wanglab/gogpt-training-data huggingface dataset:
Protein: Serine-rich coiled-coil domain-containing protein 2 (Coiled-coil serine-rich protein 2) (Granule cell antiserum positive protein 14) (Protein GCAP14) (Q3UHI0)
Organism: Mus musculus (Mouse)
Function: Microtubule-binding protein which might play a role in microtubule bundling.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22673506}. Note=Associates with microtubules in interphase. Has diffuse expression throughout the cell during mitosis. {ECO:0000269|PubMed:22673506}.
Interaction partners:
Sequence:
MEEKTQIKTFLGSKLPKYGMKSVRSTLQPMPNGATVTLLGTSKSSNVKSYIKNNGSDCSLSHSFNWRKTNKYQLGSQNTAELNNIQSTHDKLIEPEQHAPAPGTLDGHGIKGGLKSASLFTSKLARPSTMFVSSAEELSQKSFSGPSNLGKFTKGTLLGRTSYSSVNAKSHLNAFYGNRSSGNVQKPRVNSCASRSSSGESLAQSPDNAKSITCEKMVRSQSFSHSIQNVFLPPSSITRSHSFNRAVDLTKPYQNQQLPVRVPLRSGMLTRSSLQSEVLNGNEHVGFGFNRPYAAAGKKLALSNGPAVSSTLVYRMAHPPLLKSSRPPFSGPMTVDSNKNPPADMCVEEEGMVSAQDSSPGKDQELIENESYRRDNDQTGKNESKVRYLSDDVDDISLSSLSSSDKNDLSEDFSDDFIDLEDSNRTRITPEEMTLKEEKHESRPSKDIFDSPKESEQAFSKAEEWIDISVSDRSECTKHTSGNNLISPDTDYRAGSSFELSPSDSSDGTYMWDEEGLEPIGSVHPVGSYESSEMNSIDILNNLESCDLEDDDLMLDVDLPEDAPLENVECDNMNRFDRTDRNVRQSQDGFWKRPPQRWSGQDHYHLSHPGHYHHHGQSDLSRGSPYRESPLGHFESYGGTPFFQAQKMFVDVPDNTVILDEMTLRHMVQDCTAVKTQLLKLKRLLHQHDGSGSLHDVQLSLPSSPEPEDGDQIYKNEDLLNEITQLKEEIKKKDEKIQLLEQQLATRCNCQQKSKEEKCTYADKYTQTPWRRIPGGYCAPSFSPWQGSFQGMPRTVPPHRRQTSSTTAFQQPSQIYRPRPGKTNKATTYRGPQ
Protein: Sensitive to high expression protein 9, mitochondrial (Mitochondrial distribution and morphology protein 33) (Q04172)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:12591915}; Multi-pass membrane protein {ECO:0000269|PubMed:12591915}.
Interaction partners:
- Mitochondrial distribution and morphology protein 31
- Mitochondrial distribution and morphology protein 32
- Dynamin-like GTPase MGM1, mitochondrial
Sequence:
MLRYYGATRNLPLVFSINKLMLRASSFTRPFHYSSYSLQNGDTPDKGSTNKNEIRTPNNAVWKENIELQWQHLKKKLNELYSRFNFHRDQLSFQVNKAKKSIQEANRKLSEQENEINDSRLNYNKDELTSAKIEGLPSEREQHRKKWSRKLEFYFDSLQETLFTATRALNDVTGYSGIQKLKSSISLMEKKLEATKKEHKLFKAQYANAIDERAQSQREVNELLQRQSAWSSSDLERFTQLYKNDALNARQEQELKNKVKEIESKEEQLNDDLYRAILTRYHEEQIWSDKIRRTSTWGTFILMGMNIFLFIVLQLLLEPWKRKRLVGSFEDKVKSALNEYAKEQNMKMDKLLPGKSSEVTDQGNTENSIVEEHIEQRGECKINTAEIDRPEVATAETTTTEMKSFRDIWERIKALFVTLKSIQYRKLDAPLVFDTLEFYLYSISLVSMTILVSGLI
Protein: YTH domain-containing family protein (Q0WR25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Coiled-coil protein
- Probable protein phosphatase 2C 11
- DEAD-box ATP-dependent RNA helicase 8
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and protein-tyrosine-phosphatase PTEN2A
- Proline transporter 2
- Eukaryotic initiation factor 4A-III homolog
Sequence:
