wanglab/gogpt-training-data huggingface dataset:
Protein: DNA repair protein (D4A5N4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR005856}. Cytoplasm {ECO:0000256|PIRNR:PIRNR005856}.
Interaction partners:
- DNA repair protein RAD51 homolog 3
- DNA repair protein
- X-ray repair cross complementing 2
- RAD51 paralog B
- DNA repair protein RAD51 homolog
- Breast cancer type 2 susceptibility protein homolog
- DNA repair protein RAD52 homolog
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- RecQ-like DNA helicase BLM
- Structure-specific endonuclease subunit MUS81
Sequence:
MDLDQLDLNPRITAAIKRGRLKSVKEVLCYSGPDLQRLTSLPSHDVQLLLRAAALHLRGSRVLTALHLFQQRESFPEQHQRLSLGCPVLDQFLGGGLPLEGITGLAGRSSAGKTQLALQLCLAVQFPRQYGGLEAGAVYICTEDAFPSKRLWQLIEQLQELRTDVPGEVTQKIRFGNHIFIEHAADVDTLMECVSKRVPILLSRGMARLVVVDSIAAPFRCEFHLQASAVRAKHLHSLGAALQRLSSTFRSPVLCINQVTEMVEDQESAGAWEERLSPALGITWANQLLMQLMVDRIHEDSVTTGLPRSPARTLRVLFAPHLPLSSCCYTVSGEGVRGMAGTESC
Protein: alpha-mannosidase (EC 3.2.1.24) (C8VJ45)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- ZZ type zinc finger domain protein
Sequence:
MGGDVLRQTPSSLPRAPDGPVGQRIRSIYTDRLNQFTSRGQYQNQNLIGKLFEATNSDEDHVKISVYSVPDLQRPSFEEATSNEFQPTHIGASFGPSWSTHWFRIRLTIPEDMRERERLEFHWDANNEGLVWTEDGHPLQGLTGGGERIEWIIPDAWRDGNEHVFYIEMACNGMFGNAPGGDSIQPPAPDKYYTLTTARITAVNLEARALFYDFWIISDAAREFPAEGWESHEANMVANSIIDAFIAGNGSLESIKEGRRIAQKYLGDKVDCSEVYDSGTQPIVYGIGHCHIDTCWLWPWAETKRKVARSWSNQCDLMDRYPEHRFTCSQAQQFKWLKQYYPSVFDRVKGWVKKGHFQPIGGSWVEHDTNMPSGESLVRQFIYGQRFFESNFGERCTTFWLPDTFGYSTQIPQLCRLAGMSRFFTQKLSWNNINNFPHTTFQWVALDGSQVMCHMPPSETYTAEAHFGDLKRSITQHKSLDKDNTSLLVFGKGDGGGGPTFEHLEKLRRCRGLSDKTGLLPRATMGTSVDDFFAKLEKKAADGTKFATWYGELYFELHRGTYTTQANNKRNNRRAEFLLRELEFLATIASITRSDYEYPKKDIDEMWEGVLLCQFHDCLPGSSIEMCYDDSDELYAQIFETGLRAREAALEALGFSMAGRVPVAINTLPWNRSEVVRLPADMATNGSMHALLNGGPGVIPHSQAIARVPEVSVTEIKPGVFRLNNGKLRVDVEDGLITSLYDIEADREVIAADGRAGQLVIFDDKPLYWQAWDVEVFHLDSRKELQSGKTTIAENDPYRVSVVTETKISEKSWVKTTISLAATEGNRPSYVELESEVEWQETMKFLKVEFPVDITNTEASYETQYGIIRRPTHYNTSWDMAKFEVCAHKWADLSENGYGVSILNDSKYGFATCGNLMRLSLLRAPKAPDAHADMGRHTIRYAIFPHSGPLDFRTVRAGYEFNHPLILDTSLALPDEQSVFAVSALFRKIELTGSPSLILDVVKRGEDDEDIDGDPDISLPSSKRSGQSIILRIYESLGGKSRGAIRTALPVEKVWKCNVLEDDEVVIDLVDERHGWKKVDIELRAFEVATYRLQL
Protein: Terpene synthase 7 (EC 4.2.3.-) (Q54YE1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpene beta-barbatene.
