wanglab/gogpt-training-data huggingface dataset:
Protein: Prolyl 3-hydroxylase 3 (EC 1.14.11.7) (Leprecan-like protein 2) (Protein B) (Q8IVL6)
Organism: Homo sapiens (Human)
Function: Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. Required for normal hydroxylation of lysine residues in type I collagen chains in skin, bone, tendon, aorta and cornea. Required for normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly. Apparently not required for normal prolyl 3-hydroxylation on collagen chains, possibly because it functions redundantly with other prolyl 3-hydroxylases.
Subcellular location: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Decorin
- Regulator of microtubule dynamics protein 3
- Prolyl 3-hydroxylase 1
- Major centromere autoantigen B
- Dehydrogenase/reductase SDR family member 2, mitochondrial
- NKG2-D type II integral membrane protein
Sequence:
MLRLLRPLLLLLLLPPPGSPEPPGLTQLSPGAPPQAPDLLYADGLRAYAAGAWAPAVALLREALRSQAALGRVRLDCGASCAADPGAALPAVLLGAPEPDSGPGPTQGSWERQLLRAALRRADCLTQCAARRLGPGGAARLRVGSALRDAFRRREPYNYLQRAYYQLKKLDLAAAAAHTFFVANPMHLQMREDMAKYRRMSGVRPQSFRDLETPPHWAAYDTGLELLGRQEAGLALPRLEEALQGSLAQMESCRADCEGPEEQQGAEEEEDGAASQGGLYEAIAGHWIQVLQCRQRCVGETATRPGRSFPVPDFLPNQLRRLHEAHAQVGNLSQAIENVLSVLLFYPEDEAAKRALNQYQAQLGEPRPGLGPREDIQRFILRSLGEKRQLYYAMEHLGTSFKDPDPWTPAALIPEALREKLREDQEKRPWDHEPVKPKPLTYWKDVLLLEGVTLTQDSRQLNGSERAVLDGLLTPAECGVLLQLAKDAAGAGARSGYRGRRSPHTPHERFEGLTVLKAAQLARAGTVGSQGAKLLLEVSERVRTLTQAYFSPERPLHLSFTHLVCRSAIEGEQEQRMDLSHPVHADNCVLDPDTGECWREPPAYTYRDYSGLLYLNDDFQGGDLFFTEPNALTVTARVRPRCGRLVAFSSGVENPHGVWAVTRGRRCALALWHTWAPEHREQEWIEAKELLQESQEEEEEEEEEMPSKDPSPEPPSRRHQRVQDKTGRAPRVREEL
Protein: Protein FAM83H (Q6ZRV2)
Organism: Homo sapiens (Human)
Function: May play a major role in the structural organization and calcification of developing enamel. May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23902688}. Note=Colocalizes with keratin filaments. {ECO:0000269|PubMed:23902688}.
Interaction partners:
- Casein kinase I isoform alpha
- WD repeat-containing protein 72
- Casein kinase I isoform epsilon
- Amelogenin, X isoform
- Enamelin
- Odontogenesis associated phosphoprotein
- Matrix metalloproteinase-20
- Pseudokinase FAM20A
- Rho GTPase-activating protein 39
- Casein kinase I isoform delta
Sequence:
MARRSQSSSQGDNPLAPGYLPPHYKEYYRLAVDALAEGGSEAYSRFLATEGAPDFLCPEELEHVSRHLRPPQYVTREPPEGSLLDVDMDGSSGTYWPVNSDQAVPELDLGWPLTFGFQGTEVTTLVQPPPPDSPSIKDEARRMIRSAQQVVAVVMDMFTDVDLLSEVLEAAARRVPVYILLDEMNAQHFLDMADKCRVNLQHVDFLRVRTVAGPTYYCRTGKSFKGHVKEKFLLVDCAVVMSGSYSFMWSFEKIHRSLAHVFQGELVSSFDEEFRILFAQSEPLVPSAAALARMDAYALAPYAGAGPLVGVPGVGAPTPFSFPKRAHLLFPPPREEGLGFPSFLDPDRHFLSAFRREEPPRMPGGALEPHAGLRPLSRRLEAEAGPAGELAGARGFFQARHLEMDAFKRHSFATEGAGAVENFAAARQVSRQTFLSHGDDFRFQTSHFHRDQLYQQQYQWDPQLTPARPQGLFEKLRGGRAGFADPDDFTLGAGPRFPELGPDGHQRLDYVPSSASREVRHGSDPAFAPGPRGLEPSGAPRPNLTQRFPCQAAARPGPDPAPEAEPERRGGPEGRAGLRRWRLASYLSGCHGEDGGDDGLPAPMEAEAYEDDVLAPGGRAPAGDLLPSAFRVPAAFPTKVPVPGPGSGGNGPEREGPEEPGLAKQDSFRSRLNPLVQRSSRLRSSLIFSTSQAEGAAGAAAATEKVQLLHKEQTVSETLGPGGEAVRSAASTKVAELLEKYKGPARDPGGGAGAITVASHSKAVVSQAWREEVAAPGAVGGERRSLESCLLDLRDSFAQQLHQEAERQPGAASLTAAQLLDTLGRSGSDRLPSRFLSAQSHSTSPQGLDSPLPLEGSGAHQVLHNESKGSPTSAYPERKGSPTPGFSTRRGSPTTGFIEQKGSPTSAYPERRGSPVPPVPERRSSPVPPVPERRGSLTLTISGESPKAGPAEEGPSGPMEVLRKGSLRLRQLLSPKGERRMEDEGGFPVPQENGQPESPRRLSLGQGDSTEAATEERGPRARLSSATANALYSSNLRDDTKAILEQISAHGQKHRAVPAPSPGPTHNSPELGRPPAAGVLAPDMSDKDKCSAIFRSDSLGTQGRLSRTLPASAEERDRLLRRMESMRKEKRVYSRFEVFCKKEEASSPGAGEGPAEEGTRDSKVGKFVPKILGTFKSKK
