECVENMPLKEKNSETTVGGVCLEYDTNAGPTNFMVGTEQGQIFSCNRKAKNPVDRVKYVLSGHHGPIYGLRRNPFNSKYFLSIGDWTARVWVEDTAVKTPILTTKYHPTYLTGGTWSPSRPGVFFTIKMDGAMDVWDLYYKHNEPTLTVQVSDLALTAFAVQESGGTVAVGTSDGCTSVLQLSTGLSEASPAEKANINAMFERETTREKNLEKAIKEAKVKARKEQGRRDEVKDNVTEEQLKALEDEFFKTTDPAVGGGYGAGEGAAAE
Protein: 40S ribosomal proteins S11, putative (Q38CI4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 40S ribosomal protein S18, putative
- 40S ribosomal protein S8
- 40S ribosomal protein S16, putative
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S26
- Ribosomal protein S19, putative
- 40S ribosomal protein S10, putative
- 40S ribosomal protein S15a, putative
- 40S ribosomal protein S25
- 40S ribosomal protein S13, putative
Sequence:
MTSKQENYARTPTVDLTVQHEKAYQRQTAVNENIRTASKKHVNRSGHIRYSKKIGLGFATPKAAINGKYIDRKCPFTSNVSIRGRILRGVVHSTKMRRSIVIRRNYLHFIRKYQRYQKRHRNITVHCSPCFDPKPGDEVVVGQCRPLSKTIRYNVLQVVSKSAADKMGKKFSKN