MATTQSHTSDLTSEEQPASLDIMKEQTVPANNETSASFKSSQEAPVVVHPAKVAPLTGPYGLAGDFAGHLPSSILSPQAQGFYYRGYENPTGEWDEYSSYVNVEGLDITSPVGFNENASLVYQTGYGYNPQMPYGPYSPAASPLPSEGQLYSPQQFPFSGASPYYQQVVPPSMQYITSPTQPELTSLVGVDQQGDNIGPRQSYHPHPIGPFNGNQPNLGFPEWQQGFDGGIWSDWSKPSDMHRHSSSISPALSPQPLGSYGSYGQNIPMGSQRQRSFYGFGSGSNSYNRGYMHSGGRGQGSNYGSRLISNVGMGNQGWIGVDNSRGRGRVSDPSLGGAYNGTFDILNEQNRGPRASKPKTQVLEELDSAADSKKNNKGSAKEHEESNNADFVTDYTNAKLFIIKSYSEDNVHKSIKYNVWASTPNGNKKLDAAYREAKDEKEPCPLFLLFSVNASSQFCGVAEMVGPVDFEKSVDYWQQDKWSGQFPVKWHIIKDVPNSQFRHIILENNDNKPVTNSRDTQEVKLEQGIEMLKIFKNYDADTSILDDFGFYEEREKIIQDRKARRQPSLPSAGVVAGENEHKPASAALPTDFMKNMSKSFAQVVRLDEGSKEAVKASSSPDAITTAAVSSGQSN
Protein: Protein S100-A5 (Protein S-100D) (S100 calcium-binding protein A5) (P63084)
Organism: Mus musculus (Mouse)
Function: Binds calcium, zinc and copper. One subunit can simultaneously bind 2 calcium ions or 2 copper ions plus 1 zinc ion. Calcium and copper ions compete for the same binding sites (By similarity).
Interaction partners:
- Protein S100-A16
Sequence:
METPLEKALTTMVTTFHKYSGREGSKLTLSRKELKELIKTELSLAEKMKESSIDNLMKSLDKNSDQEIDFKEYSVFLTTLCMAYNDFFLEDNK
Protein: Protein RUFY3 (RUN and FYVE domain-containing protein 3) (Rap2-interacting protein x) (RIPx) (Single axon-regulated protein) (Singar) (Q5FVJ0)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the generation of neuronal polarity formation and axon growth. Implicated in the formation of a single axon by developing neurons. May inhibit the formation of additional axons by inhibition of PI3K in minor neuronal processes. Plays a role in the formation of F-actin-enriched protrusive structures at the cell periphery (By similarity). Plays a role in cytoskeletal organization by regulating the subcellular localization of FSCN1 and DBN1 at axonal growth cones (By similarity). Promotes gastric cancer cell migration and invasion in a PAK1-dependent manner (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7L099}. Endomembrane system {ECO:0000250|UniProtKB:Q7L099}. Cell projection, invadopodium {ECO:0000250|UniProtKB:Q7L099}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9D394}. Perikaryon {ECO:0000269|PubMed:17439943}. Cell projection {ECO:0000269|PubMed:17439943}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9D394}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9D394}. Lysosome {ECO:0000250|UniProtKB:Q7L099}. Note=Colocalizes with PAK1, F-actin, myosins and integrins in invadopodia at the cell periphery (By similarity). Colocalizes with Ras-related Rab-5 proteins in cytoplasmic vesicles (By similarity). Accumulates in axon growth cones in a F-actin-dependent manner (By similarity). Colocalizes with FSCN1 and F-actin at filipodia and lamellipodia of axonal growth cones (By similarity). Localized in F-actin-enriched filopodia and lamellipodia at axonal growth cones (PubMed:17439943). Colocalizes with DBN1 and F-actin at transitional domain of the axonal growth cone (By similarity). Recruitment to endolysosomes partially depends upon the presence of ARL8 (By similarity). {ECO:0000250|UniProtKB:Q7L099, ECO:0000250|UniProtKB:Q9D394, ECO:0000269|PubMed:17439943}.