Protein: Troponin I (Tn I) (Protein heldup) (Protein wings apart-A) (P36188)
Organism: Drosophila melanogaster (Fruit fly)
Function: Troponin I is the ATPase inhibitory subunit of troponin in the thin filament regulatory complex. Involved in the development and maintenance of muscle and nervous system. May also be involved in the cytoskeletal apparatus.
Interaction partners:
- Troponin T, skeletal muscle
- FI07231p
- Tropomyosin-2
- Myosin light chain alkali
- Myosin heavy chain, muscle
- Myosin regulatory light chain 2
- Paramyosin, long form
- IP16893p
- Bent, isoform F
- Troponin C, isoform 2
Sequence:
MADDEKKAAAPAAAPAAAAKPAAPAAAPAANGKAAPAANGKAAPAAAAAPAGPPKDPNDPKVKAEEAKKAKQAEIERKRAEVRKRMEEASKAKKAKKGFMTPERKKKLRLLLRKKAAEELKKEQERKAAERRRIIEERCGSPRNLSDASEGELQEICEEYYERMYICEGQKWDLEYEVRKKDWEINDLNAQVNDLRGKFVKPALKKVSKYENKFAKLQKKAAEFNFRNQLKVVKKKEFTLEEEEKEKKPDWSKGKPGDAKVKEEVEAEA
Protein: Putative vacuolar protein sorting-associated protein TDA6 (Topoisomerase I damage affected protein 6) (Q06466)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in vacuolar protein sorting.
Subcellular location: Membrane; Single-pass membrane protein.
Interaction partners:
- Polyamine transporter 3
- Polyamine transporter 2
- Uncharacterized vacuolar protein YLR297W
- Transcriptional activator HAA1
Sequence:
MHCVLARILLWFLIVDLSVIRALVLPPLKDYDPLEPLMKRDMAMGQRNRFKVDGQLPPILNSTDVTDDQRSLHTPGEIPSYVINHCPLVHLYSEEKYWPSDIAEYVQNFQIKDKNGNSISTHENLTLHDLKAEYHVDLFGNKTETHIPSSEVFLTSLDDFDKDPKWLLGHLPEYGTGYNSKAPAILIVVDKGNGWVDAFWFFFYPFNHGPFIMGHGPWGNHVGDWEHSLVRFYKGIPKYLWMSAHSSGTGYRYEAVEKFKKLRKRKQQDSDDGGDTILERPLIFSARGTHANYASAGQHAHDIPFFFMPLSDFTDRGPLWDPSLNFYSYTFDGKTVTPSSEREESLGLDWLHFQGGWGDQQLPARDPRQKWCVAQWKYIGGPRGPLFKKLDRLNLCGGVKKWNFWNGGCPARRLIKKAEGLDSESTDLMGDNCGVLLYRIRPKWLRGILRFLMWRGILCSLMEFFTN
Protein: Small vasohibin-binding protein (Coiled coil domain-containing protein 23) (Q8N300)
Organism: Homo sapiens (Human)
Function: Enhances the tyrosine carboxypeptidase activity of VASH1 and VASH2, thereby promoting the removal of the C-terminal tyrosine residue of alpha-tubulin. This activity is critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning. Also required to enhance the solubility and secretion of VASH1 and VASH2. Plays a role in axon and excitatory synapse formation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99LQ4}. Secreted {ECO:0000250|UniProtKB:Q99LQ4}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:31235911}. Note=Detected both intracellularly and extracellularly (By similarity). Within cells, localizes mainly to the apical part of the cell (By similarity). {ECO:0000250|UniProtKB:Q99LQ4}.