Interaction partners:
Sequence:
MYSIYDFKYPSDWIEPTADDKCIYDCYKEVINYKLLDENKQTFQYYYGTLSSTINFYPLCNYEQLVIACRFLTVGYLIDDFLESNLVDSETSNLMSKKIENILIDGEYLDQSNISNIEKYTMFFRGKARQFVGDKINIFNQFIKFFVEWINSINPFNKAINLNNYDSYNFFKKVNSGTYVTLSMAMLLNPNTKVDTNIWMNPRFERFVCNGAYQMSAFNDCASYAKEVRSNCHLTNPLYFLQKEIGSFDQVYKLILNFNNKIVNEICKDEELLLKECPDDQKDDLKYLTRSMKLILGGNYSWSLKCTRFNDIDSPFIEQRSINPDVIAYENIVDKIIKL
Protein: Cytochrome c oxidase assembly protein COX11, mitochondrial (Q6P8I6)
Organism: Mus musculus (Mouse)
Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9Y6N1}; Single-pass membrane protein {ECO:0000255}; Intermembrane side {ECO:0000250|UniProtKB:Q9Y6N1}.
Interaction partners:
- Protoheme IX farnesyltransferase, mitochondrial
- Surfeit locus protein 1
- Cytochrome c oxidase copper chaperone
- Protein SCO2 homolog
- Heme A synthase COX15
- Cytochrome c oxidase subunit 2
- Large ribosomal subunit protein uL24
- Cytochrome c oxidase subunit 3
- Replication factor C subunit 3
- Cytochrome c oxidase assembly protein COX19
Sequence:
MGGLWCPGWRLVASCGRGWRQPGWSGRTVVNAELVLRPGWDGLGGAERGLRRLGTWKRPCGVRGPATQPPRRPRSSNPFQRAQEDEWRRRNKTVLTYVAAAAVGMLGASYAAVPLYRLYCQTTGLGGSAVAGHSSDQIENMVPVKDRVIKVTFNADVHASLQWNFRPQQTEIYVVPGETALAFYKAKNPTDKPVIGISTYNVVPFEAGQYFNKIQCFCFEEQRLNPQEEVDMPVFFYIDPEFAEDPRMVNVDLITLSYTFFEAKEGHKLPVPGYN
Protein: T-complex protein 1 subunit eta (TCP-1-eta) (CCT-eta) (P80313)
Organism: Mus musculus (Mouse)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:7953530}.
Interaction partners:
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit zeta-2
- Chaperonin containing TCP1 subunit 8-like 1
- Cell division cycle protein 20 homolog
Sequence:
MMPTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQRKMLEKCAMTALSSKLISQQKVFFAKMVVDAVMMLDELLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFEMQPKKYKNPKIALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHQSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALVPDVLGHCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINNENIADNFQAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRSTVDPPAPSAGRGRGQARFH
Protein: Phospholipid scramblase 1 (PL scramblase 1) (Ca(2+)-dependent phospholipid scramblase 1) (Mg(2+)-dependent nuclease) (EC 3.1.-.-) (P58195)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific distribution of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface (By similarity). Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (By similarity). Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A (By similarity). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages (By similarity). May contribute to cytokine-regulated cell proliferation and differentiation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O15162}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O15162}. Cell membrane {ECO:0000250|UniProtKB:O15162}; Lipid-anchor {ECO:0000250|UniProtKB:O15162}; Cytoplasmic side. Nucleus {ECO:0000250|UniProtKB:O15162}. Cytoplasm {ECO:0000250|UniProtKB:O15162}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O15162}. Note=Localizes to the perinuclear region in the presence of RELT. Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus. {ECO:0000250|UniProtKB:O15162}.