Interaction partners:
- Shootin-1
Sequence:
MSALTPPTDMPTPTTDKITQAAMETIYLCKFRVSMDGEWLCLRELDDISLTPDPEPTHEDPNYLMANERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEANALMMEEEGAIIAGLLVGLNVIDANFCMKGEDLDSQVGVIDFSMYLKDGNSSKGSEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKLIPKHH
Protein: Gap junction protein (Q1LWG0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}.
Interaction partners:
- Immunoglobulin superfamily member 11.
- Src homology 2 domain containing transforming protein D
- Inward rectifier potassium channel 13
- Solute carrier family 12 member 7 isoform X4
- Potassium channel, subfamily K, member 5b
Sequence:
MSRADWGFLEHLLEEGQEYSTGVGRVWLTVLFLFRMLVLGTAVESAWDDEQSDFVCNTKQPGCESVCYDKAFPISHFRYFVLQVIFVSTPTIFYFGYVALRARNEKRPEEKLEEDGRRHRHRKTNACILEVIKEEDEDGSETEKNRKALEPPKLKGKLLCAYAASIIVKVLIEVGFILGLWILYGFVIEAKYVCERLPCPHTVDCFVSRPTEKNIFTIYTQVIAVVSILLNVVELFHLLQLVITRRLEKKYQAEVQIHNRVRTAPSKAQQPSFEERNHLFLPVAHGGYPTEGLDWEKRDPSLAEDMLPSYSNCIRNMKPAINKNNLPKKHLKADDKPRHYV
Protein: Calcium/calmodulin-dependent protein kinase type 1G (EC 2.7.11.17) (CaM kinase I gamma) (CaM kinase IG) (CaM-KI gamma) (CaMKI gamma) (CaMKIG) (CaMK-like CREB kinase III) (CLICK III) (Q96NX5)
Organism: Homo sapiens (Human)
Function: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates transcription factor CREB1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Calmodulin-1
- Nitric oxide synthase 3
- Calmodulin-like protein 5
- Calmodulin-like protein 3
- Calmodulin-like protein 6
- Calmodulin-like protein 4
- Small conductance calcium-activated potassium channel protein 2
- Cyclic AMP-responsive element-binding protein 1
- Cyclic AMP-dependent transcription factor ATF-1
Sequence:
MGRKEEDDCSSWKKQTTNIRKTFIFMEVLGSGAFSEVFLVKQRLTGKLFALKCIKKSPAFRDSSLENEIAVLKKIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDRILERGVYTEKDASLVIQQVLSAVKYLHENGIVHRDLKPENLLYLTPEENSKIMITDFGLSKMEQNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESKLFEKIKEGYYEFESPFWDDISESAKDFICHLLEKDPNERYTCEKALSHPWIDGNTALHRDIYPSVSLQIQKNFAKSKWRQAFNAAAVVHHMRKLHMNLHSPGVRPEVENRPPETQASETSRPSSPEITITEAPVLDHSVALPALTQLPCQHGRRPTAPGGRSLNCLVNGSLHISSSLVPMHQGSLAAGPCGCCSSCLNIGSKGKSSYCSEPTLLKKANKKQNFKSEVMVPVKASGSSHCRAGQTGVCLIM
Protein: Ferric uptake regulation protein (H7C6Q1)
Organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364037}.
