wanglab/gogpt-training-data huggingface dataset:
Protein: Nanos homolog 2 (NOS-2) (P60322)
Organism: Mus musculus (Mouse)
Function: Plays a key role in the sexual differentiation of germ cells by promoting the male fate but suppressing the female fate. Represses the female fate pathways by suppressing meiosis, which in turn results in the promotion of the male fate. Maintains the suppression of meiosis by preventing STRA8 expression, which is required for premeiotic DNA replication, after CYP26B1 is decreased. Regulates the localization of the CCR4-NOT deadenylation complex to P-bodies and plays a role in recruiting the complex to trigger the degradation of mRNAs involved in meiosis. Required for the maintenance of the spermatogonial stem cell population. Not essential for the assembly of P-bodies but is required for the maintenance of their normal state.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20133598}. Cytoplasm, P-body {ECO:0000269|PubMed:20133598}. Cytoplasm, perinuclear region {ECO:0000250}. Note=More abundant in perinuclear region of the cytoplasm of the germ cells of the adult testis (By similarity). Localizes at P-bodies during gonocyte development. {ECO:0000250}.
Interaction partners:
- CCR4-NOT transcription complex subunit 1
- Stimulated by retinoic acid gene 8 protein
- Deleted in azoospermia-like
- Zinc finger and BTB domain containing 16
- Cytochrome P450 26B1
- Synaptonemal complex protein 3
- Dead end protein homolog 1
- GDNF family receptor alpha-1
- Pumilio homolog 2
- CCR4-NOT transcription complex subunit 7
Sequence:
MDLPPFDMWRDYFNLSQVVMDIIQSRKQRQEGEVAEEPNSRPQEKSEQDLEGYPGCLPTICNFCKHNGESRHVYTSHQLKTPEGVVVCPILRHYVCPLCGATGDQAHTLKYCPLNSSQQSLYRRSGRNSAGRRVKR
Protein: Protein transport protein SEC61 subunit alpha (Q9P8E3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Appears to play a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins and is essential for cell growth. It interacts with other membrane proteins required for protein translocation. Upon binding to SEC62/63 complex, secretory precursor polypeptides may engage SEC61 to begin membrane penetration event. A cycle of assembly and disassembly of SEC62/63 from SEC61 may govern the activity of the translocase (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15341916}; Multi-pass membrane protein {ECO:0000269|PubMed:15341916}.
Interaction partners:
- Translocon subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Protein transport protein Sec61 subunit beta
- Translocation protein SEC62
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Protein-transporting protein
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit delta
- Sec63 complex subunit
- Ssh1p
Sequence:
MSGFRVLDLVKPFSPFLPEVIAPERKVQFQQRVMWTIITLLIFLVMSEIPLYGIASSDSSDPLFWLRMMLASNRGTLMELGISPIVSSGMLFQLLQGTKIIHVDMQNKNDRETFQTAQKLLAILLAVGQATVYVLTGMYGPPSSLGVGVCSLLILQLVFASTIVILLDELLQKGYGLGSGVSLFTATNTCEQVFWKAFAPTTSTSAKGTEFDGAVVAMFHLLGSRKDKKRALIESFYRPNLPNMFQLLATLLVFFAVVYLQGFRIELPMKSTRQRGPYGSYPIRLFYTSNIPIMLESALASNIFIISQLLFMRWPNNLFVKLLGTWDARAGSSQLYANGGLAYYIQPPFNFTDALLDPIKTTIYIAFVLGSCAVFSTTWIEISGTSPRDVAKQFKEQGLVIAGHRDTSAYKELKKIIPIAAAFGGATIGALSVVCDLMGTLGSGTSILLAVTTIYGYYELAVKEGGFNKSIVSGFSDGI