Interaction partners:
Sequence:
MEKHGPPEHAAYPIPQADYQGSQGPYPGPQGPYPGPQGPYAGPQGPYPGPQGPYAGPQGPYPGPQPGYPVPPGSYAGGDPSGFPVQHQPAYNHPGGPGGTPWMQAPPPPLDCPPGLEYLTQIDQILVHQQIELLEVLTGFETNNKYEIKNSLGQRVYFAVEDTDCCTRNCCGASRPFTLRILDNMGREVMTLERPLRCSSCCFPCCLQEIEIQAPPGVPVGYVIQTWHPCLPKFTLQNEKRQDVLKVVGPCVVCSCCSDIDFELKSLDEESVVGKISKQWSGFVREAFTDADNFGIQFPLDLDVKMKAVMLGACFLIDFMFFERTGNEEQRSGVW
Protein: Calcium-transporting ATPase type 2C member 2 (ATPase 2C2) (EC 7.2.2.10) (Ca(2+)/Mn(2+)-ATPase 2C2) (Secretory pathway Ca(2+)-transporting ATPase type 2) (SPCA2) (O75185)
Organism: Homo sapiens (Human)
Function: ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway. Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to the lumenal side. The transfer of ions across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state. Induces Ca(2+) influx independently of its ATP-driven pump function. At the basolateral membrane of mammary epithelial cells, interacts with Ca(2+) channel ORAI1 and mediates Ca(2+) entry independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May facilitate transepithelial transport of large quantities of Ca(2+) for milk secretion via activation of Ca(2+) influx channels at the plasma membrane and active Ca(2+) transport at the Golgi apparatus.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15831496}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:20887894}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:A7L9Z8}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- C-Maf-inducing protein
- Calcium release-activated calcium channel protein 1
- Coagulation factor VII
- Dynein axonemal assembly factor 4
- Doublecortin domain-containing protein 2
- Dyslexia-associated protein KIAA0319
Sequence:
MVEGRVSEFLKKLGFSGGGRQYQALEKDEEEALIDEQSELKAIEKEKKVTALPPKEACKCQKEDLARAFCVDLHTGLSEFSVTQRRLAHGWNEFVADNSEPVWKKYLDQFKNPLILLLLGSALVSVLTKEYEDAVSIATAVLVVVTVAFIQEYRSEKSLEELTKLVPPECNCLREGKLQHLLARELVPGDVVSLSIGDRIPADIRLTEVTDLLVDESSFTGEAEPCSKTDSPLTGGGDLTTLSNIVFMGTLVQYGRGQGVVIGTGESSQFGEVFKMMQAEETPKTPLQKSMDRLGKQLTLFSFGIIGLIMLIGWSQGKQLLSMFTIGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCSVLCSDKTGTLTANEMTVTQLVTSDGLRAEVSGVGYDGQGTVCLLPSKEVIKEFSNVSVGKLVEAGCVANNAVIRKNAVMGQPTEGALMALAMKMDLSDIKNSYIRKKEIPFSSEQKWMAVKCSLKTEDQEDIYFMKGALEEVIRYCTMYNNGGIPLPLTPQQRSFCLQEEKRMGSLGLRVLALASGPELGRLTFLGLVGIIDPPRVGVKEAVQVLSESGVSVKMITGDALETALAIGRNIGLCNGKLQAMSGEEVDSVEKGELADRVGKVSVFFRTSPKHKLKIIKALQESGAIVAMTGDGVNDAVALKSADIGIAMGQTGTDVSKEAANMILVDDDFSAIMNAVEEGKGIFYNIKNFVRFQLSTSISALSLITLSTVFNLPSPLNAMQILWINIIMDGPPAQSLGVEPVDKDAFRQPPRSVRDTILSRALILKILMSAAIIISGTLFIFWKEMPEDRASTPRTTTMTFTCFVFFDLFNALTCRSQTKLIFEIGFLRNHMFLYSVLGSILGQLAVIYIPPLQRVFQTENLGALDLLFLTGLASSVFILSELLKLCEKYCCSPKRVQMHPEDV
Protein: Ras-related protein Rab-8B (EC 3.6.5.2) (Q92930)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may be involved in polarized vesicular trafficking and neurotransmitter release. May participate in cell junction dynamics in Sertoli cells (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:21255211}; Lipid-anchor {ECO:0000269|PubMed:21255211}; Cytoplasmic side {ECO:0000269|PubMed:21255211}. Endosome membrane {ECO:0000269|PubMed:32344433}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis. Colocalized with MICAL1, GRAF1/ARHGAP26 and GRAF2/ARHGAP10 on endosomal tubules (PubMed:32344433). {ECO:0000269|PubMed:32344433}.