Interaction partners:
- Alkyl hydroperoxide reductase C
- Thioredoxin
- Bll0796 protein
- DNA-directed RNA polymerase subunit alpha
- Bll7632 protein
Sequence:
MTALKPSSASKASGIEARCAATGMRMTEQRRVIARVLAEAVDHPDVEELYRRCVAVDDKISISTVYRTVKLFEDAGIIERHDFREGRARYETMRDSHHDHLINLRDGKVIEFTSEEIEKLQAEIARKLGYKLVDHRLELYCVPLDDDKPTS
Protein: Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) (Cell division control protein 72) (Myristoyl-CoA:protein N-myristoyltransferase) (NMT) (Peptide N-myristoyltransferase) (P14743)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N-terminal glycine in the nascent polypeptide substrates. Uncharged amino acids are preferred at position 2 while neutral residues are favored at positions 3 and 4. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ADP-ribosylation factor 1
- Dihydroorotase
- ADP-ribosylation factor 2
- Guanine nucleotide-binding protein alpha-1 subunit
- Methionine aminopeptidase 2
Sequence:
MSEEDKAKKLENLLKLLQLNNDDTSKFTQEQKKAMKDHKFWRTQPVKDFDEKVVEEGPIDKPKTPEDISDKPLPLLSSFEWCSIDVDNKKQLEDVFVLLNENYVEDRDAGFRFNYTKEFFNWALKSPGWKKDWHIGVRVKETQKLVAFISAIPVTLGVRGKQVPSVEINFLCVHKQLRSKRLTPVLIKEITRRVNKCDIWHALYTAGIVLPAPVSTCRYTHRPLNWKKLYEVDFTGLPDGHTEEDMIAENALPAKTKTAGLRKLKKEDIDQVFELFKRYQSRFELIQIFTKEEFEHNFIGEESLPLDKQVIFSYVVEQPDGKITDFFSFYSLPFTILNNTKYKDLGIGYLYYYATDADFQFKDRFDPKATKALKTRLCELIYDACILAKNANMDVFNALTSQDNTLFLDDLKFGPGDGFLNFYLFNYRAKPITGGLNPDNSNDIKRRSNVGVVML
Protein: WW domain-binding protein 1 (WBP-1) (P97764)
Organism: Mus musculus (Mouse)
Interaction partners:
- Actin-related protein 5
- RuvB-like 2
- RuvB-like 1
- INO80 complex subunit C
Sequence:
MARASSRNSSEEAWGSLQAPQQQQSPAASSLEGAIWRRAGTQTRALDTILYHPQQSHLLRELCPGVNTQPYLCETGHCCGETGCCTYYYELWWFWLLWTVLILFSCCCAFRHRRAKLRLQQQQRQREINLLAYHGACHGAGPVPTGSLLDLRLLSAFKPPAYEDVVHHPGTPPPPYTVGPGYPWTTSSECTRCSSESSCSAHLEGTNVEGVSSQQSALPHQEGEPRAGLSPVHIPPSCRYRRLTGDSGIELCPCPDSSEGEPLKEARASASQPDLEDHSPCALPPDSVSQVPPMGLASSCGDIP
Protein: Granulocyte colony-stimulating factor receptor precursor (Granulocyte stimulating factor receptor) (A8Y5W0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MASVSLEIKLWMYIYVVIKVTGASSCGNVYTPAPVVLAGSPVSVSCSIEEDCPLTKGKVFYVQWRIDGQVVPRTYTYQESNMTYSVLIPRLQDTSASILCLVCVQEDCQIVDGVEVKTGNPPVPQNLSCALTLVKMPSLRCDWNPVQEIKNLPINYTLHVFRAKSQKVYAVPPGQHFYVVPRDAYGYFSELEISVTAANVLGNTTSDPLKLTPLNTVKFDPPSITRIEAHKYGCLKYSWSLSETQKWLQLTFIVQLRLKTVSNQPNKDLVYTSRQLQLNPIEVCSLLHWTDYRSTVRVKYYATSEWSEWSDPKTATTLNKAPAGRLDTWLKVNNQTAQLYWKPSQQFRANGQNLSYSVDSKDTKKRLCVTTETYCFFSLTKWDKKIFLRARNEVGFSDHNEVPVAVHRNKGLEPVSNFSVHPQSNTSLHVIWKSPAFSNVTSYVLEWRSLCGTTAAPLSFTLIHKNKSNTTLTGLEPSKPYEISIYPRYVKGIGRPVTVLAYSSETAPSDAPELNYEEISRSHLKFHWGQIPLEKRNGIIQGYRFYFWHNKNEIKEIMTTETSVEVKDLQPHTKYHALLSICTKGGCVNGSFSTLTTERLDGIEMVIFVIPACIGASLLVIIIVFTCFGKQERVKMCLWPIIPDPANSSIKRWTTTDSLQGLPAFKEDKDPVLVYLSHLSLLDMTEKEPFKSGYVKENQWPDDLNIHADTQSCDLELERESVPYATVLFSTPYQINSSNPPAYVRSESTQPLLAGDEPGSPPPPYENVPRGGAVSALNRFSAFSQSTQSEESDELWEEFPMLRSLEVNHI
Protein: Elongator complex protein 5 (AtELP5) (Elongator component 5) (F4IQJ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8TE02}. Cytoplasm {ECO:0000250|UniProtKB:Q8TE02}.