Protein: Zinc finger protein 143 (Selenocysteine tRNA gene transcription-activating factor) (Q1LYE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the activator element (AE) motif of the selenocysteine tRNA gene promoter (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger matrin-type protein 5
- THAP domain-containing protein 11
Sequence:
MLLAQVNRDTQGMEFQSVDGDPQQVTLCLTEAVTVADDNIDGMDTVSLQAVTLVDGSTAYIQHSPKVSLTENKIMEGQVIQLEDGSAAYVQHLPMSKTGGEGLRLEDGQAVQLEDGTTAYIHAPKETYDQGGLQAVQLEDGTTAYIQHMPQSNTILAIQADGTVADLQTEGTIDAETISVLEQYSTKMEATECGTGLIGRGDSDGVHMQIVLQGQDCRSPRIQHVGEKAFRCEHEGCGKLYTTAHHLKVHERSHTGDKPYICDHLGCGKKFATGYGLKSHVRTHTGEKPYRCQELNCLKSFKTSGDLQKHTRTHTGEKPFKCPFEGCGRSFTTSNIRKVHIRTHTGERPYYCAEPNCGRAFASATNYKNHMRIHTGEKPYVCTVPGCDKRFTEYSSLYKHHVVHTPCKPYNCNHCGKTYKQISTLAMHKRTAHNDTEPIEEEQEGYFEPPAEAIDDPGLMYTPSVVDDDSGSEQVSGSEIMGQHHVALISQDGTQQVLSQADMQAMGGTITMVTQEGTTITIPAHEAMLSSGGAHSVTMVSADGTEGQVAIVTPDLAAYQTEEGELIQDQEQHEVSTSPHPVTLLATSNGTHIAVQLSDHPSLEEAIRIASRIQQGETPGMDD
Protein: Heptaprenyl diphosphate synthase component 2 (HepPP synthase subunit 2) (EC 2.5.1.30) (Spore germination protein C3) (P31114)
Organism: Bacillus subtilis (strain 168)
Function: Supplies heptaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinone menaquinone-7 (MQ-7).
Interaction partners:
- Heptaprenyl diphosphate synthase component 1
- Demethylmenaquinone methyltransferase
- Isoprenyl transferase
- Farnesyl diphosphate phosphatase YisP
- Farnesyl diphosphate synthase
- 1,4-dihydroxy-2-naphthoate octaprenyltransferase
- Nucleoside diphosphate kinase
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Chorismate synthase
Sequence:
MLNIIRLLAESLPRISDGNENTDVWVNDMKFKMAYSFLNDDIDVIERELEQTVRSDYPLLSEAGLHLLQAGGKRIRPVFVLLSGMFGDYDINKIKYVAVTLEMIHMASLVHDDVIDDAELRRGKPTIKAKWDNRIAMYTGDYMLAGSLEMMTRINEPKAHRILSQTIVEVCLGEIEQIKDKYNMEQNLRTYLRRIKRKTALLIAVSCQLGAIASGADEKIHKALYWFGYYVGMSYQIIDDILDFTSTEEELGKPVGGDLLQGNVTLPVLYALKNPALKNQLKLINSETTQEQLEPIIEEIKKTDAIEASMAVSEMYLQKAFQKLNTLPRGRARSSLAAIAKYIGKRKF
Protein: Non-histone chromosomal protein HMG-14 (High mobility group nucleosome-binding domain-containing protein 1) (P18608)
Organism: Mus musculus (Mouse)
Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2.
Subcellular location: Nucleus. Cytoplasm {ECO:0000250}. Note=Cytoplasmic enrichment upon phosphorylation. {ECO:0000250}.
Interaction partners:
- Ubiquitin-like protein FUBI
- DNA excision repair protein ERCC-6
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL6
Sequence:
MPKRKVSADGAAKAEPKRRSARLSAKPAPAKVDAKPKKAAGKDKASDKKVQIKGKRGAKGKQADVADQQTTELPAENGETENQSPASEEEKEAKSD
Protein: Transcription elongation factor SPT5 (DRB sensitivity-inducing factor large subunit) (DSIF large subunit) (Protein foggy) (Q9DDT5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May function as a component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates transcription elongation by RNA polymerase II. Probably enhances transcriptional pausing at sites proximal to the promoter, which may facilitate the assembly of an elongation competent RNA polymerase II complex. Also acts to stimulate transcriptional elongation at low nucleotide concentrations. Regulation of transcriptional elongation by this protein is required for the expression of genes which control neuronal development.
Subcellular location: Nucleus {ECO:0000269|PubMed:11099044}.
Interaction partners:
- Transcription elongation factor SPT4
- RNA polymerase-associated protein LEO1
- Transcription elongation factor SPT6
- Polymerase
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase subunit
- RTF1 homolog, Paf1/RNA polymerase II complex component.
- DNA-directed RNA polymerase II subunit RPB7
- Parafibromin
- RNA polymerase-associated protein CTR9 homolog
Sequence:
MSDSEDSDFSDNQSERSSEAEEVEENEEEEEQGSVAGSDKAEEEGEDLEDEEEYDEEEEEDDDRPRKKARHGGFILDEADVDDEYEDEDPWEDGAEDILEKEEAEVSNLDHVVLDEDHSGSRRLQNLWRDSREEALGEYYMRKYAKSSGGEHFYGGSEDLSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFVAYQCTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKAAIEGVGNLRMGFWNQQMVPIKEMTDVLKVVKEVTNLKPKSWVRLKRGLYKDDIAQVDYVEPSQNTISLKMIPRIDLDRIKARMSMKDWFAKRKKFKRPPQRLFDAEKIRSLGGEVSHDGDFMIFEANRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTETTGKEREHNLQAGDNVEVCEGELINLQGKILSVDGNKITIMPKHEDLKDPLEFPAHELRKYFRMGDHVKVIAGRYEGDTGLIVRVEENFVILFSDLTMHELKVLPRDLQLCSETASGVDAGGQHEWGELVQLDPQTVGVIVRLERETFQVLNMHGKVLTVRHQAVNRRKDNRFAVALDSEQNNIHVKDIVKVIDGPHSGREGEIRHIFRGFAFLHCKKLVENGGMFVCKARHLVLAGGSKPRDVTNFTVGGFAPMSPRISSPMHPGGGGQPQRGGGGGGGGGMGRGRGRRDNDLIGQTVRISQGPYKGYIGVVKDATESTARVELHSTCQTISVDRQRLTTVGGKERQGRSSTHLRTPMYGSQTPIYGTGSRTPMYGSQTPLHDGSRTPHYGSQTPLHDGSRTPGQSGAWDPNNPNTPSRPDDEYEFAYDDEPSPSPQGYGGTPNPQTPGYPEVPSPQVNPQYNPQTPGTPAMYNTDQYSPYAAPSPQGSYQPSPSPQSYHQVAPSPVGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSNIDQASNDWVTTDIMVRVKDTFLDGGVINQTGIIRSVTGGMCSVFLQDTEKVVSISSEHLEPVTPTKNNKVKVILGEDREATGVLLSIDGEDGIVRMELDEQLKILNLRFLGKLEV
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (K7EQL6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGHLTLEDYQIWSVKNVLANEFLNLLFQVCHIVLGLRPATPEEEGQIIRGWLERESRYGLQAGHNWFIISMQWWQQWKEYVKYDANPVVIEPSSVLNGGKYSFGTAAHPMEQVEDRIGSSLSYVNTTEEKFSDNISTASEASETAGSGFLYSATPGADVCFARQHNTSDNNNQCLLGANGNILLHLNPQKPGAIDNQPLVTQEPVKATSLTLEGGRLKRTPQLIHGRDYEMVPEPVWRALYHWYGANLALPRPVIKNSKTDIPELELFPRYLLFLRQQPATRTQQSNIWVNMGNVPSPNAPLKRVLAYTGCFSRMQTIKEIHEYLSQRLRIKEEDMRLWLYNSENYLTLLDDEDHKLEYLKIQDEQHLVIEVRNKDMSWPEEMSFIANSSKIDRHKVPTEKGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWTIAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVELKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQLRSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGTTPVRYGLRLNMDEKYTGLKKQLSDLCGLNSEQILLAEVHGSNIKNFPQDNQKVRLSVSGFLCAFEIPVPVSPISASSPTQTDFSSSPSTNEMFTLTTNGDLPRPIFIPNGMPNTVVPCGTEKNFTNGMVNGHMPSLPDSPFTGYIIAVHRKMMRTELYFLSSQKNRPSLFGMPLIVPCTVHTRKKDLYDAVWIQVSRLASPLPPQEASNHAQDCDDSMGYQYPFTLRVVQKDGNSCAWCPWYRFCRGCKIDCGEDRAFIGNAYIAVDWDPTALHLRYQTSQERVVDEHESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRDPALCQHKPLTPQGDELSEPRILAREVKKVDAQSSAGEEDVLLSKSPSSLSANIISSPKGSPSSSRKSGTSCPSSKNSSPNSSPRTLGRSKGRLRLPQIGSKNKLSSSKENLDASKENGAGQICELADALSRGHVLGGSQPELVTPQDHEVALANGFLYEHEACGNGYSNGQLGNHSEEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFYEQQGIDYAQFLPKTDGKKMADTSSMDEDFESDYKKYCVLQ
Protein: Chromatin structure-remodeling complex subunit sfh1 (RSC complex subunit sfh1) (SNF5 homolog 1) (Q9USM3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:14655046, ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SWI/SNF and RSC complexes subunit ssr1
- SWI/SNF and RSC complexes subunit ssr3
- SWI/SNF and RSC complexes subunit ssr2
- Chromatin structure-remodeling complex subunit rsc4
- Chromatin structure-remodeling complex subunit rsc1
- Chromatin structure-remodeling complex subunit rsc9
- Chromatin structure-remodeling complex subunit rsc58
- Chromatin structure-remodeling complex subunit snf21
- SWI/SNF and RSC complexes subunit arp42
- Chromatin structure-remodeling complex subunit rsc7
Sequence:
MAQACKTTYSSRLKTGNTCLIQKNVAVSTRSHSSYTGRNSLRNVPAVNYAAFEQGEDFETPVETPEKEEEKFETDDRGLAVGRPTGNNIYPRFATKTRHIYVTDEQLKCAAEERDVYIPIRLDIELPNNYRLKDTFLWNMNEQVMTPDVFAQILCADLDLSTNVYGTQISSSIRAQIEEYAPVAEVPMPKGQEMLVVFNIQVQLAQLSYNDQVEWNLTSPLTPEEFSVLTCNDLGLSGESRPEIAYAIHECLLKLKKNACEGDLPDYDSDAVPGTKAGPRQDMDTLGALWQPVLETVSLEDAKKNENNRENLVKQWRREASKFGGFAADVSAERWRAAALGNLSQSETANLPSASVSDAQTLLEQERPRWRCRWCNVLGTGTFCVRRGPEGNKSLCNACGVAYAKTGQLPYWRKSLYT
Protein: Rhophilin-2 (76 kDa RhoB effector protein) (GTP-Rho-binding protein 2) (p76RBE) (Q8IUC4)
Organism: Homo sapiens (Human)
Function: Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12473120}.
Interaction partners:
- Rho-related GTP-binding protein RhoB
- Transforming protein RhoA
Sequence:
MTDALLPAAPQPLEKENDGYFRKGCNPLAQTGRSKLQNQRAALNQQILKAVRMRTGAENLLKVATNSKVREQVRLELSFVNSDLQMLKEELEGLNISVGVYQNTEEAFTIPLIPLGLKETKDVDFAVVLKDFILEHYSEDGYLYEDEIADLMDLRQACRTPSRDEAGVELLMTYFIQLGFVESRFFPPTRQMGLLFTWYDSLTGVPVSQQNLLLEKASVLFNTGALYTQIGTRCDRQTQAGLESAIDAFQRAAGVLNYLKDTFTHTPSYDMSPAMLSVLVKMMLAQAQESVFEKISLPGIRNEFFMLVKVAQEAAKVGEVYQQLHAAMSQAPVKENIPYSWASLACVKAHHYAALAHYFTAILLIDHQVKPGTDLDHQEKCLSQLYDHMPEGLTPLATLKNDQQRRQLGKSHLRRAMAHHEESVREASLCKKLRSIEVLQKVLCAAQERSRLTYAQHQEEDDLLNLIDAPSVVAKTEQEVDIILPQFSKLTVTDFFQKLGPLSVFSANKRWTPPRSIRFTAEEGDLGFTLRGNAPVQVHFLDPYCSASVAGAREGDYIVSIQLVDCKWLTLSEVMKLLKSFGEDEIEMKVVSLLDSTSSMHNKSATYSVGMQKTYSMICLAIDDDDKTDKTKKISKKLSFLSWGTNKNRQKSASTLCLPSVGAARPQVKKKLPSPFSLLNSDSSWY
Protein: Protein STRUBBELIG-RECEPTOR FAMILY 3 (Leucine-rich repeat receptor kinase-like protein SRF3) (Q6R2K3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Not essential for epidermal patterning and not redundant with STRUBBELIG.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable disease resistance protein RPP1
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic
Sequence:
MAAKRSIYCLLLLPLLLSLLIWIPSISLAATNPDDVAAINGLFAALGAPVLPGWIASGGDPCGEAWQGIICNVSDIISITVNAANLQGELGDNLAKFTSIRGIDFSNNRIGGSIPSTLPVTLQHFFLSANQFTGSIPESLGTLSFLNDMSLNDNLLSGELPDVFQNLVGLINLDISSNNISGTLPPSMENLLTLTTLRVQNNQLSGTLDVLQGLPLQDLNIENNLFSGPIPDKLLSIPKFLHEGNPFNATMINSTSTAPSLSPSLSPTKPAPTRPFSGVPPPPNERNRGKVADGPSDSEGSSSENSKGKNSSHTKKIILIAFAGVLVFIILVLAILLLLPKCARRREHANRVFKPHQVGADRGSRENALENGTPVLPPPGRSEKVQREPFKKAGEEPKVLHDLERLRRPAPISRQESQDIDFSMLMPPPPPPPPPPPPPPLDEKVTVMPIISPERPVKKTSPKRLPLTSVKHYSIASLQQYTESFAQENLIGSGMLGSVYRARLPNGKLFAVKKLDKRASEQQQDHEFIELVNNIDMIRHSNIVELVGYCAEHDQRLLVYEYCSNGTLQDGLHSDDEFKKKLSWNTRVSMALGAARALEYLHEVCEPPIIHRNFKSANVLLDDDLSVLVSDCGLAPLISSGSVSQLSGQLLAAYGYGAPEFDSGIYTWQSDVYSFGVVMLELLTGRMSYDRDRSRGEQFLVRWAIPQLHDIDALGKMVDPSLNGQYPAKSLSHFADIISRCVQSEPEFRPLMSEVVQDLLDMIRRERHGSGDSTAD
Protein: Transcriptional regulator lacI family (Q8P5C9)
Organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Interaction partners:
- Multiphosphoryl transfer protein
- Glucose/galactose transporter
- N-acetylglucosamine-6-phosphate deacetylase
- Glucosamine-fructose-6-phosphate aminotransferase
Sequence:
MRRPTIKDVAERAKVSLKTVSRVINNEPSVMQATRARVLRAIADLDYEPDPSARNLRSGTPFVIGLVYDNPNPYHIIGIQNGVLAACRETGFGLQIHPCDSTSPLLAEELAEWVQRSRLAGVVLTAPMSERPELLAGLAARGIKSVRIIASTTDPGDGPCVYIDDRDAAYEITEHLIQLGHQRIGFLWGGPQHRSSGERYAGYEAALKDYGISLDKHLVIPGDYTFDDGFRGARRLLSLREPPTAIFGSNDEIAAGVLAAAKSTGMNVPYQLSIAGFEDSPFSRQSWPALTTAKQATEDIARHAARLLISQLRSDAYDDQPAQLQNRGFVPQLVVRGSTAPAQPPAAKSPSPESA
Protein: Evasin P1182 (G3MJ83)
Organism: Amblyomma maculatum (Gulf Coast tick)
Function: Salivary chemokine-binding protein which binds to host chemokines CCL2, CCL3, CCL4, CCL8 and CCL18.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MALNWSFRVIFVSTMWCALLKFATLGEPKDDNDYGGGCPFVVLGNGTHAKPAGCSHLCNGAPETLDNIECYNVTEEVAKRMTPGIPYACWLGWCNKGECKRGNRTEVCYRGSEEE
Protein: E3 ubiquitin-protein ligase PHF7 (EC 2.3.2.27) (PHD finger protein 7) (Testis development protein NYD-SP6) (Q9BWX1)
Organism: Homo sapiens (Human)
Function: May play a role in spermatogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11829468}.
Interaction partners:
- Transcription elongation factor A protein-like 1
Sequence:
MKTVKEKKECQRLRKSAKTRRVTQRKPSSGPVCWLCLREPGDPEKLGEFLQKDNISVHYFCLILSSKLPQRGQSNRGFHGFLPEDIKKEAARASRKICFVCKKKGAAINCQKDQCLRNFHLPCGQERGCLSQFFGEYKSFCDKHRPTQNIQHGHVGEESCILCCEDLSQQSVENIQSPCCSQAIYHRKCIQKYAHTSAKHFFKCPQCNNRKEFPQEMLRMGIHIPDRDAAWELEPGAFSDLYQRYQHCDAPICLYEQGRDSFEDEGRWCLILCATCGSHGTHRDCSSLRSNSKKWECEECSPAAATDYIPENSGDIPCCSSTFHPEEHFCRDNTLEENPGLSWTDWPEPSLLEKPESSRGRRSYSWRSKGVRITNSCKKSK
Protein: Cell cycle control protein 50A (P4-ATPase flippase complex beta subunit TMEM30A) (Transmembrane protein 30A) (Q9NV96)
Organism: Homo sapiens (Human)
Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF), synthetic drug alkylphospholipid edelfosine, and, probably in association with ATP8B1, of perifosine. Also mediates the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane. Golgi apparatus. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}. Apical cell membrane {ECO:0000250}.
Interaction partners:
- Phospholipid-transporting ATPase IC
- Phospholipid-transporting ATPase IA
- Phospholipid-transporting ATPase IG
- Phospholipid-transporting ATPase IH
- Phospholipid-transporting ATPase VB
- Phospholipid-transporting ATPase VA
- Phospholipid-transporting ATPase VD
- Phospholipid-transporting ATPase ID
- Phospholipid-transporting ATPase IF
- Phospholipid-transporting ATPase IB
Sequence:
MAMNYNAKDEVDGGPPCAPGGTAKTRRPDNTAFKQQRLPAWQPILTAGTVLPIFFIIGLIFIPIGIGIFVTSNNIREIEIDYTGTEPSSPCNKCLSPDVTPCFCTINFTLEKSFEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDSSALLNPSKECEPYRRNEDKPIAPCGAIANSMFNDTLELFLIGNDSYPIPIALKKKGIAWWTDKNVKFRNPPGGDNLEERFKGTTKPVNWLKPVYMLDSDPDNNGFINEDFIVWMRTAALPTFRKLYRLIERKSDLHPTLPAGRYSLNVTYNYPVHYFDGRKRMILSTISWMGGKNPFLGIAYIAVGSISFLLGVVLLVINHKYRNSSNTADITI
Protein: Surface protein P113 (Q8ILP3)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Membrane receptor which tethers secreted RH5 to the merozoite membrane during merozoite invasion of host erythocytes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16203726, ECO:0000269|PubMed:28186186}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:16203726}.
Interaction partners:
- High molecular weight rhoptry protein 2
Sequence:
MKIPFFILHILLLQFLLCLIRCYVHNDVIKFGEENSLKCSQGNLYVLHCEVQCLNGNNEIIHKRCNDDIEKKCNGNNKCIYFFEYELRKKTQSFRNKNSIEISECVESEQNEVKTSTTCLLSNSFILDEAFIQYFFFIKNKNEEPVICKDGNINIKSALLHSPFCEIKLKDISEYIRKKCDNNKECLIDPLDVQKNLLNEEDPCYINNSYVSVNVVCNKEEEIGDESTDSSSMEIQDSTSNEQDENVKGMSSSQEMNSNNDENKNQDNESDDDVNNNNNNNNDDQDEQGNDGDVTSSMNKNEDNKDLEHGSSNDVNNNTDTLVNNKENKEFVLKEKSSLTSKINKELAHRTALFNKLADNISLLLNKKYDSFEIKDVLEDRYNEMKRDANPDVYYIYLMDTLDIEKIEDINLEEVKMSLLASLKETMNKIDTIEKKIEEFKNKYISLYNKVKTTMPELFDLNEDLVLLYNDFPFDNGMISSDIFFKYNPSENIMDHQEMVKKGSITEDELRIVNDLEPLDNYRRRKRITELRKILVEKLRILYLEKNNLFNTQASCIKSYCYKNPLNLKTLEVLLKKNYYRLKENKDYDVVSSIIQHLDNVDANKKKKWLTHERILKKLQVLIAEGYKRINEKEKDIDRRMAVYNALYEKAQSYNLQKLFNDSNDFLKKYAIMGNSFDDGDEVFGSQSSNFNIFDSNNTDQNNEQEQPKQDDQLLNNNNDDVLSESNNENKEKTSDDATHKETQEKSDQEPSQNIQEDNSDEKHAENEENVEQIETDSNVSEEANDENKDNMQTTTDEGTEELQQNDEDAESLTKENSKSEEQENEDSTDAEAIDKEEVETEEKGKDEQKKDEQKEQDEEEDGEKENKHKSSETTNETVTDIEENKNEVKGEEHLQGSEQSIEASESSQKDETKETEDKEEYVNANDDESSEEDTTPNETNKTDNGSSFFFAMSNALLVILLLLFIEFL
Protein: Solute carrier family 22 member 23 (A1A5C7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAIDRRREAAGGGPGRQPAPAEENGSLPPGDAAASAPLGGRAGPGGGAEIQPLPPLHPGGGPHPSCCSAAAAPSLLLLDYDGSVLPFLGGLGGGYQKTLVLLTWIPALFIGFSQFSDSFLLDQPNFWCRGAGKGTELAGVTTTGRGGDMGNWTSLPTTPFATAPWEAAGNRSNSSGADGGDTPPLPSPPDKGDNASNCDCRAWDYGIRAGLVQNVVSKWDLVCDNAWKVHIAKFSLLVGLIFGYLITGCIADWVGRRPVLLFSIIFILIFGLTVALSVNVTMFSTLRFFEGFCLAGIILTLYALRIELCPPGKRFMITMVASFVAMAGQFLMPGLAALCRDWQVLQALIICPFLLMLLYWSIFPESLRWLMATQQFESAKRLILHFTQKNRMNPEGDIKGVIPELEKELSRRPKKVCIVKVVGTRNLWKNIVVLCVNSLTGYGIHHCFARSMMGHEVKVPLLENFYADYYTTASIALVSCLAMCVVVRFLGRRGGLLLFMILTALASLLQLGLLNLIGKYSQHPDSGMSDSVKDKFSIAFSIVGMFASHAVGSLSVFFCAEITPTVIRCGGLGLVLASAGFGMLTAPIIELHNQKGYFLHHIIFACCTLICIICILLLPESRDQNLPENISNGEHYTRQPLLPHKKGEQPLLLTNAELKDYSGLHDAAAAGDTLPEGATANGMKAM
Protein: Gdf11-like (Growth differentiation factor 11) (Growth/differentiation factor 11 precursor) (Q8JFP9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Serine/threonine-protein kinase receptor
- Receptor protein serine/threonine kinase
- Receptor protein serine/threonine kinase
