wanglab/gogpt-training-data huggingface dataset:
Protein: Thioredoxin-like protein HCF164, chloroplastic (Protein HIGH CHLOROPHYLL FLUORESCENCE 164) (O23166)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-disulfide oxidoreductase that participates in various redox reactions in the chloroplast. Mediates the reduction of PSI-N in the thylakoid lumen. May interact and probably reduce other target proteins of the thylakoid membrane, such as FTSH2, FTSH8, LHCB5, atpA, atpB, atpE, petA and petC. Involved in the biogenesis of the plastid cytochrome b6f complex. Reducing equivalents are provided by stromal M-type thioredoxins and probably transduced through the thylakoid membrane by CCDA. Possesses low insulin disulfide bonds reducing activity.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:11701887, ECO:0000269|PubMed:16997915}; Peripheral membrane protein {ECO:0000269|PubMed:11701887, ECO:0000269|PubMed:16997915}; Lumenal side {ECO:0000269|PubMed:11701887, ECO:0000269|PubMed:16997915}.
Interaction partners:
- Cytochrome c-type biogenesis ccda-like chloroplastic protein
- Thiol-disulfide oxidoreductase LTO1
- AT4g31560
- Protein SUPPRESSOR OF QUENCHING 1, chloroplastic
- Cytochrome c biogenesis protein CCS1, chloroplastic
- Serine/threonine-protein kinase STN7, chloroplastic
- Thioredoxin-like protein CDSP32, chloroplastic
- Violaxanthin de-epoxidase, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic
- Thylakoid lumenal 17.4 kDa protein, chloroplastic
Sequence:
MARLVFSLNLPSSHGFNLSPRNLQSFFVTQTGAPRFRAVRCKPNPESSETKQEKLVIDNGETSSASKEVESSSSVADSSSSSSSGFPESPNKDINRRVAAVTVIAALSLFVSTRLDFGISLKDLTASALPYEEALSNGKPTVVEFYADWCEVCRELAPDVYKIEQQYKDKVNFVMLNVDNTKWEQELDEFGVEGIPHFAFLDREGNEEGNVVGRLPRQYLVENVNALAAGKQSIPYARAVGQYSSSESRKVHQVTDPLSHG
Protein: Monocarboxylate transporter 4 (MCT 4) (Solute carrier family 16 member 3) (O15427)
Organism: Homo sapiens (Human)
Function: Proton-dependent transporter of monocarboxylates such as L-lactate and pyruvate. Plays a predominant role in L-lactate efflux from highly glycolytic cells (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10921872, ECO:0000269|PubMed:11101640, ECO:0000269|PubMed:15505343, ECO:0000269|PubMed:23935841}; Multi-pass membrane protein. Basolateral cell membrane {ECO:0000269|PubMed:21199217}; Multi-pass membrane protein {ECO:0000255}. Note=Plasma membrane localization is dependent upon the BSG/MCT4 interaction (PubMed:10921872). Basolateral sorting signals (BLSS) in C-terminal cytoplasmic tail ensure its basolateral expression in polarised epithelial cells (PubMed:21199217). {ECO:0000269|PubMed:10921872, ECO:0000269|PubMed:21199217}.
