wanglab/gogpt-training-data huggingface dataset:
Protein: Protein phosphatase EYA4 (EC 3.1.3.48) (Eyes absent homolog 4) (Q9Z191)
Organism: Mus musculus (Mouse)
Function: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1. Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. May be involved in development of the eye (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99502}. Nucleus {ECO:0000250|UniProtKB:Q99502}.
Interaction partners:
- Homeobox protein SIX1
Sequence:
MEDTQDLNEQSVKKTCPEADVSEPQNSRSMEMQDLASPHALVGGSDTPGSSKLDKSGLSSTSVTTNGTGVSLLAVKTEPLHSSESTTTTGDGALDTFTGSVITSSGYSPRSAQQYSPQLYPSKPYPHILSTPAAQTMSAYAGQTQYSGMQQPAVYTAYSQTGQPYSLPAYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFSTPQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFSSSQQDYPSYTAFGQNQYAQYYSASTYGAYMTSNNTADGTSSSTSTYQLQESLQGLTSQPGEFDTVQSPSTPIKDLDDRTCRSSGSKSRGRGRKNNPSPPPDSDLERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYSFATDGFHAAASSANLCLPTGVRGGVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLTNALKSLSIISTRSNCVNVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNITYVVIGDGRDEEHAANQHNMPFWRISSHSDLLALHQALELEYL
Protein: 3-ketoacyl-CoA synthase 12 (KCS-12) (EC 2.3.1.199) (Very long-chain fatty acid condensing enzyme 12) (VLCFA condensing enzyme 12) (Q9SIB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:18465198}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Protein PROLINE CONTENT ALTERNATIVE 22
- Very-long-chain 3-oxoacyl-CoA reductase-like protein At1g24470
Sequence:
MDLLFLFFSLLLSYLFFKIWKLIDSKQDKDCYILDYQCHKPTDDRMVSTQFSGEIIYRNQNLGLTEYKFLLKAIVSSGIGEQTYAPRLVFEGREERPSLQDGISEMEEFYVDSIGKLLERNQISPKDIDILVVNVSMLSSTPSLASRIINHYKMRDDVKVFNLTGMGCSASLISVDIVKNIFKSYANKLALVATSESLSPNWYSGNNRSMILANCLFRSGGCAILLTNKRSLRKKAMFKLKCMVRTHHGAREESYNCCIQAEDEQGRVGFYLGKNLPKAATRAFVENLKVITPKILPVTELIRFMLKLLIKKIKIRQNPSKGSTNLPPGTPLKAGINFKTGIEHFCIHTGGKAVIDGIGHSLDLNEYDIEPARMTLHRFGNTSASSLWYVLAYMEAKKRLKRGDRVFMISFGAGFKCNSCVWEVVRDLTGGESKGNVWNHCIDDYPPKSILNPYLEKFGWIQDEDPDTFKVPDAFM
Protein: Putative zinc metalloprotease TRE2 (EC 3.-.-.-) (Transferrin receptor-like protein 2) (Q08693)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Metal homeostatis protein BSD2
Sequence:
MRSSYQPVSTTNFEHENAIPTASSSHNLLMSQRFDDSPPSSNDNSIETNITPPPEPPSYEFDIEDPHDDLHKRTHLQRVSIGFQEKILEPLMENIIHPLLQISKFVPDKADYYLSKIGNPFILRRFFYIIFMSFIAYYVLSSGYLFNEKASGSKGMFSQHDILFEYAKKSVDLAKFERDLEYISSMPHGSGTKGDAAIYRYIQESFDNNGLKLVKEMGYSVYSNYPGNVSISYYDNKNEKHDLELSKENFNPLSSNGKLSKVSLIYGGKGTTYDLQHLKDSKTIEDGKDYVLLLQYDKLVSQQVLIAEKFGAKAVIFISEPYGENIDVVQSKPVGLPQYSTGDASGLNWDGSPVEEKDHKFWRQTHIPTIPISTRQGKELLSRLSSGGVTVDDGNSDRSNSGKMGDVLIDVDLQTNVREKHFIPNIVGKIEGREQSDKAIIIAASRNSINFGTTYPNFGTAALLSIVQLFQEVKYKFGWKPLRNIYFISFGGTEFNYAGSSELVEQRLTPLKDEIYSLIDISQLGIPFAEKYENGKTRGELSIETHPLLKKFFNRNAHGNFDISVDNVQHYGDWTPFLANGIPVSVISSDSTRNRDTPTETSEDKFERVEKILEDEQNQQSVKDLLVYLLHISMELIDDPLLHFDIISYVEDIDERLQRLEQAYPEKLNFTSIIKGLLFWKKIGSEWASWTQGWENIVWSHGDGIEPSLLSINRWTWNKKLTNIGRRTCSPAGLPNRSFYKNVLFGPTLIQEDKSKNGGNVDFWTFPGVMDAIYDDDWKRAQEQIDLIGKVLHQSAALFVEETNDIGYK
Protein: Uncharacterized protein (A0A060VP85)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- FERM domain-containing protein
- FERM domain-containing protein
Sequence:
MLVAIEDISGQIGDNYMRDKWNNFEEKWLYWLLMTPIARKSCDPIFNIFHKLNIKDATSYVKEGERRGSLAFVRNENKADVDFNKKFGADFSEMMPYIMTENMGPDHVPVSSILRDSVPSVCLDMHEQDLKMRESEDFDAHHLLQQHLYKGRKQHRHRYSRKQLEVNKDEHEVQEIFQRTMRSRLESFKSAKMGVATPKKISKHLKKDQPQKMPNGKSTDNSKSHAYGDEDFEFSEGDSASGYEAAGGSFPMRAYRGAGIVNPAFMAEMDTMDPMPPMQQIPSWLAETEVDSSNMVPSQRAQLRLPWTPSNLRRLAPLCLSTHSNDSFLLADSPATQEGISELPPPPPPQDGQGQGIHK
Protein: Mycosin-1 (EC 3.4.21.-) (MycP1 protease) (O05461)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May play a dual role in regulation of ESX-1 secretion and virulence. Acts as a protease that cleaves EspB. Essential for ESX-1 function, required for early replication in macrophages and full virulence in mice.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10974545, ECO:0000269|PubMed:12366866}; Single-pass membrane protein {ECO:0000255}. Note=Cell wall-associated. {ECO:0000269|PubMed:10974545, ECO:0000269|PubMed:12366866}.
Interaction partners:
- ESX-1 secretion system protein EccE1
- ESX-1 secretion-associated protein EspB
- ESX-2 secretion system protein EccA2
- ESX-1 secretion system ATPase EccB1
- ESX-1 secretion-associated protein EspL
- ESX-4 secretion system ATPase EccB4
- ESX-1 secretion-associated protein EspK
Sequence:
MHRIFLITVALALLTASPASAITPPPIDPGALPPDVTGPDQPTEQRVLCASPTTLPGSGFHDPPWSNTYLGVADAHKFATGAGVTVAVIDTGVDASPRVPAEPGGDFVDQAGNGLSDCDAHGTLTASIIAGRPAPTDGFVGVAPDARLLSLRQTSEAFEPVGSQANPNDPNATPAAGSIRSLARAVVHAANLGVGVINISEAACYKVSRPIDETSLGASIDYAVNVKGVVVVVAAGNTGGDCVQNPAPDPSTPGDPRGWNNVQTVVTPAWYAPLVLSVGGIGQTGMPSSFSMHGPWVDVAAPAENIVALGDTGEPVNALQGREGPVPIAGTSFAAAYVSGLAALLRQRFPDLTPAQIIHRITATARHPGGGVDDLVGAGVIDAVAALTWDIPPGPASAPYNVRRLPPPVVEPGPDRRPITAVALVAVGLTLALGLGALARRALSRR
Protein: HXXXD-type acyl-transferase family protein (Q9SMM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Disease resistance protein RPS4B
Sequence:
MVASSEFIVTRKNPELIPPVSETPNGHYYLSNLDQNIAIIVKTLYYYKSESRTNQESYNVIKKSLSEVLVHYYPVAGRLTISPEGKIAVNCTGEGVVVVEAEANCGIDTIKEAISENRMETLEKLVYDVPGARNILEIPPVVVQVTNFKCGGFVLGLGMSHNMFDGVAAAEFLNSWCEMAKGLPLSVPPFLDRTILRSRNPPKIEFPHNEFDEIEDISDTGKIYDEEKLIYKSFLFEPEKLEKLKIMAIEENNNNKVSTFQALTGFLWKSRCEALRFKPDQRVKLLFAADGRSRFIPRLPQGYCGNGIVLTGLVTSSGELVGNPLSHSVGLVKRLVELVTDGFMRSAMDYFEVNRTRPSMNATLLITSWSKLTLHKLDFGWGEPVFSGPVGLPGREVILFLPSGDDMKSINVFLGLPTSAMEVFEELMKI
