wanglab/gogpt-training-data huggingface dataset:
Protein: Bud site selection protein 25 (P85052)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in bud site selection. Required for resistance to the DNA-damaging agent methyl methanesulfonate (MMS).
Interaction partners:
- Bud site selection protein 5
- Bud site selection protein RAX1
Sequence:
MFCTWDSWDTGTSRKSHSPHRNCLAVRFLQLPFSSFLPCVITYMKSWQTSIGDSEFPLTSFQILVTDAEVVVQRIFDCINGYLPGWHYRNTVFIEHTTSYHRSHFCIFVEGVWVCGEFVKKWFEIPFDNRIENYTKQFPWILIGFGNQVSKAL
Protein: Tektin-3 (Q9BXF9)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms filamentous polymers in the walls of ciliary and flagellar microtubules (By similarity). Required for normal sperm mobility (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:36708031}. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000250|UniProtKB:A6H782, ECO:0000250|UniProtKB:Q4V8G8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q4V8G8}. Note=In spermatozoa, preferentially localizes to the flagella, but also found in the head (PubMed:36708031). In the sperm flagellum, localizes to the periaxonemal region where it associates with the mitochondrial sheath and outer dense fibers (By similarity). Not detected in the central axonemal region of the flagellum (By similarity). Associates with the acrosome membrane in the equatorial segment of the sperm head (By similarity). Also detected just below the plasma membrane in the post-acrosomal region where it might localize to the postacrosomal dense lamina (By similarity). However, other studies report little or no expression in the postacrosomal region (By similarity). Translocates from the postacrosomal region to the equatorial segment after sperm activation (By similarity). Retained in the postacromal region, but not the equatorial segment, following the acrosome reaction (By similarity). Some studies report strong expression in the anterior cap region (By similarity). However, other studies report little or no expression in the acrosomal cap (By similarity). {ECO:0000250|UniProtKB:A6H782, ECO:0000250|UniProtKB:Q4V8G8, ECO:0000269|PubMed:36708031}.
Interaction partners:
- Sperm-associated antigen 8
- Tektin-2
- Cilia- and flagella-associated protein 53
- RIB43A-like with coiled-coils protein 2
- EF-hand domain-containing protein 1
- Tubulin beta-4B chain
- Tektin-1
- Enkurin
- EF-hand domain-containing family member B
- Piercer of microtubule wall 2 protein
Sequence:
MERVGCTLTTTYAHPRPTPTNFLPAISTMASSYRDRFPHSNLTHSLSLPWRPSTYYKVASNSPSVAPYCTRSQRVSENTMLPFVSNRTTFFTRYTPDDWYRSNLTNYQESNTSRHNSEKLRVDTSRLIQDKYQQTRKTQADTTQNLGERVNDIGFWKSEIIHELDEMIGETNALTDVKKRLERALMETEAPLQVARECLFHREKRMGIDLVHDEVEAQLLTEVDTILCCQERMKLHLDKAIAQLAANRASQHELEKDLSDKQTAYRIDDKCHHLRNTSDGVGYFRGVERVDATVSVPESWAKFTDDNILRSQSERAASAKLRDDIENLLVVTANEMWNQFNKVNLSFTNRIAETADAKNKIQTHLAKTLQEIFQTEMTIESIKKAIKDKTAFLKVAQTRLDERTRRPNIELCRDMAQLRLVNEVHEVDDTIQTLQQRLRDAEDTLQSLVHIKATLEYDLAVKANSLYIDQEKCMSMRKSYPNTLRLVGFC
Protein: Calcium channel, voltage-dependent, beta 4a subunit (Voltage-dependent L-type calcium channel subunit beta-4a) (Voltage-gated calcium channel beta-4 subunit variant 2) (B0F0D0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Voltage-dependent N-type calcium channel subunit alpha
- Calcium channel, voltage-dependent, P/Q type, alpha 1A subunit, a.