Interaction partners:
- Basigin
- Embigin
- Carbonic anhydrase 9
- E3 ubiquitin-protein ligase Hakai
- Monocarboxylate transporter 2
- L-lactate dehydrogenase A chain
- Solute carrier family 2, facilitated glucose transporter member 1
- Sialin
- Solute carrier family 2, facilitated glucose transporter member 3
- CD44 antigen
Sequence:
MGGAVVDEGPTGVKAPDGGWGWAVLFGCFVITGFSYAFPKAVSVFFKELIQEFGIGYSDTAWISSILLAMLYGTGPLCSVCVNRFGCRPVMLVGGLFASLGMVAASFCRSIIQVYLTTGVITGLGLALNFQPSLIMLNRYFSKRRPMANGLAAAGSPVFLCALSPLGQLLQDRYGWRGGFLILGGLLLNCCVCAALMRPLVVTAQPGSGPPRPSRRLLDLSVFRDRGFVLYAVAASVMVLGLFVPPVFVVSYAKDLGVPDTKAAFLLTILGFIDIFARPAAGFVAGLGKVRPYSVYLFSFSMFFNGLADLAGSTAGDYGGLVVFCIFFGISYGMVGALQFEVLMAIVGTHKFSSAIGLVLLMEAVAVLVGPPSGGKLLDATHVYMYVFILAGAEVLTSSLILLLGNFFCIRKKPKEPQPEVAAAEEEKLHKPPADSGVDLREVEHFLKAEPEKNGEVVHTPETSV
Protein: Colicin-E7 (EC 3.1.-.-) (Q47112)
Organism: Escherichia coli
Function: This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity.
Interaction partners:
Sequence:
MSGGDGRGHNSGAHNTGGNINGGPTGLGGNGGASDGSGWSSENNPWGGGSGSGVHWGGGSGHGNGGGNSNSGGGSNSSVAAPMAFGFPALAAPGAGTLGISVSGEALSAAIADIFAALKGPFKFSAWGIALYGILPSEIAKDDPNMMSKIVTSLPAETVTNVQVSTLPLDQATVSVTKRVTDVVKDTRQHIAVVAGVPMSVPVVNAKPTRTPGVFHASFPGVPSLTVSTVKGLPVSTTLPRGITEDKGRTAVPAGFTFGGGSHEAVIRFPKESGQKPVYVSVTDVLTPAQVKQRQDEEKRLQQEWNDAHPVEVAERNYEQARAELNQANKDVARNQERQAKAVQVYNSRKSELDAANKTLADAKAEIKQFERFAREPMAAGHRMWQMAGLKAQRAQTDVNNKKAAFDAAAKEKSDADVALSSALERRKQKENKEKDAKAKLDKESKRNKPGKATGKGKPVNNKWLNNAGKDLGSPVPDRIANKLRDKEFKSFDDFRKKFWEEVSKDPELSKQFSRNNNDRMKVGKAPKTRTQDVSGKRTSFELHHEKPISQNGGVYDMDNISVVTPKRHIDIHRGK
Protein: Protein RESISTANCE TO POWDERY MILDEW 8.1 (AtRPW8.1) (Q9C5Z7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Disease resistance (R) protein that induces localized, salicylic acid-dependent defenses. Confers resistance to powdery mildew (e.g. Erysiphe cichoracearum UCSC1).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPIGELAIGAVLGVGAQAIYDRFRKARDISFVHRLCATILSIEPFLVQIDKRSKVEGSPLREVNERLTCFLELAYVFVEAYPKLRRRQVLRKYRYIKAIETIELALRSIIVVDFQVDQWDDIKEIKAKISEMDTKLAEVISACSKIRA
Protein: DNA dC->dU-editing enzyme APOBEC-3F (EC 3.5.4.38) (Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F) (A3F) (Q8IUX4)
Organism: Homo sapiens (Human)
Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against viruse such as HIV-1 or HIV-2. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity also against hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:21835787}. Cytoplasm, P-body {ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:22915799}.