Interaction partners:
- Ras-related protein Rab-8A
- MICAL-like protein 2
- PEX5-related protein
- Rab GDP dissociation inhibitor beta
- Rab GDP dissociation inhibitor alpha
- Otoferlin
- Ras-related protein Rab-1B
- Rab-3A-interacting protein
- Guanine nucleotide exchange factor for Rab-3A
- Guanine nucleotide exchange factor MSS4
Sequence:
MAKTYDYLFKLLLIGDSGVGKTCLLFRFSEDAFNTTFISTIGIDFKIRTIELDGKKIKLQIWDTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIKNWIRNIEEHASSDVERMILGNKCDMNDKRQVSKERGEKLAIDYGIKFLETSAKSSANVEEAFFTLARDIMTKLNRKMNDSNSAGAGGPVKITENRSKKTSFFRCSLL
Protein: Small nuclear ribonucleoprotein polypeptide B2 (B5DEQ4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Small nuclear ribonucleoprotein polypeptide A'
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein-associated protein N
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D2
- Splicing factor 3A subunit 2
- Small nuclear ribonucleoprotein Sm D3
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 3
Sequence:
MDIRPNHTIYINNMNDKIKKEELKRSLYALFSQFGHVVDIVALKTMKMRGQAFVIFKELGSSTNALRQLQGFPFYGKPMRIQYAKTDSDIISKMRGTFADKEKKKEKKKAKTMEQAAAAANKKPGQGTPNSANTQGNAAPNPQVPDYPPNYILFLNNLPEETNEMMLSMLFNQFPGFKEVRLVPGRHDIAFVEFENDGQAGAARDALQGFKITPSHAMKITYAKK
Protein: Large ribosomal subunit protein mL44 (Q9VNC1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein uL13m
- Small ribosomal subunit protein uS2m
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL49
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL22m
Sequence:
MSFLRSAVGLLARVKLLEGSPTVQTRRHIKRWVSPTLRELAHRQKKLGPQKPERRSGFVEWNQRSELFAFGKRLGESFELSELQRAFTEKSFAEREEDRRRQLGIEESDLQMPHNSDLVEKGQQIARAYVEAFLQHQLPKVPNEGLQAIASYLLSTETLAHVSTHLGTKDLIQSTEYPPSAESQAKSLHAVIGALASSSGIERAFIFVRDFICTQLNQKDLLEVWTPQEPIQLLEKICQERKLGEAEPRLLGDCGKNTVLAAYQVGIYANRQLLGKGFGEDVKTATETAALDALQSIFDTRDNRRPFDFAIQLEPKTVRLG
Protein: Rap guanine nucleotide exchange factor 5 (Guanine nucleotide exchange factor for Rap1) (M-Ras-regulated Rap GEF) (MR-GEF) (Related to Epac) (Repac) (Q92565)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) for RAP1A, RAP2A and MRAS/M-Ras-GTP. Its association with MRAS inhibits Rap1 activation.
Subcellular location: Nucleus.
Interaction partners:
- Ras-related protein Rap-1A
- Ras-related protein M-Ras
- Ras-related protein Rap-1b
- GTPase HRas
- Ras-related protein R-Ras
- Ras-related protein R-Ras2
- GTPase NRas
- GTPase KRas
- GDP-fucose transporter 1
Sequence:
MGSSRLRVFDPHLERKDSAAALSDRELPLPTFDVPYFKYIDEEDEDDEWSSRSQSSTEDDSVDSLLSDRYVVVSGTPEKILEHLLNDLHLEEVQDKETETLLDDFLLTYTVFMTTDDLCQALLRHYSAKKYQGKEENSDVPRRKRKVLHLVSQWIALYKDWLPEDEHSKMFLKTIYRNVLDDVYEYPILEKELKEFQKILGMHRRHTVDEYSPQKKNKALFHQFSLKENWLQHRGTVTETEEIFCHVYITEHSYVSVKAKVSSIAQEILKVVAEKIQYAEEDLALVAITFSGEKHELQPNDLVISKSLEASGRIYVYRKDLADTLNPFAENEESQQRSMRILGMNTWDLALELMNFDWSLFNSIHEQELIYFTFSRQGSGEHTANLSLLLQRCNEVQLWVATEILLCSQLGKRVQLVKKFIKIAAHCKAQRNLNSFFAIVMGLNTASVSRLSQTWEKIPGKFKKLFSELESLTDPSLNHKAYRDAFKKMKPPKIPFMPLLLKDVTFIHEGNKTFLDNLVNFEKLHMIADTVRTLRHCRTNQFGDLSPKEHQELKSYVNHLYVIDSQQALFELSHRIEPRV
Protein: FI07666p (MIP26861p) (Q9VD00)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLGNLCRLVGARSPITRRLLHTERKVRVNGSDLNIVESGSGERSLLLMPGALGSSWTDFRPQIEQLPKLLPGHTIIAWDPPGYGKSVPPQRKFGLEFFREDAQAAVDLMRALDRPRFSILGWSDGGITALIVAGRHAEAVDRLAIWGAGAYLNADEVKALKNIRDVAKWSPRMREPMEKVYGVERFPQLWAEWVDAACAFYDQRDGDFCRTEVEKIKIPTFILHGKKDPMIAAEHIPWLRERLPHAEYYEFPEGKHNIHLRYAEEFNKLVADFFNKNN
Protein: Tubulin gamma chain (Gamma-tubulin) (P25295)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000305}.