Interaction partners:
- Tubulinyl-Tyr carboxypeptidase 1
- Tubulinyl-Tyr carboxypeptidase 2
- Tubulin alpha-1B chain
- Tubulin alpha-1A chain
- Tubulin beta-3 chain
- Tubulin beta-2B chain
- Tubulin--tyrosine ligase
Sequence:
MDPPARKEKTKVKESVSRVEKAKQKSAQQELKQRQRAEIYALNRVMTELEQQQFDEFCKQMQPPGE
Protein: BRD4 interacting chromatin remodeling complex associated protein, isoform C (A0A0B4KI07)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQMLPQQFTISQQPQQQQQAQQVFQFIQGPQGQLIATTPQQQQPIQQQQQQQPQPVQQQQQHRFVSNAGVTGMSTGKTGKAPQQILPKPQQELQQQKKGTNGGAQISQSAQQTGQANNPTQQQQQQQQQQILLPATTNQPQQLLLNQMPVLVQQNPQGVQLILRPPTPQLTTTPSLVIQQNARGQPQLQTQPAQQQLLRIVGTNGATMQLAAAPTFIVSSQANLIHQTAAGQFQSAIKSGTQLTGLHAALAQAQAQAQAPRSQPFATTATLNTQLLGQSVAAQLQNLQLAAAQIQMPNGLTAISQLPAHLQQSLGGATINLNQLNGAHIQQIANAFQAPQAPGTNSGGANSTTELFTQSSPAHVPLAVTPEPLRQPTPVPMMQQQQQAAMATIQLQQQQQQQQQAQIQQLQHQLQQTQSQVQQAQQSVQATTIPEPKKKPRPRKKKQPPAPTPPAASPTVAPAEVRPPTPQKIAIAATPAPQPTVRAKSPSPPPTTIQRSSNGKLDLGDVMKFCGITGDDDDDEDYGMGLETGLASESEPAQAHAPATGSAAATTGSSGDIMISIPNQNGSDGLPFTLTIPAPQPQSSTGSQAAGNESATEIPNILIKIDPSAEAAVPPFGLSTPRLPTAEEIQKQAQQHLAQQAAAAAAAAKATTATPTINISLPSMTLQPQVAPAPVVTPTPAPSSNQVSTTVVVKPRRKPAVRRNAKKPDVTSSASNMISSSSGTTTTISSSTSTILNNSQPTTVNTITLTTPTPVTSSSNSTLMLTHGTPTAVPSQIGNIQISQVHNHHPSALPVSSAVENKIQIMPILPPGATVMGGTPGTGGHAPTTQSTQLVFQPAAPSVAPTITSDSTGFKLSSDGRQMQLVAIPQATPPSPAASSAQPPVPTPTPALTAGGATILPPQLTGMPANVSVSVGSPASAAALVPQLTGSLTLTVSEQCERLILRHDPNNPQDHQSQLILQALLKGALPNVTIINEPTRVDPNKQTTPMLQPQQQVIQIPQPLTQPQQILQQQPKVSTAPKIEVKVANNRKLSGQVTHPASSMLGMTSTTTTMSTMKPPANLPAKQNEVVSFPQLPLNSQVLIQQQPMISAQLQPQLQPVTVPVSLPTQPVPIPSPAPAPQLANNGQQRYIALPPIDPTTQQLFCLNSVTNQITAMSAGQTAASIGPTERLLIAPAGINAQQLAQCLQLGQLHFNDVNPLPAQQQQQQVATTSSSMTLSMPLRPQPPQQQIVHPIQPITNGLAITTTASSTLTTTTSTTSLTTVTKQVANVAPIIDQSKAKLEPAKAATSGAGGGAVVKKKPVRKPKATPTNASELANLKNASVVKPMPKLDPLSQKPNNNPVQIVQPNVASGKQMIVVGSSSCTTTTTTTMSASIQPFQTTSGTKLVGVTVPMQQQQPTGTAAILQQQQQQRTSFSLTATTVATPAPMPSPTVASGVSQLQMQQLPSQQAQQQLQPQQQQQLHAPKQQQPQPNTVSRVQTIQLTPQMQQIFKQVQMQIQFLTIKLQNKSTFLPVSPEIDSATIAAYNKPMTDAEINLALQRLFAEQHRILASGKEVPTPEGMLPTANGTGGFSLMPQPVQQQQQQQQQQLQSTVPEPLKTIVPANVVQPNNHSSTPAGAATSGATTAANIQQNITQRIHIYPMQHQQQQQQQQQQQQQQPQHQQQQPQHQLQQTGAKPKQAQPKPPPQQEQQSQLQIKPKEPANRSKVTSQQLQQNPQPPNGTINMLPQKVSMMPVVQQQQQQQPQQHQQQPMLNKSGPPPLIFASSTNMLSNSNSNNLHNSNSAMQVNNMLPLPPLQPQQQPQPQLQQPPTPILPPVAPTMAMGVAPGPMGNLVPSLPTIPSLPLYMPSKMDEMPTQKPKIARLSLFVRQLEVDQESCLKPDYVKPFRTKDEAVKRLIRYHCMHENDVELPSDEDEEFESTALEFQDKFRQLNGKFQEILMQESTLPHRTSELLQMQQLMIDDLKGEINEIRTAEKELEQQLKEEQTSEKSTAESDVLSEAKVKEEIKQEPIDKSAQPDGVVDKFDLLKNSADVNKAFSKSQPQQTTTVKQEESNESGEPSVNGSVKSEGHDKESSKYIKKDYDNFDIESELTTSFIMKKVENKAALAKSAENRYQERNMMDQQQQQQHIKANGGDPVDQDDGWYCLQKELNLMNNDHMQQSQQQLNGNQQHLPINRQPAPQQSHFLDNSNSNNMMGNSNHMSDLFPNGCIDKSNQSTTSSSNSSCVSESLPGSNPVKTVSSCSGQREQPVVMDADQQNEHPAISEFFSSDSDVQKSVETRLEAMFGESPVHLDVKSSNDANDIESNLDEIFGDSKSPAANHKSKMSMWVPDASFMQQAPQQQTSQQQQQYAGPQQPSQQQHHIELNCNNNPRWMQSMEAHYSDFLSTGTSNGELVNGESRKRSWDSQLMGSGSDMEDDNSSKRLCTASSSSSSSPMSSQQQHVQVAQHGLLDSDMFPQMLMDQQPHQQQQQVQQQHNFAYANIMDQQQQQQHQQQHFQHNLQQQIQQQQQMHVSHMGGAAVVAGGEYDDDISRHVASAIDSILNLQNSGDSLQFSLGSILGDSMLDDQRQAGANLPSCQQEQAIQRRRHLGEEMNDCLISGGGSAVSGVADNSSNILLEHHHQQHQLMQSHQQQPHLQHHHHQNMSQAQAQHMGQLNDFSCVAGGLDDPVKSIMTS
Protein: Glycoprotein G (Q9IH62)
Organism: Nipah virus
Function: Interacts with host ephrinB2/EFNB2 or ephrin B3/EFNB3 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.