Interaction partners:
- Cullin-5
- Core-binding factor subunit beta
- DNA dC->dU-editing enzyme APOBEC-3G
- Elongin-B
- Elongin-C
- RING-box protein 2
- APOBEC1 complementation factor
- Cytidine deaminase
- Cytochrome c oxidase subunit 5A, mitochondrial
- Putative C->U-editing enzyme APOBEC-4
Sequence:
MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPRLDAKIFRGQVYSQPEHHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLAEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDDEEFAYCWENFVYSEGQPFMPWYKFDDNYAFLHRTLKEILRNPMEAMYPHIFYFHFKNLRKAYGRNESWLCFTMEVVKHHSPVSWKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLYYFWDTDYQEGLRSLSQEGASVEIMGYKDFKYCWENFVYNDDEPFKPWKGLKYNFLFLDSKLQEILE
Protein: 4a-hydroxytetrahydrobiopterin dehydratase (EC 4.2.1.96) (4-alpha-hydroxy-tetrahydropterin dehydratase) (Q384W7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pteridine reductase, putative
Sequence:
MFSSISPVVETMRRCVYYCMRPQPLSFPAISRALLKLPEWRVDGNNSGIIHREFTFKDFSDAIKFMNAVAVECEAAGHHPTWENKYNKVSVRLTTHDAGNRVTQKDIDLALKMNEAFERTLTNN
Protein: Gamma-aminobutyric acid type A receptor subunit gamma2 (F1RDP2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit beta-4 isoform X1
- Gamma-aminobutyric acid type A receptor beta3 subunit
- Gamma-aminobutyric acid type A receptor beta2 subunit a
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid type A receptor beta2 subunit
- Gamma-aminobutyric acid receptor subunit alpha-5
- Sodium channel regulatory subunit beta-3
- Sodium channel protein
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid type A receptor alpha2 subunit
Sequence:
MVMMASLHFSSKCLNAMAIPAVTLKLFLWAFLIAHLPLSSVQLESDDDEVTNKTWVLTPKVYESDVTHILNSLLDGYDNKLRPDIGVKPTVIHTDMFVNSIGPVNAINMEYTIDIFFAQTWYDRRLKFNSTMKVLRLNSNMVGKIWIPDTFFRNSKKADAHWITTPNRMLRIWNDGRILYTLRLTIDAECQLKLNNFPMDEHSCPLEFSSYGYPKEEIVYKWKRSSVEVGDIRSWRLYQFSFVGLRNTSEVVRTVSGDYVVLTVFFDLSRRMGYFTIQTYIPCTLIVVLSWVSFWINKDAVPARTSLGITTVLTMTTLSTIARKSLPKVSYVTAMDLFVSVCFIFVFAALIEYGTLHYFVSNRKPSKKSDKKKKNPLLRLFSSKQAPTVDIRPRSATAIQMNNATQMQERDEEYGYECLDGKDCTSFFCCFEDCRSGAWRHGRLHIRVAKIDSYARIFFPTAFGLFNVVYWFSYLYL
Protein: Glutamate receptor interacting protein 2 (E0CYS1)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLAVSLKWRLGVVRRRPKDDGPYSKGGKDTAGADGALVCRRQSIPEEFRGITMVELIKREGSTLGLTISGGTDKDGKPRVSNLRPGGLAARSDLLNVGDYIRSVNGIHLTRLRHDEIITLLKNVGERVVLELPKTTQGSFPRRWTSPSTRKATALALSSEEVPMRTCTNPAHWS
Protein: tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (Kinase-associated endopeptidase 1) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein KAE1) (tRNA threonylcarbamoyladenosine biosynthesis protein KAE1) (P36132)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. KAE1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16874308}.