Interaction partners:
- Elongator complex protein 1
- Elongator complex protein 4
- Elongator complex protein 2
- Elongator complex protein 6
- Elongator complex protein 3
- Protein KTI12 homolog
- U11/U12 small nuclear ribonucleoprotein 59 kDa protein
- Phospholipid--sterol O-acyltransferase
- Receptor-like serine/threonine-protein kinase ALE2
- Homogentisate solanesyltransferase, chloroplastic
Sequence:
MAESIFRKLRDGGEEGELAPALTIEETVASPFGLDVSGYLLTNLSSSILAGKSSSQGLVLITFSRSPSFYLQLLKQKGIVVSSSSKWIRILDCYTDPLGWIDQSSTSFSEGSSLIKLHKCVSDLKKLFSSIIEAGRELVGTGKTRFCVAIDSVNELLRHSAMPLVSGLLTDLRSHAQISSVFWSLNTDLHQEKVTNALEYISTMKANLEPLCPSSDGQRNALENLFSVHQDFGKGRFHVRFKLRKGRVRVMSEEYHVDQSGINFSPISSVDTVIAATKSLLPKVQFNLQLSEKERVEKEKVVLPFEHQDDGKSNEIYDGRRSLVDGKIETTPLSSMELQTDVVSSGKGGEIIYFRDSDDEHPDSDEDPDDDLDI
Protein: Dynein axonemal assembly factor 8 (Dynein axonemal-associated protein 1) (A0A1L8EYB2)
Organism: Xenopus laevis (African clawed frog)
Function: In cyliated cells, dynein axonemal particle-specific protein required for deployment of ODA to the axoneme. Interacts with outer dynein arm (ODA) subunits.
Subcellular location: Dynein axonemal particle {ECO:0000269|PubMed:33263282}. Cytoplasm {ECO:0000250|UniProtKB:Q8IYS4}. Note=Location is restricted to the outer dynein arm (ODA) sub-region of dynein axonemal particles (DynAPs). {ECO:0000269|PubMed:33263282}.
Interaction partners:
- Small ribosomal subunit protein uS10m
- Uncharacterized protein.
- Small ribosomal subunit protein bS6m
- Uncharacterized protein
- Uncharacterized protein.
- 28S ribosomal protein S14
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS10
Sequence:
MASEQDGFLPAATRGDSNWSGVSGWESALSAMRAEVPSIDSDDSSLSDCEEEELHIFQREDTNLIPDLSIELLDDGELNSEVVTRQMSLEKVEFSDSLEPSPNVCVPLSVQKAELDDTINSRNPETEQLCPEPIDNIQTESMVGIKDSEKEDGFRHVLHSSVTTVLKPQINSNVDSEYEIHPGNTEKEHLSTSALSSKPVGLSLQFLECLEQWDLNALLHQLKEEEVQEREMPPLILSMEESTERRHKLIMEKLVEFAAQQSEEVSSVPQLEEKEKEGTISKSSFRPYPDQKMYLKGSGKHPQSFSTICLDLRTTVSKMGQVTSLEQNPENPSQRNEQKEKHHLNKTDHTGKSLLLRNRHNIQNDSLSDANMSNSESLSKEKKELGTPTQRKQRPKSKVDISPKLQEMVGREEKDGREEQEKEKEILQYLPPKSLINSRADEFAQREKQEKEKKARLRMLTQLEDLKPRSSVNGRQPMAEATPILFHPETSYCPGISSLPDVARSGVETLLLTICLSSCGQVFIPGQHGARSSYPSLFLANTFHCLLTWLISLVPGVNTHGKVNAPFHVLGLQQAWQEEGLALYACLSPRQIATQSSPKIRKHKGKQDLRGTSSFYQRVSLFLSHNTLQSVIWWSEDVVERLQGKLFPLPTEVPAVRLSSIATLNSAPEAVEKVFSSACGFYWQTLETEEKINPLLSEIPTDSETEVVSVIVFERMLSNPTAFHHTLHIIQTEGLDVCGVRLLYPQANALHSYIDTVPSSYTGGDGQTLPVLALALRGTQAEHIWAEIAGPFDPQLARLTDQYSLNAMYGFKRGEPIMHWARKSGRLLQELSLWFGGRIPPSGSFNIGFQNPYSRSTQPRSANLRSRSDSEKDVTAFHDTDRCRPPALLTASILGDVFLVVSPAVPSAAYGDVIDICLHRGFALYGLRRLRLSAKRSAMLSMSSTQVSIFCPNVPHSQTDAQPCRQPRLHCFLLLLRKENAAHHTSGLIQALMNELAERGLLGAIHAKFSYICEVDPSFCFHVAPYTDNLLQSLGGSLHAMPDLSTVPMDMLSLRPFASDPEDEQVVVLTMSGKHTLRRAGYFLQKILRPTLKTPASNTGSVHDGFELLGLKWLPSLSRLQAKEITPYEVGDRPWQRSIEHLISNPALLCALRRSNAFAVLQHTIKQLAPTLGMEHPQLIASATPEIAFRQAALIFSDRDLVSDPESRSSLMYIPPTGINCRAGGTEDRRGTTESIFTYMLSGPPVLYTVLLLKPRIWSSALGKILYKVHQQKFILVGMKPVSLTTAMCSQILPEDVKKSEALCLTHCDYLTSGPCLALCLQRRGAVLKLLDVLGPEDPELCRAQDQFLWRAQYGTSAVQNGMYGSTSYQAAIRDIKTFFPEGLLFEESTVLQAEQIPKLTSDILVCSRSHRQTVKNPACGPELPTTDLPFTSALCQTTCLLFPPHMLRTSPPPYIPALEQLMAKEFHITAARLTAFDQLQAQLVAEMYSPGNYLTAKIKLLTEGPCLLVAAQRDNAVTCFPSLVHSDDRHNMSAQTLTEQVLCPQTESQANKMLSCFFDSLTPDSIHQILH
Protein: NADPH oxidase 2 (EC 1.6.3.-) (CGD91-phox) (Cytochrome b(558) subunit beta) (Cytochrome b558 subunit beta) (Cytochrome b-245 heavy chain) (Heme-binding membrane glycoprotein gp91phox) (Neutrophil cytochrome b 91 kDa polypeptide) (Superoxide-generating NADPH oxidase heavy chain subunit) (gp91-1) (gp91-phox) (p22 phagocyte B-cytochrome) (P04839)
Organism: Homo sapiens (Human)
Function: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15338276, ECO:0000269|PubMed:22808130}; Multi-pass membrane protein. Note=As unassembled monomer may localize to the endoplasmic reticulum. {ECO:0000305|PubMed:28351984}.
Interaction partners:
- Neutrophil cytosol factor 4
- Neutrophil cytosol factor 2
- Ras-related C3 botulinum toxin substrate 2
- Neutrophil cytosol factor 1
- Cytochrome b-245 light chain
- NADPH oxidase 1
- NADPH oxidase 4
- NADPH oxidase organizer 1
- NADPH oxidase activator 1
- RAC-alpha serine/threonine-protein kinase
Sequence:
MGNWAVNEGLSIFVILVWLGLNVFLFVWYYRVYDIPPKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRVRRQLDRNLTFHKMVAWMIALHSAIHTIAHLFNVEWCVNARVNNSDPYSVALSELGDRQNESYLNFARKRIKNPEGGLYLAVTLLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTAESLAVHNITVCEQKISEWGKIKECPIPQFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNNATNLKLKKIYFYWLCRDTHAFEWFADLLQLLESQMQERNNAGFLSYNIYLTGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASQHPNTRIGVFLCGPEALAETLSKQSISNSESGPRGVHFIFNKENF
Protein: Tetraspanin (A0A8I5Y9E0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}.