Interaction partners:
- Spindle pole body component alp4
- Spindle pole body component alp6
- Mitotic-spindle organizing protein 1
- Gamma-tubulin complex component gfh1
- Spindle pole body component alp16
- Gamma-tubulin complex subunit mod21
- Phosphatidylglycerol phospholipase C
- DASH complex subunit ask1
- Inositol phosphosphingolipids phospholipase C
- Myosin type-2 heavy chain 2
Sequence:
MGREIITLQAGQCGNQIGSQFWQQLCLEHGIGPDGTLESFATEGVDRKDVFFYQSDDTRYIPRAILIDLEPRVVNNILSDTYGSLYNPENILITKNGGGAGNNWANGYSHAERIFEDIMDMIDREADGSDSLEGFSLLHSIAGGTGSGLGSFLLERLNDRYPKKIIQTYSVFPNSQSVSDVVVQPYNSLLALKRLTLNADSVVVLDNAALAHIAADRLHTQNPTFHQQNQLVSTVMSASTTTLRYPGYMNNDLVSIIASLIPSPRCHFLLTSYTPFTNQQVEEAKAIRKTTVLDVMRRLLLPKNQMVSVNPSKKSCFISILDIIQGEADPADVHKSLLRIRERRYASFIPWGPASIQVALSKKSPYIKTNHRVSGLMLANHTSIASLFKRTLDQYDRLRKRNAFLEQYKKEAIFEDDLNEFDSSRDVVADLINEYEACEDPNYLSL
Protein: Uncharacterized protein (Q383D9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQTSPVRLGALIRYVSFRHAPKFRQPRPEEVIGLPVKETPPHCVPAFVLPDFINEAEERALLALTEPWFSRLPCNEGHMDALIHHYKEFYRSYKGLMEGEGACGSCEDGCRHVRRALERCWSAASGYVPATPLDDRVHFLRLSECGFIRAHADDTRNSSGIIAGLCLGSARVMTLTHPDHAGQRVELMLAPRAFYVLMGAARYKWEHSVDWIRDDDEHIERVRGRVPPGERSLVFDGKETEFRRGERTAIIFRGVSPLELLKHKTLERKGHT
Protein: Uncharacterized protein C1F12.05 (Q10347)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MPSLVRRFQHASTEEQPFELNIQMESPPLVMYGNPDVSSGALASGLAKLTVFPADLKCESIVMEFVRIISTKRPLRDSCPDCKAQVEAFEKWEFSKEPTVYTHGTHTWPFTFIIPGHFPQTTNSPFINVTYILKTRVKIPSQPDFVFEYPLNLKRSIVTNADKIAQRLFPPTSLIALLELPPVIHPLSCVPVEFQLTGVKPENSKVGWRLTKISWRIEEQIKAQINGCSTHTGTKKPYIFKETRLLGNNEHKSGWKEDGDRIIFEIPISTSLLSKPICDVSFDGQFSLYIAHQLILETIVVEVMNSHPINSNARILRMKVNLPLTERGGLGVSWDEECPPMFNSVGPSPPAYEQVARSSPTDIPLPPPSCPTNVQRD
Protein: Zinc metalloprotease ZmpB (EC 3.4.24.-) (Q9L7Q2)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Is a virulence factor capable of inducing inflammation in the lower respiratory tract, by increasing tumor necrosis factor alpha (TNF-alpha) concentration in the lungs. Also appears to have other functions important in virulence in models of pneumonia and septicemia.