Interaction partners:
- EKC/KEOPS complex subunit GON7
- EKC/KEOPS complex subunit BUD32
- EKC/KEOPS complex subunit PCC1
- EKC/KEOPS complex subunit CGI121
- Threonylcarbamoyl-AMP synthase
- tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
- Cell division control protein 13
Sequence:
MVNLNTIPPKNGRDYYIALGLEGSANKLGVGIVKHPLLPKHANSDLSYDCEAEMLSNIRDTYVTPPGEGFLPRDTARHHRNWCIRLIKQALAEADIKSPTLDIDVICFTKGPGMGAPLHSVVIAARTCSLLWDVPLVGVNHCIGHIEMGREITKAQNPVVLYVSGGNTQVIAYSEKRYRIFGETLDIAIGNCLDRFARTLKIPNEPSPGYNIEQLAKKAPHKENLVELPYTVKGMDLSMSGILASIDLLAKDLFKGNKKNKILFDKTTGEQKVTVEDLCYSLQENLFAMLVEITERAMAHVNSNQVLIVGGVGCNVRLQEMMAQMCKDRANGQVHATDNRFCIDNGVMIAQAGLLEYRMGGIVKDFSETVVTQKFRTDEVYAAWRD
Protein: Hydrogen peroxide stress regulator 1 (Q10076)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transcription factor that globally supports gene expression in response to hydrogen peroxide.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mitogen-activated protein kinase spk1
- Transcription factor prr1
- Protein lsd90
- Extender of the chronological lifespan protein 1
- Zinc finger protein rsv2
- Importin subunit beta-3
Sequence:
MVFFPEAMPLVTLSERMVPQVNTSPFAPAQSSSPLPSNSCREYSLPSHPSTHNSSVAYVDSQDNKPPLVSTLHFSLAPSLSPSSAQSHNTALITEPLTSFIGGTSQYPSASFSTSQHPSQVYNDGSTLNSNNTTQQLNNNNGFQPPPQNPGISKSRIAQYHQPSQTYDDTVDSSFYDWYKAGAQHNLAPPQSSHTEASQGYMYSTNTAHDATDIPSSFNFYNTQASTAPNPQEINYQWSHEYRPHTQYQNNLLRAQPNVNCENFPTTVPNYPFQQPSYNPNALVPSYTTLVSQLPPSPCLTVSSGPLSTASSIPSNCSCPSVKSSGPSYHAEQEVNVNSYNGGIPSTSYNDTPQQSVTGSYNSGETMSTYLNQTNTSGRSPNSMEATEQIGTIGTDGSMKRRKRRQPSNRKTSVPRSPGGKSFVCPECSKKFKRSEHLRRHIRSLHTSEKPFVCICGKRFSRRDNLRQHERLHVNASPRLACFFQPSGYYSSGAPGAPVQPQKPIEDLNKIPINQGMDSSQIENTNLMLSSQRPLSQQIVPEIAAYPNSIRPELLSKLPVQTPNQKMPLMNPMHQYQPYPSS
Protein: POU domain protein (A0A1C7CYV8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MDPGAGSETSLTVNEQVIVMSGHETIRVLEVGVDAQLPAEEESKGLEGVAAEGSQSGDPAEASQAAGEAGPDNLGSSAEATVKSPPGIPPSPATAIATFSQAPSQPQASQTLTPLAVQAAPQVLTQENLATVLTGVMVPAGAVTQPLLIPISIAGQVAGQQGLAVWTIPTATVAALPGLTAASPTGGVFKPPLAGLQAAAVLNTALPAPVQAAAPVQASSTAQPRPPAQPQTLFQTQPLLQTTPAILPQPTAATAAAPTPKPVDTPPQITVQPAGFAFSPGIISAASLGGQTQILGSLTTAPVITSAIPSMPGISSQILTNAQGQVIGTLPWVVNSASVAAPAPAQSLQVQAVTPQLLLNAQGQVIATLASSPLPPPVAVRKPSTPESPAKSEVQPIQPTPTVPQPAVVIASPAPAAKPSASAPIPITCSETPTVSQLVSKPHTPSLDEDGINLEEIREFAKNFKIRRLSLGLTQTQVGQALTATEGPAYSQSAICRFEKLDITPKSAQKLKPVLEKWLNEAELRNQEGQQNLMEFVGGEPSKKRKRRTSFTPQAIEALNAYFEKNPLPTGQEITEIAKELNYDREVVRVWFCNRRQTLKNTSKLNVFQIP
Protein: Modulator of smoothened protein (Attenuator of hedgehog) (Q8C784)
Organism: Mus musculus (Mouse)
Function: Acts as a negative regulator of hedgehog signaling probably by promoting internalization and subsequent degradation of smoothened protein (SMO) present in the ciliary membrane. Plays a role in sonic hedgehog (SHH)-induced spinal neural progenitor cells differentiation.