Subcellular location: Virion membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPAENKKVRFENTTSDKGKIPSKVIKSYYGTMDIKKINEGLLDSKILSAFNTVIALLGSIVIIVMNIMIIQNYTRSTDNQAVIKDALQGIQQQIKGLADKIGTEIGPKVSLIDTSSTITIPANIGLLGSKISQSTASINENVNEKCKFTLPPLKIHECNISCPNPLPFREYRPQTEGVSNLVGLPNNICLQKTSNQILKPKLISYTLPVVGQSGTCITDPLLAMDEGYFAYSHLERIGSCSRGVSKQRIIGVGEVLDRGDEVPSLFMTNVWTPPNPNTVYHCSAVYNNEFYYVLCAVSTVGDPILNSTYWSGSLMMTRLAVKPKSNGGGYNQHQLALRSIEKGRYDKVMPYGPSGIKQGDTLYFPAVGFLVRTEFKYNDSNCPITKCQYSKPENCRLSMGIRPNSHYILRSGLLKYNLSDGENPKVVFIEISDQRLSIGSPSKIYDSLGQPVFYQASFSWDTMIKFGDVLTVNPLVVNWRNNTVISRPGQSQCPRFNTCPEICWEGVYNDAFLIDRINWISAGVFLDSNQTAENPVFTVFKDNEILYRAQLASEDTNAQKTITNCFLLKNKIWCISLVEIYDTGDNVIRPKLFAVKIPEQCT
Protein: Zinc finger protein 688 (P0C7X2)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAPPPAPLLAPRPGETRPGCRKPGTVSFADVAVYFSPEEWGCLRPAQRALYRDVMQETYGHLGALGFPGPKPALISWMEQESEAWSPAAQDPEKGERLGGARRGDVPNRKEEEPEEVPRAKGPRKAPVKESPEVLVERNPDPAISVAPARAQPPKNAAWDPTTGAQPPAPIPSMDAQAGQRRHVCTDCGRRFTYPSLLVSHRRMHSGERPFPCPECGMRFKRKFAVEAHQWIHRSCSGGRRGRRPGIRAVPRAPVRGDRDPPVLFRHYPDIFEECG
Protein: Putative syntaxin 6 (P83528)
Organism: Caenorhabditis elegans
Function: SNARE promoting movement of transport vesicles to target membranes (By similarity). Potentially functions in retrograde trafficking and in the endocytic recycling pathway (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Putative syntaxin-5
- t-SNARE coiled-coil homology domain-containing protein
- t-SNARE coiled-coil homology domain-containing protein
- V-SNARE coiled-coil homology domain-containing protein
- V-SNARE coiled-coil homology domain-containing protein
- Vesicle-trafficking protein SEC22b
- YKT6
- Soluble NSF attachment protein 29
- Golgi SNAP receptor complex member 1
- t-SNARE coiled-coil homology domain-containing protein
Sequence:
MSNYRYSKLNEEEISLEDMPSSANQILTRQEQIIQEQDDELELVGNSVRTLRGMSSMIGDELDQQSTMLDDLGQEMEYSETRLDTAMKKMAKLTHLEDESSQCKMIMVLSALLFFLVFVLLV
Protein: cAMP-dependent protein kinase (EC 2.7.11.11) (A0A1D8PHU1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- Adenylate cyclase
- Ras-like protein 1
- Ras2p
- Enhanced filamentous growth protein 1
- cAMP-dependent protein kinase
- Stress-responsive transcriptional activator
- Mitogen-activated protein kinase MKC1
- Transcriptional regulator EFH1
- non-specific serine/threonine protein kinase
Sequence:
MDNHQQQQQLQHQQYQQQFQQPQQQLYPGEQIVHPAAAQTGQNTTNVTAVSSSNITQSATSSLHSQQLQHVDVSKSAAEEAIRRSLLPERSTVSKGKYSLTDFSIMRTLGTGSFGRVHLVRSVHNGRYYAIKVLKKHQVVKMKQVEHTNDERRMLKLVEHPFLIRMWGTFQDSKNLFMVMDYIEGGELFSLLRKSQRFPNPVAKFYAAEVTLALEYLHSHDIIYRDLKPENILLDRNGHIKITDFGFAKEVSTVTWTLCGTPDYIAPEVITTKPYNKSVDWWSLGVLIFEMLAGYTPFYDSTPMKTYEKILAGKIHYPSFFQPDVIDLLTKLITADLTRRLGNLINGPADIRNHPWFSEVVWEKLLAKDIETPYEPPITAGVGDSSLFDHYPEEQLDYGSQGEDPYASYFLDF
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (G gamma-I) (P59768)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 7
- C-C chemokine receptor type 5
- Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
Sequence:
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENPFREKKFFCAIL
Protein: Glucose transporter GLUT4 (Q6Q243)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
SEELWPVLVGVTVLPTVLQMVLLPFCPESPRFLYIIRSQEHHAKSGLRRLTGRQEVGDMLAEMKEEKRRMDMERKVSIAELFRSPMYRQ
Protein: Leucine zipper putative tumor suppressor 1 (F37/esophageal cancer-related gene-coding leucine-zipper motif) (Fez1) (Q9Y250)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as a tumor suppressor.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse {ECO:0000250}. Note=Associated with the plasma membrane and with microtubules. Detected in dendritic spines, especially in the postsynaptic density (By similarity). {ECO:0000250}.
Interaction partners:
- Leucine zipper putative tumor suppressor 2
- Fasciculation and elongation protein zeta-2
- Signal-induced proliferation-associated 1-like protein 1
- Protein unc-119 homolog A
- Deleted in lung and esophageal cancer protein 1
Sequence:
MGSVSSLISGHSFHSKHCRASQYKLRKSSHLKKLNRYSDGLLRFGFSQDSGHGKSSSKMGKSEDFFYIKVSQKARGSHHPDYTALSSGDLGGQAGVDFDPSTPPKLMPFSNQLEMGSEKGAVRPTAFKPVLPRSGAILHSSPESASHQLHPAPPDKPKEQELKPGLCSGALSDSGRNSMSSLPTHSTSSSYQLDPLVTPVGPTSRFGGSAHNITQGIVLQDSNMMSLKALSFSDGGSKLGHSNKADKGPSCVRSPISTDECSIQELEQKLLEREGALQKLQRSFEEKELASSLAYEERPRRCRDELEGPEPKGGNKLKQASQKSQRAQQVLHLQVLQLQQEKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDMGPPTFPEDVPALQRELERLRAELREERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLARGDSAGEPLEVDLEGADIPYEDIIATEI
Protein: Pretranslocation protein, alpha subunit, putative (Q385E6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S5, putative
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L17, putative
- Protein transport protein Sec61 gamma subunit, putative
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S14
- 40S ribosomal protein S15a, putative
- Large ribosomal subunit protein uL5
- Ribosomal protein
Sequence:
MTDILMKMSPILAFLPEVATPLRVVPIRERIMWTFVALFIFLVCCQVPVFGARPGQASDPFYWMRVVLASNKGTLMELGISPIVTASLVMELLVGVRIISYDINNKRERAVYEGVQKIVALFITIVEATAYVSSGMYGDVREIGVFMCGLIVLQLTFATMVCILLDELLQNGWGLGAGTSLFIATNICDTIIWKCFSPSTINTGRGSEFEGAIIAFFHLLVTRTDKVRALKEAFYRPQLPNLTNVFATVLLFAVVVFLQGFRVPLMTKSRNAAADRQPYIIKLFYTSNMPIILQTSVVSNINFFSQILSRRFGQFNFLINLLGRWESRAYSQSGQMYPVGGLAYYLTAPSTFYDMINDPVHAVLYIVFILFSCATFSKLWVAISHTGPRDVAKRLVSEGRWLAQARESEEDMARLLEKYIPVAASFGGLCVGALTLFADFLGAIGSGTGVLLSVTMINQYYDILREEGEDLGYNFIKRKVA
Protein: Proline rich coiled-coil 2C (E7EPN9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSEKSGQSTKAKDGKKYATLSLFNTYKGKSLETQKTTVAARHGLQSLGKVGISRRMPPPANLPSLKAENKGNDPNVNIVPKDGTGWASKQEQHEEEKTPEVPPAQPKPGVAAPPEVAPAPKSWASNKQGGQGDGIQVNSQFQQEFPSLQAAGDQEKKEKETNDDNYGPGPSLRPPNVACWRDGGKAAGSPSSSDQDEKLPGQDESTAGTSEQNDILKVVEKRIACGPPQAKLNGQQAALASQYRAMMPPYMFQQYPRMTYPPLHGPMRFPPSLSETNKGLRGRGPPPSWASEPERPSILSASELKELDKFDNLDAEADEGWAGAQMEVDYTEQLNFSDDDEQGSNSPKENNSEDQGSKASENNENKKETDEVSNTKSSSQIPAQPSVAKVPYGKGPSFNQERGTSSHLPPPPKLLAQQHPPPDRQAVPGRPGPFPSKQQVADEDEIWKQRRRQQSEISAAVERARKRREEEERRMEEQRKAACAEKLKRLDEKLGILEKQPSPEEIREREREKEREREKELEKEQEQEREKEREKDRERQQEKEKELEKEQEKQREMEKERKQEKEKELERQKEKEKELQKMKEQEKECELEKEREKLEEKIEPREPNLEPMVEKQESENSCNKEEEPVFTRQDSNRSEKEATPVVHETEPESGSQPRPAVLSGYFKQFQKSLPPRFQRQQEQMKQQQWQQQQQQGVLPQTVPSQPSSSTVPPPPHRPLYQPMQPHPQHLASMGFDPRWLMMQSYMDPRMMSGRPAMDIPPIHPGMIPPKPLMRRDQMEGSPNSSESFEHIARSARDHAISLSEPRMLWGSDPYPHAEPQQATTPKATEEPEDVRSEAALDQEQITAAYSVEHNQLEAHPKADFIRESSEAQVQKFLSRSVEDVRPHHTDANNQSACFEAPDQKTLSAPQEERISAVESQPSRKRSVSHGSNHTQKPDEQRSEPSAGIPKVTSRCIDSKEPIERPEEKPKKEGFIRSSEGPKPEKVYKSKSETRWGPRPSSNRREEVNDRPVRRSGPIKKPVLRDMKEEREQRKEKEGEKAEKVTEKVVVKPEKTEKKDLPPPPPPPQPPAPIQPQSVPPPIQPEAEKFPSTETATLAQKPSQDTEKPLEPVSTVQVEPAVKTVNQQTMAAPVVKEEKQPEKVISKDLVIERPRPDSRPAVKKESTLPPRTYWKEARERDWFPDQGYRGRGRGEYYSRGRSYRGSYGGRGRGGRGHTRDYPQYRDNKPRAEHIPSGPLRQREESETRSESSDFEVVPKRRRQRGSETDTDSEIHESASDKDSLSKGKLPKREERPENKKPVKPHSSFKPDNHVRIDNRLLEKPYVRDDDKAKPGFLPKGEPTRRGRGGTFRRGGRDPGGRPSRPSTLRRPAYRDNQWNPRQSEVPKPEDGEPPRRHEQFIPIAADKRPPKFERKFDPARERPRRQRPTRPPRQDKPPRFRRLREREAASKSNEVVAVPTNGTVNNVAQEPVNTLGDISGNKTPDLSNQNSSDQANEEWETASESSDFNERRERDEKKNADLNAQTVVKVGENVLPPKREIAKRSFSSQRPVDRQNRRGNNGPPKSGRNFSGPRNERRSGPPSKSGKRGPFDDQPAGTTGVDLINGSSAHHQEGVPNGTGQKNSKDSTGKKREDPKPGPKKPKEKVDALSQFDLNNYASVVIIDDHPEVTVIEDPQSNLNDDGFTEVVSKKQQKRLQDEERRKKEEQVIQVWNKKNANEKGRSQTSKLPPRFAKKQATGIQQAQSSASVPPLASAPLPPSTSASVPASTSAPLPATLTPVPASTSAPVPASTLAPVLASTSAPVPASPLAPVSASASVSASVPASTSAAAITSSSAPASAPAPTPILASVSTPASVTILASASIPILASALASTSAPTPAPAASSPAAPVITAPTIPASAPTASVPLAPASASAPAPAPTPVSAPNPAPPAPAQTQAQTHKPVQNPLQTTSQSSKQPPPSIRLPSAQTPNGTDYVASGKSIQTPQSHGTLTAELWDNKVAPPAVLNDISKKLGPISPPQPPSVSAWNKPLTSFGSAPSSEGAKNGQESGLEIGTDTIQFGAPASNGNENEVVPVLSEKSADKIPEPKEQRQKQPRAGPIKAQKLPDLSPVENKEHKPGPIGKERSLKNRKVKDAQQVEPEGQEKPSPATVRSTDPVTTKETKAVSEMSTEIGTMISVSSAEYGTNAKESVTDYTTPSSSLPNTVATNNTKMEDTLVNNVPLPNTLPLPKRETIQQSSSLTSVPPTTFSLTFKMESARKAWENSPNVREKGSPVTSTAPPIATGVSSSASGPSTANYNSFSSASMPQIPVASVTPTASLSGAGTYTTSSLSTKSTTTSDPPNICKVKPQQLQTSSLPSASHFSQLSCMPSLIAQQQQNPQVYVSQSAAAQIPAFYMDTSHLFNTQHARLAPPSLAQQQGFQPGLSQPTSVQQIPIPIYAPLQGQHQAQLSLGAGPAVSQAQELFSSSLQPYRSQPAFMQSSLSQPSVVLSGTAIHNFPTVQHQELAKAQSGLAFQQTSNTQPIPILYEHQLGQASGLGGSQLIDTHLLQARANLTQASNLYSGQVQQPGQTNFYNTAQSPSALQQVTVPLPASQLSLPNFGSTGQPLIALPQTLQPPLQHTTPQAQAQSLSRPAQVSQPFRGLIPAGTQHSMIATTGKMSEMELKAFGSGIDIKPGTPPIAGRSTTPTSSPFRATSTSPNSQSSKMNSIVYQKQFQSAPATVRMTQPFPTQFAPQAKQRAEVLQSTQRFFSEQQQSKQIGGGKAQKVDSDSSKPPETLTDPPGVCQEKVEEKPPPAPSIATKPVRTGPIKPQAIKTEETKS
Protein: DNA repair protein RAD51 homolog (Q8IIS8)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364139}.