- Voltage-dependent calcium channel gamma-4 subunit
- Voltage-dependent N-type calcium channel subunit alpha
- Potassium voltage-gated channel subfamily KQT member 2 isoform X2
- Voltage-dependent L-type calcium channel subunit alpha
- K2P10.1 potassium channel subunit
- Potassium voltage-gated channel subfamily C member 3b
- Voltage-dependent L-type calcium channel subunit alpha
- Sodium channel protein
Sequence:
MSRHIYTRHGIGDGVQKPIFQVNRGTYSRRSRLKRSDGSTTSTSFILRQGSADSYTSRPSDSDVSLDEEQGGRQEKEQQATVQLERAKAKAVAFAVRTNVSYCGALDEDVPVAGTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCDIGFIPSPLKLENIRLQQDQKRGRFHGKSSGNSSSSLGEMVSGTFKPNPASAGKQKQKVAEHIPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFEGRISITRVTADISLAKRSVLNNPSKRAIIERSNTRSNLAEVQSEIERIFELARSLQLVVLDADTINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPPEMFDIILDENQLEDACEHLSEYLEAYWRATHTSLSTPLNPLLGRNLGSTALSPYPTAISGLQSQRNKNSNHITDNSPMERRSLMTSDENYHNNERQKKTHNRLSSSSQQSRDHYPLVEEDYHDPYPDAYKPHRNRGSPGGYSNDSRHRL
Protein: Probable caffeoyl-CoA O-methyltransferase 2 (EC 2.1.1.104) (O-methyltransferase 6) (Q86IC8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Thymidine kinase 1
Sequence:
MEQKTAPTQYEVKVQYNNSILNYAIDHSDQLTDIQKELIQFTKENIERHIMLTQAEQCSFFKLLIQVLNAKKTIDIGVFTGLSSLTAALAMGDEGRVVACDVSTEYTQHALKFWAKAGVDHKINLKIQPASKTLQELIDQGEENTYDFVFIDADKTGYDTYYELSLKLIRKGGIIAIDNVLQHGRVADPNANVEPNLVAIRALNDKILADKRVTKSLLPIADGITLITKIN
Protein: Circumsporozoite protein (CS) (PfCSP) [Cleaved into: Circumsporozoite protein C-terminus] (P02893)
Organism: Plasmodium falciparum
Function: Essential sporozoite protein. In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (By similarity). In the vertebrate host, required for sporozoite migration through the host dermis and infection of host hepatocytes. Binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on the surface of host hepatocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P19597}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P23093}. Note=Localizes to the cytoplasm and the cell membrane in oocysts at day 6 post infection and then gradually distributes over the entire cell surface of the sporoblast and the budding sporozoites. {ECO:0000250|UniProtKB:P23093}.
Interaction partners:
Sequence:
MMRKLAILSVSSFLFVEALFQEYQCYGSSSNTRVLNELNYDNAGTNLYNELEMNYYGKQENWYSLKKNSRSLGENDDGNNNNGDNGREGKDEDKRDGNNEDNEKLRKPKHKKLKQPGDGNPDPNANPNVDPNANPNVDPNANPNVDPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNVDPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNKNNQGNGQGHNMPNDPNRNVDENANANNAVKNNNNEEPSDKHIEQYLKKIKNSISTEWSPCSVTCGNGIQVRIKPGSANKPKDELDYENDIEKKICKMEKCSSVFNVVNSSIGLIMVLSFLFLN
Protein: Palmitoyltransferase PFA4 (EC 2.3.1.225) (Protein S-acyltransferase) (PAT) (Protein fatty acyltransferase 4) (Q12006)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. Palmitoylates several amino acid permeases. Palmitoylates chitin synthase CHS3, which is required for its proper export from the ER. Can palmitoylate RAS2 in vitro.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03199, ECO:0000269|PubMed:15973437}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03199, ECO:0000269|PubMed:15973437}.