Subcellular location: Cell projection, cilium membrane {ECO:0000269|PubMed:29290584}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:29290584}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein smoothened
- E3 ubiquitin ligase Rnf157
Sequence:
MDKLTIISGCLFLAADIFAIASIANPDWINTGESAGALTVGLVRQCQTIHGRDRTCIPPRLPPEWVTTLFFIIMGIISLTVTCGLLVASHWRREATKYARWIAFTGMILFCMAALIFPIGFYINEVGGQPYKLPNNTVVGSSYVLFVLSIFFTIVGLLFAGKVCLPG
Protein: Vesicular-fusion protein sec18 (Q9P7Q4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable vesicular-fusion protein sec17 homolog
- Syntaxin-like protein psy1
- Protein sly1
- Protein transport protein sec22
- Protein transport protein sec9
- Syntaxin pep12
- Protein transport protein bos1
- Integral membrane protein sed5
- Protein transport protein sec20
- Synaptobrevin homolog ykt6
Sequence:
MDSRWKLPFMSNKGTPEQPMRKPLSGSYSHNSAGPTPNMSPFEQKPPLPTHMDVRRPSGPFRIVKATSTEDALTNCIIVSPMDFKQQYIIVDNSRVFSTKPVPGFPQGCLGASQPHREWASWSLNQQVHVADYDPYGPHGAPYLHSMTLEVDFQNRNRTTNEPFDGEEMAKLFCSSYQSQVFSPGQKIVFDFRSYNIKATVRTISCVDLLIGENQDAENTADTSKRGLLTSQTEIQFFKAAHSALRLKASMTRPASNAILQPGFKFEDMGIGGLDSEFSAIFRRAFASRLFPPGMVEKLGINHVKGILLYGPPGTGKTLIARQIGKMLNAREPKIVNGPEILNKYVGQSEENVRKLFADAEREYRDRGEESGLHIIIFDELDAICKKRGSSGGDTGVGDQVVNQLLAKMDGVDQLNNILVIGMTNRKDMIDEALLRPGRLEVHMEISLPDEHGRLQILKIHTSRMASNGILENDVDMEELASLTKNFSGAEIAGLIKSASSFAFYRHIKVGTTAAVSGNLENIKVNRNDFLNALSEVRPAYGVSEEELESRVQGGIINFGKHIEEIITEGKLFVQQVKNSERTRLVSVLLSGPIASGKTALAATIALGSEFPFVKLVSAESMVGMNENARVAHVNRVFEDSYKSPLSVIVVDEIERIIDWVPIGPRFSNTLLQTLMVLFKKQPPKGHRLLILATTSERTMLSRMDMTQSFDAEIAVPNVSNVTELDRIIQSIDSFADSNVRADTLQRLQNFTGTDAVNVGVAKILMIAETAKQDVDVVSCFVEAMARAIPME
Protein: DNA-dependent ATPase MGS1 (Maintenance of genome stability protein 1) (P40151)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the maintenance of proper DNA topology and chromosome integrity via annealing of single-stranded DNA breaks. Modulates DNA polymerase delta during replication or replication-associated repair. May function as a modulator for SGS1 when DNA is damaged.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- ATP-dependent helicase SGS1
- Postreplication repair E3 ubiquitin-protein ligase RAD18
- DNA polymerase delta small subunit
- DNA repair protein RAD5
- ATP-dependent DNA helicase SRS2
- DNA replication ATP-dependent helicase/nuclease DNA2
- Proliferating cell nuclear antigen
- DNA polymerase eta
- DNA polymerase zeta catalytic subunit
- Ubiquitin-conjugating enzyme E2 2
Sequence:
MSNKRTSVEQLISCPICSRKVFFSLINSHLDICGKEKSKPSSRPQTVSSLLAGPKKRKQANSEKFIDLENKDHEIKPGLKSESDDIEIVENESKRFKAAPSTDFAKSIVEPASSRDQLHNDYESRWLQKISHLPLSEKLRPKELRDYVGQQHILSQDNGTLFKYIKQGTIPSMILWGPPGVGKTSLARLLTKTATTSSNESNVGSRYFMIETSATKANTQELRGIFEKSKKEYQLTKRRTVLFIDEIHRFNKVQQDLLLPHVENGDIILIGATTENPSFQLNNALISRCLIFVLEKLNVNELCIVLSRGIALLNKCRKQVWNIENPLKLSRSILEYVVDLSVGDTRRALNMLEMIEVSTRERKADEEELSIDDVRDIIKNNSSNGLNTYYDPKGDNHYDTISAFHKSIRGGDENASLYYLARMLQGGEDPLYVARRMIRIASEDIGLRDSSLLPLAVAAHDAVMKVGLPEADLALAQCCVALARAPKSVELYRAWKKLRAMMSENMYSLASSEIPMHIRNAPTKLMEELGYHKGYKYNPDYIEGKVQQDYFPKEVLEKCPNKTDLKFLDGKHLGDKEDPDLRQSYQG
Protein: Kinetochore-associated protein DSN1 homolog (Q9H410)
Organism: Homo sapiens (Human)
Function: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}. Note=Associated with the kinetochore. {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.
Interaction partners:
- Protein MIS12 homolog
- Kinetochore-associated protein NSL1 homolog
- Polyamine-modulated factor 1
- Outer kinetochore KNL1 complex subunit ZWINT
- PMF1-BGLAP readthrough
- Outer kinetochore KNL1 complex subunit KNL1
- Centromere protein C
- Kinetochore protein Spc24
- Kinetochore protein Nuf2
- Kinetochore protein NDC80 homolog
Sequence:
MTSVTRSEIIDEKGPVMSKTHDHQLESSLSPVEVFAKTSASLEMNQGVSEERIHLGSSPKKGGNCDLSHQERLQSKSLHLSPQEQSASYQDRRQSWRRASMKETNRRKSLHPIHQGITELSRSISVDLAESKRLGCLLLSSFQFSIQKLEPFLRDTKGFSLESFRAKASSLSEELKHFADGLETDGTLQKCFEDSNGKASDFSLEASVAEMKEYITKFSLERQTWDQLLLHYQQEAKEILSRGSTEAKITEVKVEPMTYLGSSQNEVLNTKPDYQKILQNQSKVFDCMELVMDELQGSVKQLQAFMDESTQCFQKVSVQLGKRSMQQLDPSPARKLLKLQLQNPPAIHGSGSGSCQ
Protein: GH15905p (Q95SL6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRILYENKVICSGALISTRLVLTSALCFPRTLRQPPPRSYKLQASRSRIYSVANLITGAIEDMALLLLHAPLEDPFVHPIDLCESPLRRNDNVTMYMSQQHLRFLRTKLIPNSNCKRSYAQDENAFITQTMLCALNSNRLVDCQTAKGDVLLHQDRLCGVDIYGQHCSDGGVNGELYADVFKARTELMHLIERYSN
Protein: Spore protein YabP (P37558)
Organism: Bacillus subtilis (strain 168)
Function: Required for sporulation.
Subcellular location: Forespore outer membrane {ECO:0000269|PubMed:15231775}. Note=Forms a ring around the forespore.
Interaction partners:
- Spore protein YabQ
- Probable sporulation protein YtaF
- Stage V sporulation protein T
- Uncharacterized protein YqfD
- Cell division protein DivIC
- Sporulation integral membrane protein YlbJ
- Stage V sporulation protein AF
- Stage IV sporulation protein A
- Stage III sporulation protein D
- Stage II sporulation protein R
Sequence:
MNSYYDQKGSSSVPEQHDVTMKGRKHLDISGVKHVESFDNEEFLLETVMGMLSVRGQNLQMKNLDVEKGIVSIKGRVFDLVYLDEQQGDKAKGFFSKLFK
Protein: Ookinete surface protein P25 (Q7KQL2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Sortilin
Sequence:
MNKLYSLFLFLFIQLSIKYNNAKVTVDTVCKRGFLIQMSGHLECKCENDLVLVNEETCEEKVLKCDEKTVNKPCGDFSKCIKIDGNPVSYACKCNLGYDMVNNVCIPNECKNVTCGNGKCILDTSNPVKTGVCSCNIGKVPNVQDQNKCSKDGETKCSLKCLKENETCKAVDGIYKCDCKDGFIIDNESSICTAFSAYNILNLSIMFILFSVCFFIM
Protein: Myosin-binding protein C, slow-type (Slow MyBP-C) (C-protein, skeletal muscle slow isoform) (Q63518)
Organism: Rattus norvegicus (Rat)
Function: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. Slow skeletal protein that binds to both myosin and actin. In vitro, binds to native thin filaments and modifies the activity of actin-activated myosin ATPase. May modulate muscle contraction or may play a more structural role.
Interaction partners:
Sequence:
EEIVPGPKSRYRIKVEGKKHTLIIEGATKADSAEYSVMTTGGQSSAKLSVDLRPLKITTPLTDQTVKLGKEVCLKCEISENVPGKWTKNGLPVQEGERLKVVHKGRIHKLVIANALIEDEGEYVFTPDAITVPLVCQIHVIDPPKIILDGLEADNTVTVIAGSKLRLEIPVTGEPPPKAIWSRADKAIMEGSGRIRAESYPDSSTLVIDVAERDDSGVYNINLKNEAGEAHASIKLRLWISLILRLAPNVTEVGDDWCIMNWEPPVYDGGSPILGYFIERKKKQSSRWMRLNFDLCKETTFEPKKMIEGVAYEVRIFAVNAIGISKPSMPSKPFVPLAVTSPPTLLAVDSVTDSSVTMKWRPPDQIGAAGLSGYVLEYCFEGSTSAKQSNENGEAANDLPAEDWSLQTQTGSTRPKFTITGLPTDAKIFVRVKAINAAGASETKYYSQPILVKEIIEPPKIRIPRHLKQTYIRRVGEAVNLVIPFQGKPRPELTWKKDGAEIDKNQINIRNSETDTIIFIRKAERSHSGKYDLEVKVDKYVENASIDIQIVDRPGPPQAVTIEDVWGENVALTWTPPKDDGNAAITGYTIQKADKKSMEWFAVIEHYHRTNATITELVIGN
Protein: Serine/threonine-protein phosphatase 5 (PP5) (EC 3.1.3.16) (Protein phosphatase T) (PP-T) (PPT) (P53041)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function (By similarity). Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1 (By similarity). Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2 (By similarity). Dephosphorylate FNIP1, disrupting interaction with HSP90AA1/Hsp90.
Subcellular location: Nucleus {ECO:0000269|PubMed:15383005}. Cytoplasm {ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:19948726}. Cell membrane {ECO:0000269|PubMed:19948726}. Note=Predominantly nuclear (PubMed:15383005). But also present in the cytoplasm (PubMed:15383005). Translocates from the cytoplasm to the plasma membrane in a RAC1-dependent manner (PubMed:19948726). {ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:19948726}.
Interaction partners:
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Hsp90 co-chaperone Cdc37
- Prostaglandin E synthase 3
- Serine/threonine-protein kinase B-raf
- Mitogen-activated protein kinase kinase kinase 5
- Stress-induced-phosphoprotein 1
- Hamartin
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit theta
Sequence:
MAMAEGERTECAEPPRDEPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQKAFERAIAGDEHKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM