wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein eL22 (60S ribosomal protein L22) (Heparin-binding protein HBp15) (P67984)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL24
Sequence:
MAPVKKLVAKGGKKKKQVLKFTLDCTHPVEDGIMDAANFEQFLQERIKVNGKAGNLGGGVVTIERSKSKITVTSEVPFSKRYLKYLTKKYLKKNNLRDWLRVVANSKESYELRYFQINQDEEEEEDED
Protein: Allophycocyanin alpha chain (Q01951)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers.
Subcellular location: Cellular thylakoid membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Forms the core of the phycobilisome. {ECO:0000250}.
Interaction partners:
- C-phycocyanin alpha subunit
- Phycobilisome 7.8 kDa linker polypeptide, allophycocyanin-associated, core
- Phycobilisome rod-core linker polypeptide CpcG
- C-phycocyanin beta subunit
- Allophycocyanin beta chain
- Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod 1
- Phycobiliprotein ApcE
- Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod 2
- Allophycocyanin subunit beta-18
- Photosystem I-associated linker protein CpcL
Sequence:
MSIVTKSIVNADAEARYLSPGELDRIKAFVTGGAARLRIAETLTGSRETIVKQAGDRLFQKRPDIVSPGGNAYGEEMTATCLRDMDYYLRLVTYGVVSGDVTPIEEIGLVGVREMYRSLGTPIEAVAQSVREMKEVASGLMSSDDAAEASAYFDFVIGKMS
Protein: Metallophosphoesterase 1 (EC 3.1.-.-) (Post-GPI attachment to proteins factor 5) (Q53F39)
Organism: Homo sapiens (Human)
Function: Metallophosphoesterase required for transport of GPI-anchor proteins from the endoplasmic reticulum to the Golgi. Acts in lipid remodeling steps of GPI-anchor maturation by mediating the removal of a side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of the GPI intermediate, an essential step for efficient transport of GPI-anchor proteins.
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:19837036}; Multi-pass membrane protein {ECO:0000269|PubMed:19837036}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:19837036}; Multi-pass membrane protein {ECO:0000269|PubMed:19837036}. Note=Also localizes to endoplasmic reticulum exit site.
Interaction partners:
- Cell division cycle protein 27 homolog
- Basic leucine zipper transcriptional factor ATF-like 3
- Chemokine XC receptor 1
- C-type lectin domain family 9 member A
- Guanine nucleotide-binding protein G
- T-cell surface glycoprotein CD8 alpha chain
- Proteasome subunit beta type-5
- Integrin alpha-E
- Thrombomodulin
- Lymphotactin
Sequence:
MAMIELGFGRQNFHPLKRKSSLLLKLIAVVFAVLLFCEFLIYYLAIFQCNWPEVKTTASDGEQTTREPVLKAMFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSHVQLKVVAGNHDIGFHYEMNTYKVERFEKVFSSERLFSWKGINFVMVNSVALNGDGCGICSETEAELIEVSHRLNCSREARGSSRCGPGPLLPTSAPVLLQHYPLYRRSDANCSGEDAAPAEERDIPFKENYDVLSREASQKLLWWLQPRLVLSGHTHSACEVHHGGRVPELSVPSFSWRNRNNPSFIMGSITPTDYTLSKCYLPREDVVLIIYCGVVGFLVVLTLTHFGLLASPFLSGLNLLGKRKTR
Protein: Autophagy-related protein 21 (Meiotically up-regulated gene 179 protein) (Q9P6N1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for cytoplasm to vacuole transport (Cvt) vesicles formation and autophagy (By similarity). Has a role in sporulation.
Subcellular location: Cytoplasm. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. Preautophagosomal structure membrane; Peripheral membrane protein.