Interaction partners:
- Palmitoyltransferase AKR1
- Probable palmitoyltransferase AKR2
- Ras modification protein ERF4
- Chitin synthase 3
Sequence:
MPVKLRWPWLGIAIPTFLISFIGYGAHYFILSNFLSVPKQITFEFCLSMIWLSYYLAICTNPGRPLPNYKPPPDIWRNFCKKCQSYKPERSHHCKTCNQCVLMMDHHCPWTMNCVGFANYPHFLRFLFWIIVTTSVLFCIQAKRIYFIWQQRHLPGYFFKKSELIFLTISSPLNSFVLLTITILFLRCLFNQILNGRSQIESWDMDRLESLFNSGRLTQKLIDNTWRIYPESRSFQNKKDAEEHLTKKRPRFDELVNFPYDFDLYTNALLYLGPIHLWLWPYGVPTGDGNNFPKNGISKYEANSSLEDHILSLPWPPDGGKTNTVFNHGSSTIEMRNESGEQLIRTRLPQNGRHASREKWYNDWGESLDDFGVDVDME
Protein: Suppression of tumorigenicity 18 protein (Zinc finger protein 387) (O60284)
Organism: Homo sapiens (Human)
Function: Repressor that binds to DNA sequences containing a bipartite element consisting of a direct repeat of the sequence 5'-AAAGTTT-3' separated by 2-9 nucleotides. Represses basal transcription activity from target promoters (By similarity). Inhibits colony formation in cultured breast cancer cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:15489893}.
Interaction partners:
Sequence:
MDAEAEDKTLRTRSKGTEVPMDSLIQELSVAYDCSMAKKRTAEDQALGVPVNKRKSLLMKPRHYSPKADCQEDRSDRTEDDGPLETHGHSTAEEIMIKPMDESLLSTAQENSSRKEDRYSCYQELMVKSLMHLGKFEKNVSVQTVSENLNDSGIQSLKAESDEADECFLIHSDDGRDKIDDSQPPFCSSDDNESNSESAENGWDSGSNFSEETKPPRVPKYVLTDHKKDLLEVPEIKTEGDKFIPCENRCDSETERKDPQNALAEPLDGNAQPSFPDVEEEDSESLAVMTEEGSDLEKAKGNLSLLEQAIALQAERGCVFHNTYKELDRFLLEHLAGERRQTKVIDMGGRQIFNNKHSPRPEKRETKCPIPGCDGTGHVTGLYPHHRSLSGCPHKVRVPLEILAMHENVLKCPTPGCTGRGHVNSNRNTHRSLSGCPIAAAEKLAMSQDKNQLDSPQTGQCPDQAHRTSLVKQIEFNFPSQAITSPRATVSKEQEKFGKVPFDYASFDAQVFGKRPLIQTVQGRKTPPFPESKHFPNPVKFPNRLPSAGAHTQSPGRASSYSYGQCSEDTHIAAAAAILNLSTRCREATDILSNKPQSLHAKGAEIEVDENGTLDLSMKKNRILDKSAPLTSSNTSIPTPSSSPFKTSSILVNAAFYQALCDQEGWDTPINYSKTHGKTEEEKEKDPVSSLENLEEKKFPGEASIPSPKPKLHARDLKKELITCPTPGCDGSGHVTGNYASHRSVSGCPLADKTLKSLMAANSQELKCPTPGCDGSGHVTGNYASHRSLSGCPRARKGGVKMTPTKEEKEDPELKCPVIGCDGQGHISGKYTSHRTASGCPLAAKRQKENPLNGASLSWKLNKQELPHCPLPGCNGLGHVNNVFVTHRSLSGCPLNAQVIKKGKVSEELMTIKLKATGGIESDEEIRHLDEEIKELNESNLKIEADMMKLQTQITSMESNLKTIEEENKLIEQNNESLLKELAGLSQALISSLADIQLPQMGPISEQNFEAYVNTLTDMYSNLERDYSPECKALLESIKQAVKGIHV
Protein: Pcdhga12 protein (Q6NXW8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MIPMQRREDCKGLVFLGVLLGMLWKAGSTQIRYSVPEELEKGSRVGNISKDLGLKPRELAERGVRIVSRGRAQLFALNPRSGSLVTAGRIDREELCMGSIKCQLNLEILMEDIGKIYGVEIEVRDINDNAPYFRESELEIKMSENAAAGMRFPLPHAWDPDIGKNSLQSYQLSPNAHFSLEVQNGADGNKYPELVLESSLDREEKAAHLLVLTASDAGDPVRTGTARIRVTVLDANDNAPAFARSEYRVSVRENVAVGTQLLLVNATDRDEGANAEVIYSFRYVDDKAAKVFKLDSNLGTISTIGELNHEESGFYEMEVQATDNAGYSARAKVLVTVLDVNDNAPEVAITSLTNSVPENSPRGTLIALLNVNDQDSGENGQVICSIQENLPFKLEKSYGNYYRLVTDAVLDREEVPSYNITVTATDRGSPPLTTETHLALDIADTNDNSPVFLQASYWAYIPENNPRGASIASVTAHDPDSDKNAQVTYSLAEDTHQGVPLSSYVSINSDTGVLYALHSFDYEQFPDLQLQVMARDSGDPPLSSNVSLSLFVLDQNDNVPEILYPTLPTDGSTGVELAPRSAEPGYLVTKVVAVDRDSGQNAWLSYRLLKASEPGLFSVGLHTGEISTARALMDRDALKQNLVVSVQDHGQPPLSATVTLTVAIADSIPDVLADLDNLESPSTSETSGLTLYLVVAVAAVSTVFLVFVLVLLALRLRRWHSLRLLRAGGPGLADVAASHFVGVDGVQAFLQTYSHEVSLTAGSRKSHLIFPQPNYADTLISQESCEKTEPLLPSGDSVFSKDNHALNQVSLF
Protein: Sp110 nuclear body protein (Intracellular pathogen resistance protein 1) (Q8BVK9)
Organism: Mus musculus (Mouse)
Function: May act as a transcription factor. Plays a role in the innate immunity against intracellular pathogens. Required for resistance to M.tuberculosis and L.monocytogenes. Promotes apoptosis of infected cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185, ECO:0000255|PROSITE-ProRule:PRU00747}.
Interaction partners:
Sequence:
MFTLTKALEKALLQHFIYMKVNIAYAINKPFPFFEALRDNSFITERMYKESLEACQNLVPLSKVVHNILTSLEQTFHPSVLLTLFSKVNLREYPSLVAIFRSFRNVGYTYEEKNRPPLTLLEDLANPAEGCSLQTLLPPPRPQISLPSHLSSAPRVCDPRATAQPIIEILDEQPSPSPRAVPLLGCIQEGKTTPVSSRDHQRKDKEDSREMPHSPSGPESVVKDDSPAANDLEMAREVPCTPANKKARRKKRPNWSNSKRRRQKKKPRQDEMMGVASPGHGVQEKLKAVSRRTLWKDDSSTNVKEVTKTQRTRMRRAQTSNSQEISKEASKTSGRKRPSTARRTTQVPEKTKNDAVDFSPTLPVTCGKAKGTLFQEKLKQGASKKCIQNEAGDWLTVKEFLNEGGRATSKDWKGVIRCNGETLRHLEQKGLLFFTSKSKPQKKGA
Protein: Probable GABA transporter 2 (Q8L4X4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the transport of GABA.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- glutamate decarboxylase
- Aluminum-activated malate transporter 8
- Aluminum-activated malate transporter 7
- Glutamate decarboxylase 3
- Glutamate decarboxylase 2
- Gamma-aminobutyrate transaminase POP2, mitochondrial
- Protein kinase PINOID 2
Sequence:
MTDPPRPDPFPVTRLDSDAGALFVLQSKGEWWHAGFHLTTAIVGPTILTLPYAFRGLGWWLGFVCLTTMGLVTFYAYYLMSKVLDHCEKSGRRHIRFRELAADVLGSGLMFYVVIFIQTAINTGIGIGAILLAGQCLDIMYSSLFPQGTLKLYEFIAMVTVVMMVLSQLPSFHSLRHINCASLLLSLGYTFLVVGACINLGLSKNAPKREYSLEHSDSGKVFSAFTSISIIAAIFGNGILPEIQATLAPPATGKMLKGLLLCYSVIFFTFYSAAISGYWVFGNNSSSNILKNLMPDEGPTLAPIVVIGLAVIFVLLQLFAIGLVYSQVAYEIMEKKSADTTKGIFSKRNLVPRLILRTLYMAFCGFMAAMLPFFGDINAVVGAFGFIPLDFVLPMLLYNMTYKPTRRSFTYWINMTIMVVFTCAGLMGAFSSIRKLVLDANKFKLFSSEVVD
Protein: Even-skipped-like1 (F1R6B2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Chordin
- Bone morphogenetic protein 2
- Sizzled
- T-box transcription factor T-A
Sequence:
MLAEDRESPVSTVAHADSDQGEEECPRISLLNGIDQSRRHRTAFTREQLTRLEQEYCKESYVSRPRRCELAAALNLPETTIKVWFQNRRMKDKRQRHSLHWPNPLDPNLCAFMVGQTAAALPYPLLPRLPIHLYSHLGMGSLSGFSTPYSATTRPVDTLHLPPSTYPWLGGLPQPALYSPVQTMHHPVGCHCPQCLQWRPDHLLKPRGGARTGLQPQTFGSASG