Subcellular location: Secreted, cell wall. Membrane; Multi-pass membrane protein. Secreted, cell wall; Peptidoglycan-anchor.
Interaction partners:
Sequence:
MFKKDRFSIRKIKGVVGSVFLGSLLMAPSVVDAATYHYVNKEIISQEAKDLIQTGKPDRNEVVYGLVYQKDQLPQTGTEASVLTAFGLLTVGSLLLIYKRKKIASVFLVGAMGLVVLPSAGAVDPVATLALASREGVVEMEGYRYVGYLSGDILKTLGLDTVLEETSAKPGEVTVVEVETPQSITNQEQARTENQVVETEEAPKEEAPKTEESPKEEPKSEVKPTDDTLPKVEEGKEDSAEPAPVEEVGGEVESKPEEKVAVKPESQPSDKPAEESKVEQAGEPVAPREDEKAPVEPEKQPEAPEEEKAVEETPKQEESTPDTKAEETVEPKEETVNQSIEQPKVETPAVEKQTEPTEEPKVEQAGEPVAPREDEQAPTAPVEPEKQPEVPEEEKAVEETPKPEDKIKGIGTKEPVDKSELNNQIDKASSVSPTDYSTASYNALGPVLETAKGVYASEPVKQPEVNSETNKLKTAIDALNVDKTELNNTIADAKTKVKEHYSDRSWQNLQTEVTKAEKVAANTDAKQSEVNEAVEKLTATIEKLVELSEKPILTLTSTDKKILEREAVAKYTLENQNKTKIKSITAELKKGEEVINTVVLTDDKVTTETISAAFKNLEYYKEYTLSTTMIYDRGNGEETETLENQNIQLDLKKVELKNIKRTDLIKYENGKETNESLITTIPDDKSNYYLKITSNNQKTTLLAVKNIEETTVNGTPVYKVTAIADNLVSRTADNKFEEEYVHYIEKPKVHEDNVYYNFKELVEAIQNDPSKEYRLGQSMSARNVVPNGKSYITKEFTGKLLSSEGKQFAITELEHPLFNVITNATINNVNFENVEIERSGQDNIASLANTMKGSSVITNVKITGTLSGRNNVAGFVNNMNDGTRIENVAFFGKLHSTSGNGSHTGGIAGTNYRGIVRKAYVDATITGNKTRASLLVPKVDYGLTLDHLIGTKALLTESVVKGKIDVSNPVEVGAIASKTWPVGTVSNSVSYAKIIRGEELFGSNDVDDSDYASAHIKDLYAVEGYSSGNRSFRKSKTFTKLTKEQADAKVTTFNITADKLESDLSPLAKLNEEKAYSSIQDYNAEYNQAYKNLEKLIPFYNKDYIVYQGNKLNKEHHLNTKEVLSVTAMNNNEFITNLDEANKIIVHYADGTKDYFNLSSSSEGLSNVKEYTITDLGIKYTPNIVQKDNTTLVNDIKSILESVELQSQTMYQHLNRLGDYRVNAIKDLYLEESFTDVKENLTNLITKLVQNEEHQLNDSPAARQMIRDKVEKNKAALLLGLTYLNRYYGVKFGDVNIKELMLFKPDFYGEKVSVLDRLIEIGSKENNIKGSRTFDAFGQVLAKYTKSGNLDAFLNYNRQLFTNIDNMNDWFIDATEDHVYIAERASEVEEIKNSKHRAFDNLKRSHLRNTILPLLNIDKAHLYLISNYNAIAFGSAERLGKKSLEDIKDIVNKAADGYRNYYDFWYRLASDNVKQRLLRDAVIPIWEGYNAPGGWVEKYGRYNTDKVYTPLREFFGPMDKYYNYNGTGAYAAIYPNSDDIRTDVKYVHLEMVGEYGISVYTHETTHVNDRAIYLGGFGHREGTDAEAYAQGMLQTPVTGSGFDEFGSLGINMVFKRKNDGNQWYITDPKTLKTREDINRYMKGYNDTLTLLDEIEAESVISQQNKDLNSAWFKKIDREYRDNNKLNQWDKIRNLSQEEKNELNIQSVNDLVDQQLMTNRNPGNGIYKPEAISYNDQSPYVGVRMMTGIYGGNTSKGAPGAVSFKHNAFRLWGYYGYENGFLGYASNKYKQQSKTDGESVLSDEYIIKKISNNTFNTIEEFKKAYFKEVKDKATKGLTTFEVNGSSVSSYDDLLTLFKEAVKKDAETLKQEANGNKTVSMNNTVKLKEAVYKKLLQQTNSFKTSIFK
Protein: Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.-) (Q54HY5)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2