Interaction partners:
- Autophagy-related protein 2
- Serine/threonine-protein kinase atg1
- Putative lipase atg15
- Autophagy protein 5
- Autophagy-related protein 9
- SVP1-like protein 2
- Probable cysteine protease atg4
- Ubiquitin-like protein ATG12
- Autophagy protein 13
- Autophagy-related protein 17
Sequence:
MPSIILYCSWNQDRGFLSIGSENGYQVYRSNPFTLCFSKKANGASICEMLYESSLLAFVNISPESTRLLKLVDIKRDIVLCRIFYPSPVLSVRFTWNRLVVLIKGSIYVYNLKNMELINTLNTSKGNVIAFAVHENYVAYNSPTNPGDIYLASLDTAIPVTLIHCHSSAVQVVDFHPRGHLIATASAKGTVIRVITTSDGELVTELRRGYIPASIVSISFHPVEPFLACASENGTIHVFKISKQPSDPNSSPTSSVTVSSSWSKYLTSNVAKVWDTRKEFATAKIPEASFYGKIIFSSSGPHIQVASYSGHYYRFAVNLKNGGNCALLERYIFDD
Protein: Nucleoporin NUP49/NSP49 (Nuclear pore protein NUP49/NSP49) (Q02199)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP49 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Interaction partners:
- Nucleoporin NUP2
- Nucleoporin NUP57
- Nucleoporin NUP159
- Nucleoporin NUP133
- Nucleoporin NIC96
- Nucleoporin NSP1
- Nucleoporin ASM4
- Nucleoporin NUP85
- Nucleoporin NUP192
- Nucleoporin NUP145
Sequence:
MFGLNKASSTPAGGLFGQASGASTGNANTGFSFGGTQTGQNTGPSTGGLFGAKPAGSTGGLGASFGQQQQQSQTNAFGGSATTGGGLFGNKPNNTANTGGGLFGANSNSNSGSLFGSNNAQTSRGLFGNNNTNNINNSSSGMNNASAGLFGSKPAGGTSLFGNTSTSSAPAQNQGMFGAKPAGTSLFGNNAGNTTTGGGLFGSKPTGATSLFGSSNNNNNNNNSNNIMSASGGLFGNQQQQLQQQPQMQCALQNLSQLPITPMTRISELPPQIRQEIEQLDQYIQKQVQISHHLKADTIDHDELIDSIPRDVAYLLKSESATSQYLKQDLKKISSFKSLIDEDLLDTQTFSVLLQQLLTPGSKISSNDLDKFFQKKIHLYEKKLEDYCRILSDIETAVNGIDTDLFGAPNNPNSTAITADLGSSEAENLLQLKTGLAAIVSTVIEEFTLFMDIAERIAVLHQKTKTLASLSI
Protein: Drebrin (Developmentally-regulated brain protein) (Q9QXS6)
Organism: Mus musculus (Mouse)
Function: Actin cytoskeleton-organizing protein that plays a role in the formation of cell projections (By similarity). Required for actin polymerization at immunological synapses (IS) and for the recruitment of the chemokine receptor CXCR4 to IS (By similarity). Plays a role in dendritic spine morphogenesis and organization, including the localization of the dopamine receptor DRD1 to the dendritic spines. Involved in memory-related synaptic plasticity in the hippocampus.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q16643}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q16643}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q16643}. Cell junction {ECO:0000250|UniProtKB:Q16643}. Cell projection {ECO:0000269|PubMed:24720729}. Cell projection, growth cone {ECO:0000269|PubMed:24720729}. Note=In the absence of antigen, evenly distributed throughout subcortical regions of the T-cell membrane and cytoplasm. In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation clusters (SMAC) (By similarity). Colocalized with RUFY3 and F-actin at the transitional domain of the axonal growth cone (PubMed:24720729). {ECO:0000250|UniProtKB:Q16643, ECO:0000269|PubMed:24720729}.
Interaction partners:
- Microtubule-associated protein RP/EB family member 3
- Homer protein homolog 2
- Gap junction alpha-1 protein
- Zinc finger, MYND-type containing 8
- Neurabin-2
- Adenylyl cyclase-associated protein 2
- Nexilin
- Cofilin-1
- Cofilin-2
- Disks large homolog 4
Sequence:
MAGVSFSGHRLELLAAYEEVIREESAADWALYTYEDGSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDSQAALPKYVLINWVGEDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDIDAGAIGQRLSNGLARLSSPVLHRLRLREDENAEPVGTTYQKTDAAVEMKRINREQFWEQAKKEEELRKEEERKKALDARLRFEQERMEQERQEQEERERRYREREQQIEEHRRKQQSLEAEEAKRRLKEQSIFGDQRDEEEESQMKKSESEVEEAAAIIAQRPDNPREFFRQQERVASASGGSCDAPAPAPFNHRPGRPYCPFIKASDSGPSSSSSSSSSPPRTPFPYITCHRTPNLSSSLPCSHLDSHRRMAPTPIPTRSPSDSSTASTPIAEQIERALDEVTSSQPPPPPPPPPPTQEAQETTPSLDEELSKEAKVTAAPEVWAGCAAEPPQAQEPPLLQSSPLEDSMCTESPEQAALAAPAEPAASVTSVADVHAADTIETTTATTDTTIANNVTPAAASLIDLWPGNGEEASTLQAEPRVPTPPSGAEASLAEVPLLNEAAQEPLPPVGEGCANLLNFDELPEPPATFCDPEEEVGETLAASQVLTMPSALEEVDQVLEQELEPEPHLLTNGETTQKEGTQASEGYFSQSQEEEFAQSEEPCAKVPPPVFYNKPPEIDITCWDADPVPEEEEGFEGGD
Protein: Nucleoside diphosphate kinase, putative (EC 2.7.4.6) (Q581Q9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- CTP synthase
- Ribonucleoside-diphosphate reductase
- Guanylate kinase, putative
- Guanylate kinase, putative
- dTMP kinase
- dTMP kinase
- 40S ribosomal protein S13, putative
- Pyruvate kinase
- Nucleoside diphosphate kinase, putative
- Ribonucleoside-diphosphate reductase small chain
Sequence:
MARSLQDPRLSFYCEQYDHIAHRMNHYVLQFYFEDRTVEIREVTKNRLHLKRAHFPHLNRDDFKVGSSLSLLGGVIKLTAYADEVTRELCGERGEVTAVMFGEQLLPQLGRCLAVLTEECGFVALEMQMAWLPVETAAAYGVPPDLVEGRIVVVKCANTNALQRGIDFMARMPGARAAESVEEVGRWEQIVEKAKEQPVAILGDPNSTVVIIKPHALQKLAGGVIVQQLIDAGLEISGISLTNMTSQQANELLKPYKGVLPDFPDTMRSLMGTVWVLQFVSLDEGVDVVSVAREVCGPFDPVIAKELRPTSIRARFGVDRAHNAVHCCDLHEEGPLYSNFFFRPEDVDE
Protein: Purine nucleoside phosphorylase (EC 2.4.2.1) (Inosine-guanosine phosphorylase) (G3V5M2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQRGLALSLVSGARRQSHAAASAGRDARGNRAGVAPPEQEGDRYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQMGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 5 (ADAM-TS 5) (ADAM-TS5) (ADAMTS-5) (EC 3.4.24.-) (A disintegrin and metalloproteinase with thrombospondin motifs 11) (ADAM-TS 11) (ADAMTS-11) (ADMP-2) (Aggrecanase-2) (Q9UNA0)
Organism: Homo sapiens (Human)
Function: Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its VCAN remodeling properties. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration (By similarity). Participates in development of brown adipose tissue and browning of white adipose tissue (By similarity). Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18992360}.
Interaction partners:
- Aggrecan core protein
- Syndecan-4
- Brevican core protein
- Collagenase 3
- Stromelysin-1
- Metalloproteinase inhibitor 3
- Collagen alpha-1
- Runt-related transcription factor 2
- Interleukin-1 beta
- Metalloproteinase inhibitor 1
Sequence:
MLLGWASLLLCAFRLPLAAVGPAATPAQDKAGQPPTAAAAAQPRRRQGEEVQERAEPPGHPHPLAQRRRSKGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDGSVGIAGFVPAGGGTSAPWRHRSHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEKGRVYGDGSARILHVYTREGFSFEALPPRASCETPASTPEAHEHAPAHSNPSGRAALASQLLDQSALSPAGGSGPQTWWRRRRRSISRARQVELLLVADASMARLYGRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYDAAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDSKFCEETFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQILGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGTPCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSLMPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVLPADVCKLTCRAKGTGYYVVFSPKVTDGTECRLYSNSVCVRGKCVRTGCDGIIGSKLQYDKCGVCGGDNSSCTKIVGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPTKPLDVRYSFFVPKKSTPKVNSVTSHGSNKVGSHTSQPQWVTGPWLACSRTCDTGWHTRTVQCQDGNRKLAKGCPLSQRPSAFKQCLLKKC
Protein: BCL-6 corepressor (BCoR) (Q6W2J9)
Organism: Homo sapiens (Human)
Function: Transcriptional corepressor. May specifically inhibit gene expression when recruited to promoter regions by sequence-specific DNA-binding proteins such as BCL6 and MLLT3. This repression may be mediated at least in part by histone deacetylase activities which can associate with this corepressor. Involved in the repression of TFAP2A; impairs binding of BCL6 and KDM2B to TFAP2A promoter regions. Via repression of TFAP2A acts as a negative regulator of osteo-dentiogenic capacity in adult stem cells; the function implies inhibition of methylation on histone H3 'Lys-4' (H3K4me3) and 'Lys-36' (H3K36me2).
Subcellular location: Nucleus {ECO:0000269|PubMed:10898795}.
Interaction partners:
- Polycomb group RING finger protein 1
- B-cell lymphoma 6 protein
- E3 ubiquitin-protein ligase RING2
- E3 ubiquitin-protein ligase RING1
- Protein AF-9
- Lysine-specific demethylase 2B
- Chromobox protein homolog 8
- RING1 and YY1-binding protein
- Polycomb group RING finger protein 2
- Polycomb complex protein BMI-1
Sequence:
MLSATPLYGNVHSWMNSERVRMCGASEDRKILVNDGDASKARLELREENPLNHNVVDASTAHRIDGLAALSMDRTGLIREGLRVPGNIVYSSLCGLGSEKGREAATSTLGGLGFSSERNPEMQFKPNTPETVEASAVSGKPPNGFSAIYKTPPGIQKSAVATAEALGLDRPASDKQSPLNINGASYLRLPWVNPYMEGATPAIYPFLDSPNKYSLNMYKALLPQQSYSLAQPLYSPVCTNGERFLYLPPPHYVGPHIPSSLASPMRLSTPSASPAIPPLVHCADKSLPWKMGVSPGNPVDSHAYPHIQNSKQPRVPSAKAVTSGLPGDTALLLPPSPRPSPRVHLPTQPAADTYSEFHKHYARISTSPSVALSKPYMTVSSEFPAARLSNGKYPKAPEGGEGAQPVPGHARKTAVQDRKDGSSPPLLEKQTVTKDVTDKPLDLSSKVVDVDASKADHMKKMAPTVLVHSRAGSGLVLSGSEIPKETLSPPGNGCAIYRSEIISTAPSSWVVPGPSPNEENNGKSMSLKNKALDWAIPQQRSSSCPRMGGTDAVITNVSGSVSSAGRPASASPAPNANADGTKTSRSSVETTPSVIQHVGQPPATPAKHSSSTSSKGAKASNPEPSFKANENGLPPSSIFLSPNEAFRSPPIPYPRSYLPYPAPEGIAVSPLSLHGKGPVYPHPVLLPNGSLFPGHLAPKPGLPYGLPTGRPEFVTYQDALGLGMVHPMLIPHTPIEITKEEKPERRSRSHERARYEDPTLRNRFSEILETSSTKLHPDVPTDKNLKPNPNWNQGKTVVKSDKLVYVDLLREEPDAKTDTNVSKPSFAAESVGQSAEPPKPSVEPALQQHRDFIALREELGRISDFHETYTFKQPVFTVSKDSVLAGTNKENLGLPVSTPFLEPPLGSDGPAVTFGKTQEDPKPFCVGSAPPSVDVTPTYTKDGADEAESNDGKVLKPKPSKLAKRIANSAGYVGDRFKCVTTELYADSSQLSREQRALQMEGLQEDSILCLPAAYCERAMMRFSELEMKEREGGHPATKDSEMCKFSPADWERLKGNQDKKPKSVTLEEAIAEQNESERCEYSVGNKHRDPFEAPEDKDLPVEKYFVERQPVSEPPADQVASDMPHSPTLRVDRKRKVSGDSSHTETTAEEVPEDPLLKAKRRRVSKDDWPEREMTNSSSNHLEDPHYSELTNLKVCIELTGLHPKKQRHLLHLRERWEQQVSAADGKPGRQSRKEVTQATQPEAIPQGTNITEEKPGRKRAEAKGNRSWSEESLKPSDNEQGLPVFSGSPPMKSLSSTSAGGKKQAQPSCAPASRPPAKQQKIKENQKTDVLCADEEEDCQAASLLQKYTDNSEKPSGKRLCKTKHLIPQESRRGLPLTGEYYVENADGKVTVRRFRKRPEPSSDYDLSPAKQEPKPFDRLQQLLPASQSTQLPCSSSPQETTQSRPMPPEARRLIVNKNAGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKMTHSELMEKFLTDYLNDLQGRNDDDASGTWDFYGSSVCEPDDESGYDVLANPPGPEDQDDDDDAYSDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDLEAFNPESKELLDLVEFTNEIQTLLGSSVEWLHPSDLASDNYW
Protein: CNR2 (O88690)
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:
MDFTTEGRLGTRCMLLSLLLLAAWEAGSGQLHYSVPEEPKHGTFVGRIAQDLGLELTELVPRLFRVASKDRGDLLEVNLQNGILFVNSRIDREELCGRSVECSIHLEVIVDRPLQVFHVEVEVRDINDNPPVFSVKEQRMLIYESRLPDSLFPLEGASDADVGLNSMLTYKLSPSEYFGLDVKSNSDGNKQIRLLLKKSLDREDAPEHKLLLTATDGGKPELTGSVQLLVTVLDVNDNAPTFQHPEYEVRILENSDNGTTVIRLNASDKDEGTNSAISYSFNRLVPPKTLEQFSIDADTGEIITQGNLDFEQVDVYKIHVDATDKGHPPMVGHCTVLVKVLDENDNVPQITLTSLSLPVREDAALSTVIALISVSDLDSGSNGQVTCSLSPHVPFKLVSTFKNYYSLVLDSALDRETTADYQVVVTARDGGSPSLWTTASVSVEVADVNDNAPSFAQPDYTVFVKENNPPGAHIFTVSAMDADAQENALVSYSLVERRVGERLLSSYVSVHAESGKVFALQPLDHEELELLQFQVSARDAGVPALGSNVTLQVFVLDENDNAPTLLGPWTPGSGGVVSELVSPSVGAGQVVTKVRAVDADSGYNAWLSYELHPLAGGTRSLFRVGLYTGEISTTRALEEADAPRHRLLVLVKDHGEPALIATATVLVSLVENSQTPKASSRAQGATGQEVSLVNVNVYLIIAICAVSSLLVLTLMVYTALRCSVPPTEGVCGAGKPVLVCSSAVGSWSYSQQRRQKVCSGEGPPKTDLMAFSPSLPPCPVVGEHQDLNDDHCSRPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
Protein: Immunoglobulin kappa variable 3D-20 (A0A0C4DH25)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
METPAQLLFLLLLWLPDTTGEIVLTQSPATLSLSPGERATLSCGASQSVSSSYLAWYQQKPGLAPRLLIYDASSRATGIPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSP
Protein: Dynactin subunit 5 (Q54XU5)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Dynactin subunit 4
- Dynactin subunit 6
- Dynactin subunit 2
- Dynactin 150 kDa subunit
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha
- Cytoplasmic dynein 1 light intermediate chain 1
- Uncharacterized protein
- Actin-related protein 10
Sequence:
MQVQPKYFEKSQYIETLNGNKVSKSSILCGIMNIRLHGKTIIKPGVIVRGDLASVNIGRLSIISENTVIRPSSKKFKGSLVYFPQNIGDHVLVGEGCVISAASIGSNVYIGNNCIISKRCILKDCCIIADNTILPPDTVVPPFTYYSGTPGVYKEDLPDCIEQFQKEYTTSLYESFLPNTPASKGLPSTPTKLQTTTT
Protein: Myogenesis-regulating glycosidase (EC 3.2.1.-) (Uncharacterized family 31 glucosidase KIAA1161) (Q6NSJ0)
Organism: Homo sapiens (Human)
Function: Putative glycosidase. Promotes myogenesis by activating AKT signaling through the maturation and secretion of IGF2.
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:Q69ZQ1}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q69ZQ1}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:29910000}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q69ZQ1}. Note=Only a minor fraction is present in the peripheral endoplasmic reticulum. {ECO:0000250|UniProtKB:Q69ZQ1}.
Interaction partners:
- Sodium-dependent phosphate transporter 2
Sequence:
MLQNPQEKSQAYPRRRRPGCYAYRQNPEAIAAAAMYTFLPDNFSPAKPKPSKDLKPLLGSAVLGLLLVLAAVVAWCYYSVSLRKAERLRAELLDLKAGGFSIRNQKGEQVFRLAFRSGALDLDSCSRDGALLGCSLTADGLPLHFFIQTVRPKDTVMCYRVRWEEAAPGRAVEHAMFLGDAAAHWYGGAEMRTQHWPIRLDGQQEPQPFVTSDVYSSDAAFGGILERYWLSSRAAAIKVNDSVPFHLGWNSTERSLRLQARYHDTPYKPPAGRAAAPELSYRVCVGSDVTSIHKYMVRRYFNKPSRVPAPEAFRDPIWSTWALYGRAVDQDKVLRFAQQIRLHHFNSSHLEIDDMYTPAYGDFDFDEVKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSRFGEGVERELFVREPTGRLPALVRWWNGIGAVLDFTHPKARDWFQGHLRRLRSRYSVASFKFDAGEVSYLPRDFSTYRPLPDPSVWSRRYTEMALPFFSLAEVRVGYQSQNISCFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDMVGGNAVPQRTAGGDVPERELYIRWLEVAAFMPAMQFSIPPWRYDAEVVAIAQKFAALRASLVAPLLLELAGEVTDTGDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKWRSYKGELFDKTPVLLTDYPVDLDEIAYFTWAS
Protein: Golgi to ER traffic protein 4 (O74432)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATPase get3
- Small glutamine-rich tetratricopeptide repeat-containing protein 2
- Protein get1
- Maintenance of telomere capping protein 1
- UV excision repair protein rhp23
- ER lumen protein-retaining receptor
Sequence:
MDAKIKRAEGRLREDPYEGHQMLRTLVNRQVKAKKHDDAVALLYSGAKTLFEIEQTGSAADLAIYMLDVYEKASYAASLDNKARALTLLGLFPAEEGARKQYVKRLLEWSKSAGPQGDKDVHFAVATMFVKWKEPASAEKHFVLGNEKSARAYGETMYYWFTSDSSISPDTFAGRPVLNYLLAENLISAWNSLETFTKHFTKSNAPDVENMSFDGKDFPVFKEYPQMNFLHLLIFTAYRKDKETYLSLVQKYPKKQDWEAALAKIEEIYFGIRPVSNQPNILANLMSSLFSGPPAATNQLDLE
Protein: Cadherin domain-containing protein (Q8CAC6)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MDLLSGTYIFAVLLACVVFQSGAQEKNYTVREEMPENVLIGDLLKDLNLSLIPDKSLTTPMQFKLVYKTGDVPLIRIEEGTGEIFTTGARIDREKLCAGIVLDARCFYEVEVAVLPDEIFRLVKIRFLIEDINDNAPLFPTTVINISIPENSAINSRYSLPAAIDPDIGINGVQNYQLIKSQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVADTNDNHPIFIEKEIEVSIPENAPIGSSVTQLHATDADIGENARIHFYFSNLVSNIAKRLFHLNTTTGLITVKEPLDREESPSHKLLVLATDGGSTPARATVLVNVTDINDNIPSIDIRYIVNPTNGTVLLSENAPLNTKIALITVMDKDSEHNGRVTCFTDHEVPFRLRPVFSNQFLLETAAFLDFESTREYAIKLLAADAGKPPLNQSSMLLIKV
Protein: LD32469p (SR family splicing factor SC35) (SR family splicing factor SC35, isoform C) (SR family splicing factor SC35, isoform D) (Q9V3T8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD40489p
- RNA-binding protein 1
- Splicing factor U2af 38 kDa subunit
- LD29830p
- Splicing factor U2AF 50 kDa subunit
- Transformer-2 sex-determining protein
- U1 small nuclear ribonucleoprotein 70 kDa
- Heterogeneous nuclear ribonucleoprotein A1
- Serine/arginine repetitive matrix protein 1
- Serine/arginine-rich splicing factor x16
Sequence:
MSNGGGAGGLGAARPPPRIDGMVSLKVDNLTYRTTPEDLRRVFERCGEVGDIYIPRDRYTRESRGFAFVRFYDKRDAEDALEAMDGRMLDGRELRVQMARYGRPSSPTRSSSGRRGGGGGGGSGGRRRSRSRSPMRRRSRSPRRRSYSRSRSPGSHSPERRSKFSRSPVRGDSRNGIGSGSGGLAPAASRSRSRS