Protein: MOB kinase activator-like 2 (Mob as tumor suppressor protein 2) (Dmob2) (Mps one binder kinase activator-like 2) (Q8IQG1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the normal morphogenesis of a variety of polarized outgrowths including epidermal hairs, bristles, arista laterals, and dendrites.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15975907}. Nucleus {ECO:0000269|PubMed:15975907}. Note=Trc colocalizes with Mob1 to the cell periphery in wing cells and wing hairs. {ECO:0000269|PubMed:15975907}.
Interaction partners:
- Serine/threonine-protein kinase tricornered
- Serine/threonine-protein kinase Warts
- IP06473p
- Serine/threonine-protein kinase hippo
- Protein phosphatase PP2A 55 kDa regulatory subunit
- Amino acid transporter transmembrane domain-containing protein
Sequence:
MNWAISNLTGGNRVSRAILVRYSSVPLADATNDGSSTAPQTPTASTPRPSSSHSSLSSTFAATFLHASSRHIPGRAVPRQNANGQNGGKGNASGAGGGAGGGGAGGASGGTGGTGAQAAGQLSLPLDVEETVTCFCRKARRKERDGDQNSTDTKLYLEESVLERKLPEADLKALVDLPAGLDYNEWLASHTLALFEHVNLVYGTISEFCTQSGCADMTGPGNRTYLWFDEKGKKTRVAAPQYIDYVMTFTQKTVSDESIFPTKYANEFPGSFESIARKILRLQFHVIAHLYAAHFREIALLGLHTHLNLTFAHLTALHRRFNLIDEKETDVLRDLEVALRLTDDTGGCQDATSTTSSVHDHSHSGDLQHQSLQQQQQHHNSSSNSTSSAEAFHVNSQSNNGSTSASASVSLIDGDAVAPPICTQPEAGAGCKPAGSSGLLGGILGDLTSGEFGDTTRYCTSAVPQAAAAAGAGVGGTAIGATDAAALNNGAGALHLNFSNNNNNNHNLNHHHHHHHHHGHHGHHHAAQQQQQHSGLIQCNAAGGGGNATGVATGGATAAASSTTTA
Protein: Protein kinase superfamily protein (Q8GXQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVAMKKVRFVNMDPESVRFMAREINILRKLDHPNVMKLECLVTSKLSGSLYLVFEYMEHDLSGLALRPGVKFTESQIKCYMKQLLSGLEHCHSRGILHRDIKGPNLLVNNDGVLKIGDFGLANIYHPEQDQPLTSRVVTLWYRAPELLLGATEYGPGIDLWSVGCILTELFLGKPIMPGRTEVEQMHKIFKFCGSPSDDYWQKTKLPLATSFKPQQPYKRVLLETFKNLPPSALALVDKLLSLEPAKRGTASSTLSSKFFTMEPLPCNVSSLPKYPPSKELDAKVRDEEARRKKSETVKGRGPESVRRGSRDFKSTATTPEFVASGQSKDTITTKRFNPQEDSRTGLRGDRDQKGFSHTNSMIHPSITATWSKNESCRNNVVELKATRSSNVPMTGRYLSPSHKEDVAVQTTTTYVRKKNRMHCSGPLMPPGGNIEDILKDHERQIQEAVRKSRLEKSATRKNNKTCVK
Protein: Sperm-associated antigen 4 protein (Outer dense fiber-associated protein SPAG4) (SUN domain-containing protein 4) (Q9NPE6)
Organism: Homo sapiens (Human)
Function: Involved in spermatogenesis. Required for sperm head formation but not required to establish and maintain general polarity of the sperm head. Required for anchoring and organization of the manchette. Required for targeting of SUN3 and probably SYNE1 through a probable SUN1:SYNE3 LINC complex to the nuclear envelope and involved in accurate posterior sperm head localization of the complex. May anchor SUN3 the nuclear envelope. Involved in maintenance of the nuclear envelope integrity. May assist the organization and assembly of outer dense fibers (ODFs), a specific structure of the sperm tail.