Interaction partners:
- 3'-5' exonuclease
- DNA repair and recombination protein RAD54, putative
- Meiotic recombination protein DMC1, putative
- DNA 3'-5' helicase
- Uncharacterized protein
- Crossover junction endonuclease MUS81
- DNA 3'-5' helicase
- Replication protein A1, small
- Replication protein A1, large subunit
- Double-strand break repair protein MRE11
Sequence:
MKQANTKEDKSQKISNSSTIDEIEEEQLYTGPLKIEQLLAKGFVKRDLELLKEGGLQTVECVAYAPMRTLCAIKGISEQKAEKLKKACKELCNSGFCNAIDYHDARQNLIKFTTGSKQLDALLKGGIETGGITELFGEFRTGKSQLCHTLAITCQLPIEQSGGEGKCLWIDTEGTFRPERIVAIAKRYGLHPTDCLNNIAYAKAYNCDHQTELLIDASAMMADARFALLIVDSATALYRSEYIGRGELANRQSHLCRFLRGLQRIADIYGVAVIITNQVVAKVDAMSMFGGHEKIPIGGNIIAHASQTRLYLRKGRGESRICKIYDSPVLPEGEAVFAITEGGIADYEEK
Protein: Leucine-rich repeat protein SHOC-2 (Protein soc-2 homolog) (protein Sur-8 homolog) (X6RI37)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV
Protein: FI23914p1 (HP1 and insulator partner protein 1, isoform A) (Q9VPB0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Zinc finger protein su
- Centrosome-associated zinc finger protein Cp190
- Modifier of mdg4
- FI18814p1
- Insulator binding factor 2
Sequence:
MEQVSDSAVTTLESTQAEEPPPGVEKVETLELKTAALETLSESAGPTDLENELANLNGSEEGPGLDELSTLEREIAKLHNIRPPDAASEVKDSDTPIALADNGGLEPRQAPDEAKCRTPIIEEGNAASGNGQSSESPLEEVDLIALLKGTDTSHDQPTGEEKCTLEKALSELDGVGEDGDVGVTIEGEGQFEIMEIDDDEGESSSRKASPKVPASKPIKSNSLPSISKHKLSPEQARAVALEQMAGLKPKSRRKEPPAPPSVVAPIDIVSSLNDDWDDYDSEEDKSASALVTEVITLPSAHVVTKKPPLPVKKLSSPVKHSPNSAILLNNKISGVKVMLKTVSQKQLAASTGAAAEKTKPTVVVSPPKETEEHTTGFKRMRVIKRKIIWDPDVPETKKSFAQYASTKAACPAPTTPKTTVKSISPTTTTKKEVAPKKRSATPTARSTKAGTPVGGTERGPSPVKRRAQTPNTGLANGGTQKKKKVSEIDRLMGDEGAANMIHAVEHEQRELSGGEVSNKPLMRKRAMTITGRNQAARVAVEPTPPKKESAQSAAKRTPADSVFTKATANTSARKPRASDSWDYVYKQRASEESMIMRRRSNSSYSSNASVSRNSLDNRPGAANLSDDAGEGSDPSFKFVKPVSKSSQRGGEDTSSHTLANDMKANNGSELVCLHKVNKVAHLVIHTERGNFGHTYSKQLLEQLNDTLSSVARKGEFNTVLLTVEGPQFCQGIDCQELIQGSLEKRKDSASQLAVALKCYLRTLATFPKPLVAGIVGSQINLGVMQLPFADYVVASDDCSFETNYAKLGQLPEGYALWHGHQRVSSEVHSRLFLMGERLFATELLESNSFVDKICKARNVNEMALAKAKQISTSSAEMYRTLKKLNHSAVNVTKFPRLDEELKVIGEQWVTADCLANFKRYLNDVDF