Protein: MAGE family member D2 (Q5H909)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSDTSESGAGLTRFQAEASEKDSSSMMQTLLTVTQNVEVPETPKASKATEVSKTPEAREAPATQASSTTQLTDTQVLAAENKSLAADTKKQNADPQAVTMPATETKKVSHVADTKVNTKAQETEAAPSQAPADEPEPESAAAQSQENQDTRPKVKAKKARKVKHLDGEEDGSSDQSQASGTTGGRRVSKALMASMARRASRGPIAFWARRASRTRLAAWARRALLSLRSPKARRGKARRRAAKLQSSQEPEAPPPRDVALLQGRANDLVKYLLAKDQTKIPIKRSDMLKDIIKEYTDVYPEIIERAGYSLEKVFGIQLKEIDKNDHLYILLSTLEPTDAGILGTTKDSPKLGLLMVLLSIIFMNGNRSSEAVIWEVLRKLGLRPGIHHSLFGDVKKLITDEFVKQKYLDYARVPNSNPPEYEFFWGLRSYYETSKMKVLKFACKVQKKDPKEWAAQYREAMEADLKAAAEAAAEAKARAEIRARMGIGLGSENAAGPCNWDEADIGPWAKARIQAGAEAKAKAQESGSASTGASTSTNNSASASASTSGGFSAGASLTATLTFGLFAGLGGAGASTSGSSGACGFSYK
Protein: Nucleolar protein 58 (Q9P7S7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for pre-18S rRNA processing. May bind microtubules (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 17
- Probable U3 small nucleolar RNA-associated protein 13
- Probable nucleolar complex protein 14
- U3 small nucleolar RNA-associated protein 21 homolog
- rRNA 2'-O-methyltransferase fibrillarin
- H/ACA ribonucleoprotein complex subunit cbf5
- U3 small nucleolar RNA-associated protein 10
- 13 kDa ribonucleoprotein-associated protein
- Nucleolar protein 56
- Uncharacterized WD repeat-containing protein C2E1P5.05
Sequence:
MFILTETAAGYAIFKAKDKLLKKRDALIEDLKSPEGASNLLKLQSFAKFESTVDALDNVSALVEGKVSSKLSSLLEGLSDSKSSTLVVADPKLGNAINKLPGLEFEIISDSSVQDLYRGIREHLSSLISGLAPSDLNAMSLGLSHSLSRHKLKFSPDKVDTMIVQAIALLDDLDKELNTYAMRVREWYGWHFPEMGKIIQDNLAYARVIKAMGMRTKCSETDFSDILPEEIEATLKSAAEISMGTEITEEDLDNIVMLADQVLELASYRAQLSEYLRNRMQAIAPNLTALVGELVGARLIAHAGSLMNLAKQPASTIQILGAEKALFRALKTKHSTPKYGLIYHASLVGQANSKNKGKIARVLATKAALSLRVDALSDKDTTNGNIGLENRIRVENRLRSLEGGKLLPLPTAPVQQSKVQINGTSAYSTATDAVTKDAEESQEDVEMDIVIEKKKKKSSKLKEADGESSKKEKKEKKDKKHKKSKRKSEESEDGESPKKKKKSKKSKD
Protein: Efficient mitochondria targeting-associated protein 19 (Q10255)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKVVSLRRIYSSEIYKLPTTRLHMDTLYYYYFVSHLAAALFVDLPITEWLGGSLSCLSGLRRFYLSTYEDPILLIPAPWKTALFSSELFFQVPFFIWVSLRLRKKARDPVLWVAILIYGVHAFTTTWCCMFELFAEKKWMIMSFYFPYLAIPLWMAIDMGGRLVKSCHAAKSGPSSTITSKSD
Protein: C-X-C chemokine receptor type 5 (CXC-R5) (CXCR-5) (Burkitt lymphoma receptor 1) (Monocyte-derived receptor 15) (MDR-15) (CD antigen CD185) (P32302)
Organism: Homo sapiens (Human)
Function: Cytokine receptor that binds to B-lymphocyte chemoattractant (BLC). Involved in B-cell migration into B-cell follicles of spleen and Peyer patches but not into those of mesenteric or peripheral lymph nodes. May have a regulatory function in Burkitt lymphoma (BL) lymphomagenesis and/or B-cell differentiation.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-X-C motif chemokine 13