- Major vault protein beta
- Major vault protein alpha
Sequence:
MSNIFQSCNIYLSTVSNKQTLSKTIKDNGGSVSFMLTKNVTHFVCDEKEVQSDSFNYKKAKGYNIPIVSEEFITESVSKSSRLRESDFGFDNVKKVKPFSYFDSPSKSPIKSPIKSPEPIAPIGTVSFTSSTNPLSFSPSSSSSSWSSSNTFTTSTTPIESALPILPPKAIAKKTIAKVVPNPSTSSTTSYTPISSSSSSYSTTSYTTPISSFSSTQSKPTIEIKSNPKKITTKLYPLNDSRQPSFAIGYEVLVSHTLQFTNLTGISSNNKYYHLELQKDSQGIHRVYTSYGRTDGPKTLEVRYVDNLEDGIDLYSSIYNEKTSDKKGYKPVKLDSSSVSSSTSTESLITADSQLEPLIKTLVENLYVEATTQLTNSFSVTITERGIETPLGVLSMEQVENGELVLKKINTYLNGTTNPSSVELEKLSSEFFTIIPHKLGRGSDVVSKNTIRNLDQLNTKFELLQLMKDLLVVKVSGTGKHALDMKYRALKTNLSPLGKYSYDYSVVKNLLKGVEGINDLNIYQIQKEGDVESHSLQSPSKLLFHGSRASNFVGILSRGLLLPKVIVNNGGGRTDFGYLGAGIYFGDGFDTALKYAHPSLSNGKRYALVSKVGLGRVSNHLKINSSLTQPPSGFDSCLGIKKNSTNQSDFHDNEYVIYNTNQYRQEYLIEFTFSGVINSHINNNNNPVSSITSSFNKLNIIPTPVAAVEPKKRTKEAVASVPIASISTFVPLQVPTPPTSVFFPTTTTTTPVATTNLESSMKFNEFVTSFNNISIGDKSIYQEDSTENEYRKLFVNNRNDSKLNNLYLHCEKVFKSKPTTSELPNVNGVDCIMGFNAKQHSFSNDIKFKQEWNRFSNNMFDGFNWSNVFIAGGSVLGCSLEGGIIGNTGFQNSDIDIFLYGLSEDGANSKLDEIEQFIKSKSPQAQMARTKYAITFVSGSGFRNVQIVLRIYKSPAEVLMGFDIDCCSIGFDGTDVYAMPRAIKAVTTSCNIVSMSRRSLTYETRLFKYALRGFSIRVPNLDKRKIPMGQICSSDGKGSTGLLRLLIMEFKFVTGKGDPSSFNLGGASASDYSEIEIPNGQNWSVNSAVNFINYKEKSQFFAKKKHGFKHCHLIVVGTQAKEGKASWCKKCKQGHTPENSDSQDVVTGPIKWITENPGQQILTGSFHPVNDNSWYDLNQPSTTTTTTDKKGLNYYKYRIINNLDVSDIPDYSPRSLSSHGPTTQFLIDSNNLLSIAAGFGSNVSLKSMLSTYKQYVNTIDDLGYYPIHYASFSGNKECLELLLQNNASTSLRNPSYGLTCAMLCKFYNHNDAFNRIISHSPRVFKIKCYLNKVKNLRQWNLLSSAHNTEPAKHLAHPPMIIPSSLKYDQQYLFKSVYNSDLELIKKLLSLPEFKECFDPLGNSLFHYAVLSPYPESVIALLKEKGLDINTTPTNIFGQSVLHFAKSTIGTIQGWTKTIFPLENLGIKLSPIYLHNQLSQIIQSLSKNSNNNSDNFVSKIPSTFMKNYVNDNSFTILNTLQQPQTFGGFGSTSQSFGGSTMIGGGFGSTAQSFGGPGQSFGGPGQSFGPKPIASGGFGSTAIPFGGPGQSFGGSATSGGFGSTAQSFGGPKPTTIGSSGFGSTAVSFGGPGQPFGGSATSGGFGSSTPQSTPAFPSSFGIGGKFAAKIPPSASIPASGFVPLASNISATPTGLFSNTQHSLKNIPQNMGGSSVSNVSLSIAKPATLLNSTQFLESSVMAQCLYLVDDLSTTKKLPDQTVKRIKELLFSLYLPIFNCFEAFLLNTNEKALIENLLLALKNYDQKQ
Protein: Catalase-related peroxidase (EC 1.11.1.-) (Protein SrpA) (Sulfur-regulated plasmid-encoded protein A) (Q55025)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Has an organic peroxide-dependent peroxidase activity.