- Serine/threonine-protein kinase receptor
- Serine/threonine-protein kinase receptor
- receptor protein serine/threonine kinase
- Serine/threonine-protein kinase receptor
- Follistatin 2
- Follistatin-A
- Serine/threonine-protein kinase receptor
Sequence:
MKRYNFLLCLTVLISLGLSGSDEPNLFLAPLSEMSSDIGVSLFDVDDVESSECSACVWREQSKVLRLETIKSQILSKLRLKQAPNISREVVNQLLPKAPPLQQLLDHHDFQGDASSLEDFIDADEYHATTESVITMASEPEPLVQVDGKPTCCFFKFSPKLMFTKVLKAQLWVYLQPLKQTSTVYLQILRLKPITEQGSRHIRIRSLKIELDSQAGHWQSIDFKHVLQNWFKQPHTNWGIDINAYDESGNDLAVTSLGPGEEGLQPFLEVKILETTKRSRRNLGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQHANPRGSAGPCCTPTKMSPINMLYFNDKQQIIHGKIPGMVVDRCGCS
Protein: Chondroadherin-like protein (E9Q7T7)
Organism: Mus musculus (Mouse)
Function: Potential negative modulator of chondrocyte differentiation. Inhibits collagen fibrillogenesis in vitro. May influence chondrocyte's differentiation by acting on its cellular collagenous microenvironment.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:25451920}.
Interaction partners:
Sequence:
MERPQSSIWVFMLLLFMVLLQSPAWHVAAQRCPQTCVCDNSRRHVTCRHQNLTEVPNTIPELTQRLDLQGNILKVLPAAAFQDLPHLTHLDLRNCQVEMVAEGAFRGLGRLLLLNLASNRLSTLPQEALDGLGSLRRLELEGNMLEELRPGTFGALGSLTTLNLAHNALVYLPAMAFQGLLRTRWLQLSHNALSVLAPEALAGLPALRRLSLHHNELQALPGAALSQARSLARLELGHNPLTYTGEEDGLALPGLRELALDHGSLQALGPRAFAHCPRLHTLDLRGNQLTTLPPLQVPGQLRRLRLQGNPLWCACHARPLLEWLVRARVRSDGACRGPRRLRGEALDTLRPSDLRCPGDAAAGDGDGDEDEDRPAGPRAPPLRSPHGEAAWATPCPPACACVAETRHSTCDGRGLQAVPRGFPNDTQLLDLRRNHFPSVPRAAFPGLRHLVSLHLQHCGVAELEPGALAGLDRLLYLYLSHNQLSGLSAAALEGAPNLGYLYLEHNRFLRIPGTALRALPTLVSLHLQDNAVDRLAPGDLAGARALRCLYLSGNHITQVSPGALGPARELEKLHLDRNRLREVPTGALEGLPALKELQLSGNPLRALPDGAFQPVGRSLQQLFLNSSDLEQISPRAFSGLGKGLRSLYLHKNQLQSLPAPLGLSGLELVDLSGNPFHCDCQLLPLHRWLTGLNLRVGATCATPPSVRGQKVKVAAPVFEACPGWTARKAKRTPTSRGSARRTPSLSRH
Protein: ETS-domain lacking (LD15796p) (MAE) (Q7K119)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ets DNA-binding protein pokkuri
- ETS-like protein pointed
Sequence:
MQVESSYTKYAGRVPPLDLTQVNGGQDLWGGNGGGNNASARRHLHHPYQMLDKCRGGVTLISASSAISSTSNSSDDNNNRLMSADDGTTSLLHPLGSDGLPLDPRDWTRADVWKWLINMAVSEGLEVTAELPQKFPMNGKALCLMSLDMYLCRVPVGGKMLYRDFRVRLARAMALLS