Interaction partners:
Sequence:
MAGVSGCLKYSMFFFNFLFWVCGTLILGLAIWLRVSKDGKEIITSGDNGTNPFIAVNILIAVGSIIMVLGFLGCCGAVKESRCMLLLFFIGLLLILLLQVAAGILGATFKSESSRILNETLYENAKLLSETSNEAKEVQKAMIAFQSEFKCCGLRFGAADWGKNFPDAKESCQCTGSDCESYNGENVYRTTCLSLIKELVEKNIIIVIGIAFGLAVIEVQYSSDHLSMHL
Protein: Disease resistance protein RPP4 (EC 3.2.2.6) (Protein CHILLING-SENSITIVE 2) (Protein RECOGNITION OF PERONOSPORA PARASITICA 4) (F4JNA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: TIR-NB-LRR receptor-like protein that confers resistance to the pathogen Hyaloperonospora arabidopsis isolates Emoy2 and Emwa1 (downy mildew disease). Plays a role in the regulation of temperature response during plant growth and survival.
Interaction partners:
- Disease resistance protein RPP8
- Disease resistance protein RPP13
- Disease resistance protein RPM1
- Protein EDS1
- Negative regulator of systemic acquired resistance SNI1
- Lipase-like PAD4
- Cysteine and histidine-rich domain-containing protein RAR1
- Protein LSD1
- Uncharacterized protein
- LRR protein
Sequence:
MASSSSSPSSRRYDVFPSFSGVDVRKTFLSHLIEALDRRSINTFMDHGIVRSCIIADALITAIREARISIVIFSENYASSTWCLNELVEIHKCYKKGEQMVIPVFYGVDPSHVRKQIGGFGDVFKKTCEDKPEDQKQRWVKALTDISNLAGEDLRNGPTEAFMVKKIANDVSNKLFPLPKGFGDFVGIEDHIKAIKSILCLESKEARIMVGIWGQSGIGKSTIGRALFSQLSSQFHHRAFITYKSTSGSDVSGMKLSWEKELLSEILGQKDIKIDHFGVVEQRLKHKKVLILLDDVDNLEFLKTLVGKAEWFGSGSRIIVITQDKQLLKAHEIDLVYEVELPSQGLALKMISQYAFGKDSPPDDFKELAFEVAELVGSLPLGLSVLGSSLKGRDKDEWVKMMPRLRNDSDDKIEETLRVGYDRLNKKNRELFKCIACFFNGFKVSNVKELLEDDVGLTMLADKSLIRITPDGDIEMHNLLEKLGREIDRAKSKGNPAKRQFLTNFEDIQEVVTEKTGTETVLGIRVPPTVLFSTRPLLVINEESFKGMRNLQYLEIGHWSEIGLWSEIGLWSKIDLPQGLVYLPLKLKLLKWNYCPLKSLPSTFKAEYLVNLIMKYSKLEKLWEGTLPLGSLKKMDLGCSNNLKEIPDLSLAINLEELNLSKCESLVTLPSSIQNAIKLRTLYCSGVLLIDLKSLEGMCNLEYLSVDWSSMEGTQGLIYLPRKLKRLWWDYCPVKRLPSNFKAEYLVELRMENSDLEKLWDGTQPLGSLKEMYLHGSKYLKEIPDLSLAINLERLYLFGCESLVTLPSSIQNATKLINLDMRDCKKLESFPTDLNLESLEYLNLTGCPNLRNFPAIKMGCSYFEILQDRNEIEVEDCFWNKNLPAGLDYLDCLMRCMPCEFRPEYLTFLDVSGCKHEKLWEGIQSLGSLKRMDLSESENLTEIPDLSKATNLKRLYLNGCKSLVTLPSTIGNLHRLVRLEMKECTGLELLPTDVNLSSLIILDLSGCSSLRTFPLISTRIECLYLENTAIEEVPCCIEDLTRLSVLLMYCCQRLKNISPNIFRLTSLMVADFTDCRGVIKALSDATVVATMEDHVSCVPLSENIEYTCERFWDELYERNSRSIFSYKDEDGDVYWVNWDLMMMLMLI