- C-C motif chemokine 19
- Stromal cell-derived factor 1
- C-C motif chemokine 21
- C-X-C motif chemokine 10
- C-C motif chemokine 5
- C-C chemokine receptor type 7
- C-X-C motif chemokine 9
- Inducible T-cell costimulator
- C-C motif chemokine 16
Sequence:
MNYPLTLEMDLENLEDLFWELDRLDNYNDTSLVENHLCPATEGPLMASFKAVFVPVAYSLIFLLGVIGNVLVLVILERHRQTRSSTETFLFHLAVADLLLVFILPFAVAEGSVGWVLGTFLCKTVIALHKVNFYCSSLLLACIAVDRYLAIVHAVHAYRHRRLLSIHITCGTIWLVGFLLALPEILFAKVSQGHHNNSLPRCTFSQENQAETHAWFTSRFLYHVAGFLLPMLVMGWCYVGVVHRLRQAQRRPQRQKAVRVAILVTSIFFLCWSPYHIVIFLDTLARLKAVDNTCKLNGSLPVAITMCEFLGLAHCCLNPMLYTFAGVKFRSDLSRLLTKLGCTGPASLCQLFPSWRRSSLSESENATSLTTF
Protein: IL4I1 protein (Nuclear pore complex glycoprotein p62) (Nucleoporin 62kDa L homeolog) (Q91349)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
- 54 kDa nucleoporin
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup153
- Uncharacterized protein.
- Uncharacterized protein.
- Nuclear pore complex protein
- 54 kDa nucleoporin
- Nuclear pore complex protein Nup85
- Uncharacterized protein.
- Nuclear pore complex protein Nup93
Sequence:
MSGFNFGAASAGGFSFGNPKSTTTTAPTGFSFGAATAAPSGGFSFGTATPTPASTTGQTSGLFSFSNPAPSLAPTSGFSFGAQVTSTPAPSSGGLAFGANTSKLNSGVGNQPAGGTTQTSQPMGGFSFGAATTQTQPSATSVGGFSFAGGVGSTSTNVFAQPAASTGITLQSAVSTAAAPTATTSQPTSTFSFGTQPQAAPALNFGLLSSSSVLSTASTPAAAQPVAPTTGLSLNFGKPADTSAAVTSTGSTTTNTPSLSSLLGTSGPSLFSSVATSTVPSVVSTVASGLSLTSTATSTGFGMKTLASSAVPTGTLATSTASLGVKAPLAGTIVQANAVGSAAATGISTATAMTYAQLENLINKWSLELEDQEKHFLQQATQVNAWDRTLMQNGERITTLHREMEKVKLDQKRLDQELDFILSQQKELEDLLTPLEESVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKEVIEHLNTSAGPGDASNPLQQICKILNAHMDSLQWIDQNSALLQRKVEQVTKECESRRKEQERGFSIAFD
Protein: Vang-like protein (A1Z7N9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MENESVKSEHSGRSRRSRNHNNNGGGGGGGGGGGGGSVNNGYHRERDRSRHSHRSTHSSKSAKGFQRGDMAPYQTSVNMTGDGSHDGQEVIEVQILPQDENWGENTTAVTGNTSEQSISMEDINNMWHRESDKGFSFACRRYVESSFYFLLGCGAFFSPVAMVVMPYVGFFPSAFDHPEITQTVRTQLLACSEQCKGQLVSLAARLLLLAIGLWAVFMRRTSATMPRIFLYRALVLLLVTICTFAYWLFYIVQVTNGAKIVVETGGDAVDYKSLVGYATNFVDTLLFIHYVAVVLLELRHQQPCYYIKIIRSPDGVSRSYMLGQLSIQRAAVWVLQHYYVDFPIFNPYLERIPISVSKSQRNKISNSFKYYEVDGVSNSQQQSQSRAVLAANARRRDSSHNERFYEEHEYERRVKKRRARLITAAEEAFTHIKRIHNEPAPALPLDPQEAASAVFPSMARALQKYLRVTRQQPRHTFESILKHLAHCLKHDLSPRAFLEPYLTESPVMQSEKERRWVQSWSLICDEIVSRPIGNECTFQLIQNDVSLMVTVHKLPHFNLAEEVVDPKSNKFVLKLNSETSV
Protein: Serine protease HTRA2, mitochondrial (EC 3.4.21.108) (High temperature requirement protein A2) (HtrA2) (Omi stress-regulated endoprotease) (Serine protease 25) (Serine proteinase OMI) (Q9JIY5)