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O55034}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:O55034}. Nucleus envelope {ECO:0000250|UniProtKB:Q9JJF2}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9JJF2}. Note=In spermatids, it is localized in the transient manchette and in the axoneme of elongating spermatids and epididymal sperm (By similarity). Colocalized with SEPT12 at the nuclear periphery in round spermatids, at sperm neck in elongated spermatids and at midpiece regions in ejaculated spermatozoa (PubMed:25775403). {ECO:0000250|UniProtKB:O55034, ECO:0000269|PubMed:25775403}.
Interaction partners:
- Outer dense fiber protein 1
- Nesprin-1
- Nesprin-3
- Nesprin-2
- SUN domain-containing protein 5
- Protein KASH5
- Sperm-associated antigen 5
- Nesprin-4
Sequence:
MRRSSRPGSASSSRKHTPNFFSENSSMSITSEDSKGLRSAEPGPGEPEGRRARGPSCGEPALSAGVPGGTTWAGSSQQKPAPRSHNWQTACGAATVRGGASEPTGSPVVSEEPLDLLPTLDLRQEMPPPRVFKSFLSLLFQGLSVLLSLAGDVLVSMYREVCSIRFLFTAVSLLSLFLSAFWLGLLYLVSPLENEPKEMLTLSEYHERVRSQGQQLQQLQAELDKLHKEVSTVRAANSERVAKLVFQRLNEDFVRKPDYALSSVGASIDLQKTSHDYADRNTAYFWNRFSFWNYARPPTVILEPHVFPGNCWAFEGDQGQVVIQLPGRVQLSDITLQHPPPSVEHTGGANSAPRDFAVFGLQVYDETEVSLGKFTFDVEKSEIQTFHLQNDPPAAFPKVKIQILSNWGHPRFTCLYRVRAHGVRTSEGAEGSAQGPH
Protein: Acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.12) (Q86YI5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MWRVCARRAQNVAPWAGLEARWTALQEVPGTPRVTSRSGPAPARRNSVTTGYGGVRALCGWTPSSGATPRNRLLLQLLGSPGRRYYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAFKNYTLDSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL
Protein: At1g72640 (NAD(P)-binding Rossmann-fold superfamily protein) (Q6NMC1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein At2g34460
- Probable plastid-lipid-associated protein 10, chloroplastic
- Ribosome biogenesis protein BOP1 homolog
- Inactive GDSL esterase/lipase-like protein 23
- DEAD-box ATP-dependent RNA helicase 51
Sequence:
MAGTSLPSCLLSQGPSLLFSSSNQDSEANKCRIGITSGKRCLVRCFAKKKISFVDQILDYIEGGPKLRKWYGAPELRPKDGSLSGDDDEFEAEEKEDDLDGEKDVVFVTDGDSDLGQMIILQLIVKGTRVKALVKDKRKALEAFGSYVELTTGDASDERFLKKAFKGVGAVISPTEGFLSIVKSFRGVKHAVLLSQLSVYESSGGIQAMMNSKAKKLAEQDENAAISSNVPYTIIRTGKLENSPGGSQGFNFSAGAAAKGSISKEDAARICVEALSVIPPTGLIFEVTNGEEVVSDWEGQLMKVMQRQSDKK
Protein: ADP-ribosylation factor 4 (P18085)
Organism: Homo sapiens (Human)
Function: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:25673879}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
- NF-kappa-B essential modulator
- Ras-related protein Rab-11A
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- ADP-ribosylation factor 5
- Rhodopsin
- Rab11 family-interacting protein 3
- Ras-related protein Rab-8A
- ADP-ribosylation factor 1
- Rab-3A-interacting protein
Sequence:
MGLTISSLFSRLFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDRIRPLWKHYFQNTQGLIFVVDSNDRERIQEVADELQKMLLVDELRDAVLLLFANKQDLPNAMAISEMTDKLGLQSLRNRTWYVQATCATQGTGLYEGLDWLSNELSKR
Protein: Acyl-coenzyme A thioesterase 5 (Acyl-CoA thioesterase 5) (EC 3.1.2.2) (Peroxisomal acyl-coenzyme A thioester hydrolase Ic) (PTE-Ic) (Peroxisomal acyl-CoA thioesterase Ic) (Q6Q2Z6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Mainly active on medium-chain acyl-CoAs. Seems to be involved in intraperoxisomal regulation of acyl-CoA levels, but not CoASH levels. May have a function in termination of beta-oxidation of fatty acids.
Subcellular location: Peroxisome {ECO:0000269|PubMed:15007068}.
Interaction partners:
- Cytosolic acyl coenzyme A thioester hydrolase
- Acyl-coenzyme A thioesterase THEM5
- Acyl-coenzyme A thioesterase THEM4
- Acyl-coenzyme A thioesterase 2, mitochondrial
- Acyl-coenzyme A thioesterase 3
- Peroxisomal succinyl-coenzyme A thioesterase
- Acyl-coenzyme A thioesterase 1
- Fructose-1,6-bisphosphatase isozyme 2
- Fructose-1,6-bisphosphatase 1
- Very-long-chain enoyl-CoA reductase
Sequence:
MVPTVSLEPTGHSCWDEPLSIAVRGLAPEQPVTLRTALRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFWRLIKRDVQTPFVVELEVLDGHEPDGGRLLARAVHERHFMAPGVRRVPVREGRVRATLFLPPGTGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYKYDDLPKVIDILHLEYFEEAVTYLLSHPQVKGPGVGLLGISKGAELSLSMASFLKGITAAVVINGATVNVISTLYYKEESLPGLGMHLERIKVTKDGFKDIIDILNVPLEAPDQKSLIPLERSDTAFLFLVGQDDHNWKSEFYAREASKRLQAHGKEKPQIVCYPKTGHHIEPPYIPWSIAAPHSYFDKPILLGGEPRAHAMAQVDAWQRLQTFFHKHLSGDKRPSPAKL
Protein: Cytochrome c oxidase subunit 8B, mitochondrial (Cytochrome c oxidase polypeptide VIII-heart) (Cytochrome c oxidase subunit 8-1) (Cytochrome c oxidase subunit 8H) (IX) (VIIIb) (P10175)
Organism: Bos taurus (Bovine)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
Interaction partners:
- Cytochrome c oxidase subunit 7A1, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6A2, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 7B, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 6C
Sequence:
MLRLAPTVRLLQAPLRGWAVPKAHITAKPAKTPTSPKEQAIGLSVTFLSFLLPAGWVLYHLDNYKKSSAA
Protein: ESAT-6-like protein (A0A0H3LFK0)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MTINYQFGDVDAHGAMIRAQAGLLEAEHQAIVRDVLAAGDFWGGAGSVACQEFITQLGRNFQVIYEQANAHGQKVQAAGNNMAQTDSAVGSSWA