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (A0A0B4LH21)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
MGTKTQPQLAKENERRIRANDKEFNAQFKYHNNYIKTSKYSLFTFLPFNLLEQFQRLANFYFLCLLVLQLIPAISSLTPVTTAIPLIGVLTLTAVKDAYDDIQRHISDSQVNNRKSKTLRNGKLVEAKWSEVQVGDVIRLDNNQFVAADTLLLSTSEPNGLCFIETAELDGETNLKAKQCLTETIELGDRHDSLWNFNGEIICERPNNLLNKFDGTLIWRGQRFALDNEKILLRGCVLRNTQWCYGVVVFAGVDTKLMQNSGKTQFKSTGVDRLLNFIIIGIVLFLVSICALFAIGCAIWEGLIGQHFQLYLPWEHIIPKDYIPTGATVIGLLVFFSYAIVLNTVVPISLYVSVEVIRFVQSFLINWDEEMYYPTTNTYAKARTTTLNEELGQIQYIFSDKTGTLTQNIMTFNKCSINGRSYGDVIDLRTGELVEITEQQTIFQNSNTNNRPSPLSGAIVAPPAAPPPIILVHKAEVHAKKTSMVVTSSGEAQVLPDRPRSDIERSAPPMDASEKRPGLKHVRYSAPSRSQDADAGRLSPRLDGSGGLSPPVGNEERRISGGFKRSGAGCMQRQLSRTSSCDKALQSVDFSANPHHESDFRWYDRTLLDAVRSDEEHSHVFFRLLALCHTVMAETVDGKLEYQAQSPDEAALVSAARNFGFVFRTRTPNSITIEVMGQTEEYELLNILDFNNVRKRMSVILRRGDSMVLYCKGADNVIYDRLHGGQEDLKARTQDHLNKFAGEGLRTLALAERRLTEQYYNDWRSRQQEAALSMDSREQKLNAIYEEIESEMQLVGVTAIEDKLQDGVPKSIANLQNAGIKIWVLTGDKQETAINIGYSCQLLTDELADVFIVDGNSVEEVEKQLRQFKESIKIYNRFRPGGFDPFDRLNSDSNMDPLSVTMTQTSAFMQETNLPPTPPPPPAISVVTFRWDEKNKDNKGGPDSAECNNLFGDEKGSEDGGTASIVVDENTGFALVVNGHSLVHCLSPELENKFLDIASQCKAVICCRVTPLQKALVVELIKRAKNAVTLAIGDGANDVSMIKAAHIGVGISGQEGLQAVLSSDYSIAQFRYLERLLLVHGRWSYYRMCKFLRYFFYKNFAFTLCHCWYSLFCGFSAQTVFDPMFISVYNLFYTSLPVLALGVFEQDVSDKNSLEFPRLYTPGLKSELFNIREFIYSVLHGAFTSLVLFLIPYGVYKDGVSANGFVVSDHMTLGAVVATILIVDNTAQISLYTSYWTVVNHVTIWGSLVWYFVLDYFYNYVIGGPYVGSLTQAMKDLTFWVTMLITVMALVAPVLAYKFYLLDVHPSLSDKIRQKSLKKIHSRASSDVRRTASSRRGRRSVRSGYAFAHQEGFGRLITSGKIMHKLPQDFAFPLGLGTKKTQVLHNNLNSADGPNSKGNNVTGHHMVNNNTNMRHNQNQNHSSMADITADGRGNGGDDGRGSGGSDDMSPRAPCQDLDTINL
Protein: Small ribosomal subunit protein uS17m (37S ribosomal protein S17, mitochondrial) (Q9UUB0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein mS29
Sequence:
MKLNYVGIVISRAMPKTAKVRVAKEKFHPVVKKYVTQYQNYMVQDDLNCNVGDAVTIQPCRPRSATKRFEIIKILSTANRMSPASEISKE
Protein: D-dopachrome decarboxylase (EC 4.1.1.84) (D-dopachrome tautomerase) (O35215)
Organism: Mus musculus (Mouse)
Function: Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P30046}.
Interaction partners:
- H-2 class II histocompatibility antigen gamma chain
Sequence:
MPFVELETNLPASRIPAGLENRLCAATATILDKPEDRVSVTIRPGMTLLMNKSTEPCAHLLVSSIGVVGTAEQNRTHSASFFKFLTEELSLDQDRIVIRFFPLEAWQIGKKGTVMTFL