Organism: Mus musculus (Mouse)
Function: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis (By similarity).
Subcellular location: Mitochondrion intermembrane space. Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with BID.
Interaction partners:
- E3 ubiquitin-protein ligase XIAP
- Serine/threonine-protein kinase PINK1, mitochondrial
- Baculoviral IAP repeat-containing protein 2
- Baculoviral IAP repeat-containing protein 3
- Cytochrome c, testis-specific
- Cytochrome c, somatic
- Diablo IAP-binding mitochondrial protein
- Tumor necrosis factor receptor superfamily member 1A
- Baculoviral IAP repeat-containing protein 5
- TNF receptor-associated factor 2
Sequence:
MAALKAGRGANWSLRAWRALGGIFWRKPPLLAPDLRALLTSGTPDSQIWMTYGTPSLPAQVPEGFLASRADLTSRTPDLWARLNVGTSGSSDQEARRSPGSRRREWLAVAVGAGGAVVLLLWGWGRGLSTVLAAVPAPPPTSPRSQYNFIADVVEKTAPAVVYIEILDRHPFSGREVPISNGSGFVVASDGLIVTNAHVVADRRRVRVRLPSGDTYEAMVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQNNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVTAGISFAIPSDRLREFLHRGEKKNSWFGTSGSQRRYIGVMMLTLTPSILIELQLREPSFPDVQHGVLIHKVILGSPAHRAGLRPGDVILAIGEKLAQNAEDVYEAVRTQSQLAVRIRRGSETLTLYVTPEVTE
Protein: Pectin methylesterase inhibitor (B5TQZ3)
Organism: Triticum aestivum (Wheat)
Interaction partners:
Sequence:
MASFYAAIGFILPFLLTIEVAFLPHSTGSPAAAPSTTGSLSIEDACKQTATLYDLCMATLSPDRSTLTDDAVGLTRAAILAVQKNASETATYLSNIDEDDNINKTAQLQQCLEDCGERYEAAVEQLTDATMALDMGAYDESQVLVSAGQAEVKLCQRGCQDLPEHRSILMARNTEVDHLCNITLAIAKLIPR
Protein: Small ribosomal subunit protein eS24B (40S ribosomal protein S24-B) (RP50) (P0CX32)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
Sequence:
MSDAVTIRTRKVISNPLLARKQFVVDVLHPNRANVSKDELREKLAEVYKAEKDAVSVFGFRTQFGGGKSVGFGLVYNSVAEAKKFEPTYRLVRYGLAEKVEKASRQQRKQKKNRDKKIFGTGKRLAKKVARRNAD
Protein: Protein Cripto (Cripto, EGF-CFC family member) (Cripto-1 growth factor) (CRGF) (Epidermal growth factor-like cripto protein CR1) (Teratocarcinoma-derived growth factor 1) (P13385)
Organism: Homo sapiens (Human)
Function: GPI-anchored cell membrane protein involved in Nodal signaling. Cell-associated TDGF1 acts as a Nodal coreceptor in cis. Shedding of TDGF1 by TMEM8A modulates Nodal signaling by allowing soluble TDGF1 to act as a Nodal coreceptor on other cells. Could play a role in the determination of the epiblastic cells that subsequently give rise to the mesoderm.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18930707, ECO:0000269|PubMed:27881714}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18930707, ECO:0000269|PubMed:27881714}. Secreted {ECO:0000269|PubMed:27881714}. Note=Released from the cell membrane by GPI cleavage. {ECO:0000269|PubMed:27881714}.