Subcellular location: Periplasm {ECO:0000269|PubMed:7536734}.
Interaction partners:
Sequence:
MIRIRNRWFRWLAIALASLVASIGIATVGFAATGVTPDQVLSAIEGTFGVNVGQRRNHIKGTCAVGNFVATTEAKTYSRSPLFSGQSIPVVARFSLAGGNPKAPDTAKNPRGLGLQFQLPNNRFLNMALLNTPVFGVASPEGFYENILAIRPDPTTGKPDPEKVKAFREKYPENKAQAAFLASNNPPTSYANTSYFGLHAFKFINQTNQTRLVRWQFVPQDGEKRLTDAELQAAPANFLEQKLIERTQDSPVKWDFWITLGQPGDAEDNPTIAWPSDRQQVKVGTLTLTAASPQPGAACEGINYDPLVLSDGIEPTNDPVLQFRSGVYALSYSKRTRGL
Protein: Uncharacterized protein (Q3V1X2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEEMLSFRDVAVDFSAEEWECLEPAQWNLYRDVMLENYSHLVFLGLAFSKPYLVTFLEQRQEPLNEKRQVATTMHPDIKPYKCKECGKACDWNSLLLEHQRTNPGENAYKCEECGQASGSYSVIPEHHINDTEEKACKCEECGKVICTCSENSSYQRICIGENPYKCEECGKAFSSHSCLAQHEVEHTGQQFYNCEECGKLFYCPSHLTEHQKIHSQENLFKIEVCSEVFCAPIELSKDQNFCTEEKPYRYEDYVKAFSACSVLSEHPTIHPGEKAFKCEECGNAFCTLHSVSKMKIHYEVKSYKCEECGKAFATHLSLIQHKIGHTREKPYQCEECGKMFYCSSNLKQHQITHSQEKPYKCEVCGKVFRTCWQLSKHLRIHSGEKPYKCEECGKAFYTLSYLTQHKLGHTGEKPYKCEECGKTFYYPSVLKEHLAIHSGEKPYRCDECGKDFCTRSGRSRHQRIHTGEKPYKCEQCGKAFSTHSYLSHHKIVHTGHKPYKCEECGKKFYYPSRLKEHQRIHSQENPYKCEICGKAFYTHSYFTQHKLGHTGEKPYKCEECGKTFYYPSILKEHLAIHSGKKPYRCEECGKDFCTRSGRSRHQRIHTGEKPHKCEECGKVFSTHSYLTQHKVVHSGEKPYKCEECGKKFYYPSRLKEHQRIHSQENPYKCEICGNVFCTPKGLSKHQRFHTGEKPYKCEECGKMFYYPSRLKEHQRIHSQENPYKCEICGKAFYTHSYLTQHKLGHTGEKPYKCEECGKTFYYPSILKEHLAIHSGKKPYRCEECGKDFCTRSGRSSHQRIHTGEKPYKCEQCGKAFSTHSYLSQHKVVHSGEKPYKCEECGKMFYYSSRLKEHQRIHSQENPYKCEVCGKVFSAHLELATHLSIHSG