Interaction partners:
- Activin receptor type-1B
- Activin receptor type-2B
- Nodal homolog
- Activin receptor type-1C
- Growth/differentiation factor 3
- Activin receptor type-2A
- Formin-like protein 1
- Left-right determination factor 2
- Embryonic growth/differentiation factor 1
- Endoplasmic reticulum chaperone BiP
Sequence:
MDCRKMARFSYSVIWIMAISKVFELGLVAGLGHQEFARPSRGYLAFRDDSIWPQEEPAIRPRSSQRVPPMGIQHSKELNRTCCLNGGTCMLGSFCACPPSFYGRNCEHDVRKENCGSVPHDTWLPKKCSLCKCWHGQLRCFPQAFLPGCDGLVMDEHLVASRTPELPPSARTTTFMLVGICLSIQSYY
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FTK8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome L complete sequence
Sequence:
MHKTYSLRESRKPTAQEIQSPPPPAASTKSKFFGKGGLAYSLRKTTAGNVGPELSRKLSKLVKIEKNVMRSMEVASVEKKDAAKTLSLWGLENDDDVSDITDKLGVIIFEMAELDDQFVDRYDQYRLTMKSIRDIEGSVQPVRDRKDKITDKIAYMKYKDPHSQKIEILEQELVRCEAETLVAEAQLSNITRSKMKAAFNYQFDAMIEHSEKIALLAGYGKALLELLDDGPVTPGETRPTYDGYEASKQIIVDAEGALNEWTLDNAQVRPSLSFKEQEYTVEEVEDEEDEYENEPLNETVINPEDMTPVS
Protein: Delta-theraphotoxin-Hm1a (Delta-TRTX-Hm1a) (Heteroscodratoxin-1) (HmTx1) (Kappa-theraphotoxin-Hm1a) (Kappa-TRTX-Hm1a) (P60992)
Organism: Heteroscodra maculata (Togo starburst tarantula) (Togo starburst baboon spider)
Function: Gating-modifier toxin that potently inhibits inactivation of the mammalian Nav1.1/SCN1A sodium channel (EC(50)=38 nM). Also moderately inhibits inactivation of Nav1.2/SCN2A (EC(50)=236 nM) and Nav1.3/SCN3A (EC(50)=220 nM) when the channels are expressed in oocytes without the beta-1 auxiliary subunit. Does not inhibit inactivation of Nav1.2/SCN2A when the channel is coexpressed with the beta-1 auxiliary subunit. When tested on Nav1.1/SCN1A channel, it enhances peak current amplitude and potently delays channel inactivation in a dose-dependent manner, leading to a large sustained current. It has no effect on the voltage-dependence of steady-state activation, and induces a depolarizing shift in the voltage dependence of inactivation. In addition, it does not modify the recovery from fast inactivation in Nav1.1/SCN1A. The binding affinity and subtype selectivity of the toxin towards Nav1.1/SCN1A channel is determined by residues within both the S1-S2 and S3-S4 loops of the domain IV voltage sensor of the channel. This toxin also weakly inhibits several subtypes of voltage-gated potassium channels. It moderately blocks Kv2.1/KCNB1 (23% inhibition at 100 nM), Kv2.2/KCNB2 (19.7% at 100 nM and 51% at 300 nM), Kv4.1/KCND1 (IC(50)=280 nM), Kv4.2/KCND2 (39% at 300 nM) and Kv4.3/KCND3 (43% at 300 nM). In vivo, intracerebroventricular injection into mice elicits convulsions, spasms, tremors and rapid death. When injected into mouse hindpaw, the toxin elicits an immediate and robust response to pain. However, intraplantar injection of toxin does not cause neurogenic inflammation or alter sensitivity to heat, indicative of a modality-specific effect on mechanosensitive neurons. In Dravet syndrome mice model, intracerebroventricular infusion of this peptide rescues mice from seizures and premature death.
Subcellular location: Secreted {ECO:0000269|PubMed:12065754, ECO:0000269|PubMed:27281198}.
Interaction partners:
Sequence:
ECRYLFGGCSSTSDCCKHLSCRSDWKYCAWDGTFS
Protein: Protocadherin gamma C3 (Protocadherin gamma subfamily C, 3) (Q91XX1)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MVAEARSSGLVSPWRTVGVLLLLAALTEASTIIHYEILEERERGFPVGNVVTDLGLDLGSLSARRLRVVSGASRRFFEVNWETGEMFVNDRLDREELCGTLPSCTVTLELVVENPLELFSAEVVVQDINDNNPSFPTGEMKLEISEALAPGTRFPLESAHDPDVGSNSLQTYELSHNEYFALRVQTREDGTKYAELVLERALDWEREPSVQLVLTALDGGTPARSATLPIRITVLDANDNAPAFNQSLYRARVREDAPPGTRVAQVLATDLDEGLNGEIVYSFGSHNRAGVRELFALDLVTGVLTIKGRLDFEDTKLHEIYIQAKDKGANPEGAHCKVLVEVVDVNDNAPEITVTSVYSPVPEDAPLGTVIALLSVTDLDAGENGLVTCEVPPGLPFSLTSSLKNYFTLKTSAALDRETMPEYNLSITARDSGIPSLSALTTVKVQVSDINDNPPQSSQSSYDVYVEENNLPGVPILNLSVWDPDAPPNARLSFFLLEPGAETGLVSRYFTINRDNGVLTTLVPLDYEDQREFQLTAHINDGGTPVLATNISVNVFVTDRNDNAPQVLYPRPGQSSVEMLPRGTAAGHVVSRVVGWDADAGHNAWLSYSLLGAPNQSLFAVGLHTGQISTARPIQDTDSPRQILTVLISDSGEPLLSTTATLTVSVTEESPEARAEFPSGSAPREQNKNLTFYLLLSLILVSVGFAVTVLGVIIFKVYKWKRSRDLYRAPVSSLYRTPGPSLHADAVRGGLMPPHLYHQVYLTTDSRRSDPLLKKPGAASPLASRQNTLRSCDPVFYRQVLGAESAPPGQQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Probable T-complex protein 1 subunit eta (TCP-1-eta) (CCT-eta) (P87153)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- T-complex protein 1 subunit alpha
- Probable T-complex protein 1 subunit theta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit zeta
- Probable T-complex protein 1 subunit beta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit epsilon
- Phosducin-like protein C2A9.09
- Probable prefoldin subunit 5
- Large ribosomal subunit protein eL36B
Sequence:
MSLGGPQIPVIVLKEGTDDSQGRGQLLSNINACVAVQDTIRTTLGPLGADKLMVDDRGEVVISNDGATIMKLLDIVHPAAKTLVDIARAQDAEVGDGTTSVVVFAGELLREARTFVEDGVSSHLIIRGYRKAAQLAVNKIKEIAIHLDLSDEGKLRDLLTKCASTAMNSKLIRSNSTFFTKMVVDAVLTLDQEDLNENMIGIKKVPGGAMEDSLLVKGVAFKKTFSYAGFEQQPKFFKNPKILCLDVELELKAEKDNAEVRVDKVQEYQNIVDAEWRIIFSKLEAIVATGAKVVLSKLPIGDLATQYFADRDIFCAGRVAADDLNRVVQAVGGSIQSTCSNIEEKHLGTCDTFEERQIGGDRFNLFEGCPKAKTCTLILRGGADQFIAEVERSLHDAIMIVKHALKNNLVVAGGGACEMELSKYLRDYSLTISGKQQNFIAAFARSLEVIPRQLCDNAGFDSTNILNKLRMQHAKGEMWAGVDMDSEGVANNFEKFVWEPSTVKSNAILSATEAATLILSVDETIKNEPSQQPQAPQGALPPGAANRIMRGRGRGMPR
Protein: ORF483 (Ribosomal protein S2) (Q35316)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MKKTNQIKLFLEKPTPTLRSVSFLFGGILPHWRRVEELGSIPFIRDVAKKTDSTKYAMPALLLTTSISGNGKPEMTILSMVYTKLLCTNAHLGGRRVDAHHFNVYICGSRSGIAILDSDKTLICLRTALHFIGSPIRKKCRSFLLKTNHLFRCEILEKMASCINDSQWKIGTFFSNYLAKKKKFRLRTKKINFGLNQQPDCAVILNADRKSSVILEAARSQIPIAFLVDSTIPGESHKRITYPIPANDPIQFVYLFRHSVTKTGILERKSVHEPMQTGLKAVDSLVPIGRGRRELIIGGRKTSICSATSRVTKTRSIYTAADSELFLAVLPFLSEMPEQVVSTVEPFLSTIPEQVVPTYIPQMQNFIGETTTSLPQLQGEAGPSNSTGGGAAPSSSIYLAYAAEHASFLKAISEELYRRVGEQINLKSPLDEENIRNIVYKIMNDDFELFFDPIEDLKDWLQFIKANPLSFQDLIQFWMALAK
Protein: Uncoordinated 115a, isoform C (E1JIH2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYILIYISIPKHPQTDKTRPIYPSTLGTELRTELGKQKIYCAKCTKKCSGEVLRVADNHFHKACFQCCQCKKSLATGGFFTKDNAYYCIPDYQRLYGTKCANCQQYVEGEVVSTMGKTYHQKCFTCSKCKQPFKSGSKVTNTGKEVLCEQCVTGAPVSPSRQATGGGVSSPAPPAESPTRATAHQQHGSVISHKAHLKEDYDPNDCAGCGELLKEGQALVALDRQWHVSCFRCKACQAVLNGEYMGKDAVPYCEKCYQKGFGVKCAYCSRFISGKVLQAGDNHHFHPTCARCTKCGDPFGDGEEMYLQGSAIWHPRCGPGPSESGIILNGGGGTSSVVGGASNGNFTDTECDRMSSSALSEMYIRSRTPSFNGSLYSSSRKHYRTVSPGLILREYGRPNAEDISRIYTYSYLTDAPHYLRKPIDPYDKTPLSPHFHRPSSYATTASNAGSVAGSRPPSRPHSRTRSAMKVLVDAIRSETPRPKSPGMNNEEPIELSHYPAAKKPPPGEQPKIERDDFPAPPYPYTDPERRRRYSDTYKGVPASDDEDENVENGKPNGKVKNGEEQQRLQREAEQLEKLNSGIGSAIAKDLKEHAKYRKWKQNNLDPRNASRTPSASKEPLYKLRYESPIGASPSRNLDHQKPFYEDEMFDRSTSYRGSLGKSLGNAPSYNAIHSYRSPPKPGYGFKTTTLPYIRNGFSSDFSYGGLGDKTHSTDLSCGKSEASVDSITEGDRRALMGGDLPASSTYSGALSYHYPQAGLIRRSLPNMSHSMLVHEPAKIYPYHLLLITNYRLPSDVDRCNLERHLSDIEFEHILQCARSEFYRLPQWRRNELKRRVKLF
Protein: Acetyl-CoA carboxylase alpha (A0A0C4DGT1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLSDLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEK