wanglab/gogpt-training-data huggingface dataset:
Protein: Vesicle-associated protein 1-1 (Plant VAP homolog 11) (AtPVA11) (VAMP-associated protein 1-1) (Vesicle-associated protein 27-1) [Cleaved into: Vesicle-associated protein 1-1, N-terminally processed] (Q8VZ95)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of a membrane-cytoskeletal adapter complex that forms a bridge between the endoplasmic reticulum and the plasma membrane. Associates with microtubules.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16227454, ECO:0000269|PubMed:24909329}; Single-pass type IV membrane protein {ECO:0000269|PubMed:16227454}. Protein storage vacuole membrane {ECO:0000269|PubMed:16227454}; Single-pass type IV membrane protein {ECO:0000269|PubMed:16227454}; Cytoplasmic side {ECO:0000269|PubMed:16227454}. Note=Localizes to immobile punctate structures reminiscent of the ER-plasma membrane contact sites. {ECO:0000269|PubMed:24909329}.
Interaction partners:
- Protein NETWORKED 3C
- Synaptotagmin-1
- Oxysterol-binding protein-related protein 3A
- Syntaxin-71
- Signal peptidase complex subunit 1
- Thioredoxin superfamily protein
- Oxysterol-binding protein-related protein 3B
- Protein NETWORKED 4A
- Protein NETWORKED 1A
- Synaptotagmin-5
Sequence:
MSNIDLIGMSNRDLIGMSNSELLTVEPLDLQFPFELKKQISCSLYLTNKTDNNVAFKVKTTNPKKYCVRPNTGVVLPRSTCEVLVTMQAQKEAPSDMQCKDKFLLQGVIASPGVTAKEVTPEMFSKEAGHRVEETKLRVTYVAPPRPPSPVHEGSEEGSSPRASVSDNGHGSEFSFERFIVDNKAGHQENTSEARALITKLTEEKQSAIQLNNRLQRELDQLRRESKKSQSGGIPFMYVLLVGLIGLILGYIMKRT
Protein: Grifin (Galectin-related inter-fiber protein) (Q9D1U0)
Organism: Mus musculus (Mouse)
Interaction partners:
- Beta-crystallin A4
Sequence:
MTLQFEAFCAGGLAPGWSLTVQGHADAGEEKFEINFLTDAGDIAFHVKPRFSSATVVGNAFQGGRWGQEEVSSIFPLTLGEPFEMEVSADAEHFHIYAQEQKVLQFPHRHRPLATITRVRVLSEHRLAQVELAKRSLSWGDGGY
Protein: Insulin-like growth factor 2.S (Insulin-like growth factor 2-A) (xIGF-2) (Insulin-like growth factor II-A) (IGF-II-A) (Q90WW4)
Organism: Xenopus laevis (African clawed frog)
Function: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. Promotes anterior neural development. Acts as a ligand for integrin which is required for IGF2 signaling (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MEQLSCKHRSSSVEAEAQLCRQTESRSTQLPRMSVMRHLFLLSITFLVYTLDSAKAYRATETLCGGELVDTLQFVCGDRGFYFSTNNGRSNRRPNRGIVDVCCFKSCDLELLETYCAKPTKNERDVSTAPATAIPPLSKQDLYHKHHHTKSSKYDIWQRKSIHRLRRGVPAIVRARQYRLLMEKAEEAEQALSHRPLTTLPITRPLRLQQASEPSHN
Protein: Transport and Golgi organization 2 homolog (Ser/Thr-rich protein T10 in DGCR region) (P54797)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6ICL3}. Mitochondrion {ECO:0000269|PubMed:18775783}. Golgi apparatus {ECO:0000250|UniProtKB:Q6ICL3}.
Interaction partners:
- 39S ribosomal protein L40
- Tricarboxylate transport protein, mitochondrial
- Palmitoyltransferase ZDHHC8
Sequence:
MCIIFFKFDPRPVSKNAYRLILAANRDEFYNRPSKLADFWGNNSEILSGLDMEEGKAGGTWLGISTRGKLGALTNYLQPRQEPDARGRGELVSHFLTSDMDSLSYLKKVSTEGHLYNGFNIIAADLSTSKGDVVCYYGNRGEPEPIVLTPGTYGLSNALLETPWKKLCFGKQLFMEAVEQSEALPKDVLVTQLLDVLNNEEAQLPDPAIEDQGQEYVQPILNKYAAVCVRCATYGTRTNTIILVDANGHVTFTERSMLDKDTSRWETNTYEFTLQS
Protein: RAD51-associated protein 1 (HsRAD51AP1) (RAD51-interacting protein) (Q96B01)
Organism: Homo sapiens (Human)
Function: Structure-specific DNA-binding protein involved in DNA repair by promoting RAD51-mediated homologous recombination. Acts by stimulating D-Loop formation by RAD51: specifically enhances joint molecule formation through its structure-specific DNA interaction and its interaction with RAD51. Binds single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures: has a strong preference for branched-DNA structures that are obligatory intermediates during joint molecule formation. Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during homologous recombination and DNA repair. WDR48/UAF1 and RAD51AP1 also have a coordinated role in DNA-binding to promote USP1-mediated deubiquitination of FANCD2. Also involved in meiosis by promoting DMC1-mediated homologous meiotic recombination. Key mediator of alternative lengthening of telomeres (ALT) pathway, a homology-directed repair mechanism of telomere elongation that controls proliferation in aggressive cancers, by stimulating homologous recombination. May also bind RNA; additional evidences are however required to confirm RNA-binding in vivo.
Subcellular location: Chromosome {ECO:0000269|PubMed:26323318, ECO:0000269|PubMed:31400850}. Nucleus {ECO:0000269|PubMed:26323318}. Chromosome, telomere {ECO:0000269|PubMed:31400850}. Note=Colocalizes with RAD51 to multiple nuclear foci (By similarity). Colocalizes with DMC1 on meiotic chromatin (By similarity). {ECO:0000250|UniProtKB:Q8C551}.
Interaction partners:
- DNA repair protein RAD51 homolog 1
- WD repeat-containing protein 48
- Ubiquitin carboxyl-terminal hydrolase 1
- Partner and localizer of BRCA2
- Exonuclease 1
- Condensin complex subunit 3
- Maternal embryonic leucine zipper kinase
- Disks large-associated protein 5
- Ubiquitin carboxyl-terminal hydrolase 46
- Kinesin-like protein KIF11
Sequence:
MVRPVRHKKPVNYSQFDHSDSDDDFVSATVPLNKKSRTAPKELKQDKPKPNLNNLRKEEIPVQEKTPKKRLPEGTFSIPASAVPCTKMALDDKLYQRDLEVALALSVKELPTVTTNVQNSQDKSIEKHGSSKIETMNKSPHISNCSVASDYLDLDKITVEDDVGGVQGKRKAASKAAAQQRKILLEGSDGDSANDTEPDFAPGEDSEDDSDFCESEDNDEDFSMRKSKVKEIKKKEVKVKSPVEKKEKKSKSKCNALVTSVDSAPAAVKSESQSLPKKVSLSSDTTRKPLEIRSPSAESKKPKWVPPAASGGSRSSSSPLVVVSVKSPNQSLRLGLSRLARVKPLHPNATST
Protein: GPI mannosyltransferase 3 (EC 2.4.1.-) (GPI mannosyltransferase III) (GPI-MT-III) (Glycosylphosphatidylinositol-anchor biosynthesis protein 10) (TbGPI10) (P86935)
Organism: Trypanosoma brucei brucei
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MPWWLISLTFIYRLFLCATIRTVEAPDEWWQSTEVAYNMVFGKGHLPWEWRYGLRSVLFPAVVALPFYLLKLLGRDTTWAVWFAPRVLQALVLTLIDVSVFCMGATLDELLAKRELELAEETRQSKTKGFSYFCEVSVSRSRRGICNSISYTALLLSLSNWYMAYCGVRLYGNVIEALLVLLTLQQRRYVPFLLLTGLASAIRVTSAVVLSPLVFRHLANATREHGFIRGLFRIVLTGLIVLVAVLGGVMVLDYCFYGRWVLTPLAFFRFNVLHNLSRFFGEHPWYFYVGPVLVGIVGPHVLFTIAAPLVLWRDTASRAVSRPVLGMLGIGAWTLGFYSLIDHKEMRFVFVVIPLSLITAAFVLVRWSRTSAVVVKMNRLFVLFNIVMIYLMGYVYRRGPLDVMAEVRDGPRINRLDVIATCYTVPGYSYMHKKVNHLGFVDCSIDLDEKTGLPKVTEDIMFRRYPKEYVLWRYDGKHSFNMSDLEESRKASELQSVVMPKSAPHPDAMVMTRAVAKEIEEPFLKRHGYRLYRTFLHSPLTLAPYEDIYIQMWVKVTK
Protein: SD03094p (Q960G3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endosome {ECO:0000256|ARBA:ARBA00004177}.
Interaction partners:
Sequence:
MEAVPRLHMLWFALKSSPEGTSFAALKKYIAEFYHEDPEAYSKEVHALETLRNQAMHTTKDGAPVMKRYYCQLHALQNRFPQLADRGIFTFKWKDLYHSAVHEVTDLRFERAAVLFNIAALHTQSGASVTRGDVDGMKMACTHFQAAAWAYGELRERYANVNGGGDFMTPELLVFQQQVCFAQAQECILEKSLIDNRKPHIVAKVTAQIVVYYGAALAALLTGGDDGPVAQVIDSSVYKLWKKYVRFKINYLTCILYLYQGQHSEEKRQMGERVTLYQASWDKLEEARKESKGLPDQREINESLSFTADVVEAKRKNAKNENEFIYHEAVPELSTIAAVQGANLVNGIGFQVSDEEHAGPDIFARLVPMKAHEASSLYSEEKAKLLRKYGALLEEKDTQLESYMSSLTLDNLNINEEQANKLPQGIVDRCAALNANKTAISDLVEAMSQLAEITADVETNLGEISSMLEAEAKAEREFQSATGVQRTPNAHITELSREFQKYSEAHARAGESNNTLRKAMSLHVNNLKILARPLPEIQQLMPKLSSELNTTEIFRDVKLILNKVNEMKAQRAQFHADLRIAINEDDITGKVIAHGGQEGLQALFATELGKHDKITELLDQNMVAQGNILQALTENYAKAAPVLKTLQDVKQKREHFYSSLAASYDVYEDLLAKSAKGLEFYKKLAGNVQKLLTRFRSARDVQSEERQQRMQSVKAATTPVVSKPIAETTPVPAVSSTPKLRDYLKAKAAMADASNPAYVPTVRPVPVGSENPTQAACSYATAPPNEPPPPYSLTQQQYFDPSAAGYTNPMYQQQQQHIAPPAYKAQASPNSQTLHGALGQMNLQGQSQDNNQAGMAYNYGYPSGSVPPLAYAPPGTVPASSASQGLNIQQPLYVATSGNPVSVSNPSELPSTLQAPFVVNPMSNPYQTAAGYSGQAYQQVNAQAQQVTYPTAPSGSSTGQSAQQPLGYAPSQGPQQQAGGYPQSQTPQQQVGAYQQQPLSGYAQQLTPQQQTGYSQSQAPQLQAPSYAQNQQSTGQAQQQTPQQQQTGYPQTPQQHLAGYAQSQQQATGYPQSQTSQQQTTGYSQSQTPQQPLAYQQQPSGYPQQQQQQSLAPQQPSLYPSQAVQASPQPIPGQQATPPNAGQPLPYPQQYTDPNATPAPAPGVSSVPSPVPVPTPAPTSSQAQVPTSPHPSATYSSYSNHPGYSFNPQTGKYEYSSGYQQDTSSLKGSQASQSYQFSQSGKQQSVGTTDSEIASRSNTATGFDPPIVSHTKVNMAAKDSISAIEGNESSNYYSTPYGYLGSVNPQQQPTPAPPSNSNASIYMQSGASSTAETQTTSSGVPYASSAALTKVEPKPEALPPKVTSNVDLLSDLDIDCSVAVPPPMLPQPVLQPHVVATPTPPASQVSVPVKVESVAEHAAPATPEIPVAATEGTAQTPVTIPSGPKCASLDNLSNCSDLSSLENFDWDSVSVTHSVSEKQTKASATANGHSSSFAFQSETFTDEKTTKYFQKEVESYEKLLENLHVKMLNGKTQLGAKWQELQQKLDKEAAANKRSTTIAKLFPEKNRSLDCLPYDHARVKLDKQTDDYINAAYMKNLSAGCPNFIVAQTPQPNTINDFWSMIWSEKSRTVVCLHTPNELFDPYWPQALDQPTHYDDYTVTCLKVQQLSHCSEYQLKLSMHGADAVLDLSLLQLKQWTKGAPAQLLGVAENALETHRQRCKAANAPQSPLIMNCLTGSERSELVAIGVCAIIATQNKQPILINTIDVWSRICAQRQNSLRDSAILEQSMQIVLCNAHNVLNKRGIMTSYQMKMAPQVTAKEQQENKDPLNELDALWKLK
Protein: AF4/FMR2 family member 3 (Lymphoid nuclear protein related to AF4) (Protein LAF-4) (P51826)
Organism: Homo sapiens (Human)
Function: Putative transcription activator that may function in lymphoid development and oncogenesis. Binds, in vitro, to double-stranded DNA.
Subcellular location: Nucleus.
Interaction partners:
- Protein AF-9
- Protein ENL
- Cyclin-dependent kinase 9
- ELL-associated factor 1
- AF4/FMR2 family member 4
- RNA polymerase II elongation factor ELL
- RNA polymerase II elongation factor ELL2
- Cyclin-T1
- AF4/FMR2 family member 1
- RNA polymerase II elongation factor ELL3
Sequence:
MDSFDLALLQEWDLESLCVYEPDRNALRRKERERRNQETQQDDGTFNSSYSLFSEPYKTNKGDELSNRIQNTLGNYDEMKDFLTDRSNQSHLVGVPKPGVPQTPVNKIDEHFVADSRAQNQPSSICSTTTSTPAAVPVQQSKRGTMGWQKAGHPPSDGQQRATQQGSLRTLLGDGVGRQQPRAKQVCNVEVGLQTQERPPAMAAKHSSSGHCVQNFPPSLASKPSLVQQKPTAYVRPMDGQDQAPDESPKLKSSSETSVHCTSYRGVPASKPEPARAKAKLSKFSIPKQGEESRSGETNSCVEEIIREMTWLPPLSAIQAPGKVEPTKFPFPNKDSQLVSSGHNNPKKGDAEPESPDNGTSNTSMLEDDLKLSSDEEENEQQAAQRTALRALSDSAVVQQPNCRTSVPSSKGSSSSSSSGSSSSSSDSESSSGSDSETESSSSESEGSKPPHFSSPEAEPASSNKWQLDKWLNKVNPHKPPILIQNESHGSESNQYYNPVKEDVQDCGKVPDVCQPSLREKEIKSTCKEEQRPRTANKAPGSKGVKQKSPPAAVAVAVSAAAPPPAVPCAPAENAPAPARRSAGKKPTRRTERTSAGDGANCHRPEEPAAADALGTSVVVPPEPTKTRPCGNNRASHRKELRSSVTCEKRRTRGLSRIVPKSKEFIETESSSSSSSSDSDLESEQEEYPLSKAQTVAASASSGNDQRLKEAAANGGSGPRAPVGSINARTTSDIAKELEEQFYTLVPFGRNELLSPLKDSDEIRSLWVKIDLTLLSRIPEHLPQEPGVLSAPATKDSESAPPSHTSDTPAEKALPKSKRKRKCDNEDDYREIKKSQGEKDSSSRLATSTSNTLSANHCNMNINSVAIPINKNEKMLRSPISPLSDASKHKYTSEDLTSSSRPNGNSLFTSASSSKKPKADSQLQPHGGDLTKAAHNNSENIPLHKSRPQTKPWSPGSNGHRDCKRQKLVFDDMPRSADYFMQEAKRMKHKADAMVEKFGKALNYAEAALSFIECGNAMEQGPMESKSPYTMYSETVELIRYAMRLKTHSGPNATPEDKQLAALCYRCLALLYWRMFRLKRDHAVKYSKALIDYFKNSSKAAQAPSPWGASGKSTGTPSPMSPNPSPASSVGSQGSLSNASALSPSTIVSIPQRIHQMAANHVSITNSILHSYDYWEMADNLAKENREFFNDLDLLMGPVTLHSSMEHLVQYSQQGLHWLRNSAHLS
Protein: Trivet, isoform J (A0A0B4LIU0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLAMPTLMMPATAQMTLSAAHGKPYETKLLAIHQTHLQQQQQQQAPAPPQQQQQVQQSQQQAPNGKQQSQQMTIVTTQQQQQQQHPQSQSPHQQQQSQQQAAAAAAAAAAAAHHQQQQAVAAAVCAAQQQAVVVQQQQQQQYQIHSQQQSPQQQQVLCISPKQEQFHIFVGDLSSEIETQQLREAFTPFGEISDCRVVRDPQTLKSKGYGFVSFIKKSEAESAITAMNGQWLGSRSIRTNWATRKPPASKENIKPLTFDEVYNQSSPSNCTVYVGGVNSALTALSEEVLQKTFAPYGAIQEIRVFKDKGYAFVRFSTKEAATHAIVGVHNTEINAQPVKCSWGKESGDPNNAQTIATQALNSAAAAAAGFPYGVGAAAAAAAYGQQLAATGCWYSPTPTYPASSATAAAVTPAAASAAAVQNQFLQGIQGYHFGQYGGYQQGYMGMGVQIPATWQGVTQAQISPAQQLATGVAGTAIPQAAGVVAYPIQQFQVSPQVGDSHSDTDTDT
Protein: Pi-ta protein (Q9AY26)
Organism: Oryza sativa (Rice)
Interaction partners:
Sequence:
MAPAVIASQGVIMRSLTSKLDSLLLQPPEPPPPAQPSSLRKGERKKILLLRGDLRHLLDDYYLLVEPPSDTAPPPDSTAACWAKEVRELSYDVDDFLDELTTQLLHHRGGGDGSSTAGAKKMISSMIARLRGELNRRRWIADEVTLFRARVKEAIRRHESYHLGRRTSSSRPREEDDDDDREDSAGNERRRFLSLTFGMDDAAVHGQLVGRDISMQKLVRWLADGEPKLKVASIVGSGGVGKTTLATEFYRLHGRRLDAPFDCRAFVRTPRKPDMTKILTDMLSQLRPQHQHQSSDVWEVDRLLETIRTHLQDKRYFIIIEDLWASSMWDIVSRGLPDNNSCSRILITTEIEPVALACCGYNSEHIIKIDPLGDDVSSQLFFSGVVGQGNEFPGHLTEVSHDMIKKCGGLPLAITITARHFKSQLLDGMQQWNHIQKSLTTSNLKKNPTLQGMRQVLNLIYNNLPHCLKACLLYLSIYKEDYIIRKANLVRQWMAEGFINSIENKVMEEVAGNYFDELVGRGLVQPVDVNCKNEVLSCVVHHMVLNFIRCKSIEENFSITLDHSQTTVRHADKVRRLSLHFSNAHDTTPLAGLRLSQVRSMAFFGQVKCMPSIADYRLLRVLILCFWADQEKTSYDLTSIFELLQLRYLKITGNITVKLPEKIQGLQHLQTLEADARATAVLLDIVHTQCLLHLRLVLLDLLPHCHRYIFTSIPKWTGKLNNLRILNIAVMQISQDDLDTLKGLGSLTALSLLVRTAPAQRIVAANEGFGSLKYFMFVCTAPCMTFVEGAMPSVQRLNLRFNANEFKQYDSKETGLEHLVALAEISARIGGTDDDESNKTEVESALRTAIRKHPTPSTLMVDIQWVDWIFGAEGRDLDEDLAQQDDHGYGFFILFPGYNLQGLLSFFLSLPWLLSLPAMHLQPDLMIV
Protein: Acryloyl-coenzyme A reductase (Acryloyl-CoA reductase) (EC 1.3.1.84) (A4YGN2)
Organism: Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
Function: Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the acryloyl-CoA dependent NADPH oxidation and formation of propionyl-CoA.
Interaction partners:
- 3-hydroxypropionyl-coenzyme A dehydratase
- Biotin carboxylase
- Biotin carboxyl carrier protein
- Acetyl-CoA carboxylase carboxyltransferase subunit alpha / acetyl-CoA carboxylase carboxyltransferase subunit beta / propionyl-CoA carboxylase carboxyltransferase subunit
- Putative signal-transduction protein with CBS domains
- 3-hydroxypropionyl-coenzyme A synthetase
- Iron-containing alcohol dehydrogenase
- Succinate-semialdehyde dehydrogenase
- Enoyl-CoA hydratase
- NADH:flavin oxidoreductase/NADH oxidase
Sequence:
MKAVVVKGHKQGYEVREVQDPKPASGEVIIKVRRAALCYRDLLQLQGFYPRMKYPVVLGHEVVGEILEVGEGVTGFSPGDRVISLLYAPDGTCHYCRQGEEAYCHSRLGYSEELDGFFSEMAKVKVTSLVKVPTRASDEGAVMVPCVTGMVYRGLRRANLREGETVLVTGASGGVGIHALQVAKAMGARVVGVTTSEEKASIVGKYADRVIVGSKFSEEAKKEDINVVIDTVGTPTFDESLKSLWMGGRIVQIGNVDPTQSYQLRLGYTILKDIAIIGHASATRRDAEGALKLTAEGKIRPVVAGTVHLEEIDKGYEMLKDKHKVGKVLLTT
Protein: Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 [Includes: Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (EC 1.14.11.4) (Lysyl hydroxylase 3) (LH3); Procollagen glycosyltransferase (EC 2.4.1.50) (EC 2.4.1.66) (Galactosylhydroxylysine-glucosyltransferase) (Procollagen galactosyltransferase) (Procollagen glucosyltransferase)] (O60568)
Organism: Homo sapiens (Human)
Function: Multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine. Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues. Essential for normal biosynthesis and secretion of type IV collagens (Probable). Essential for normal formation of basement membranes (By similarity).
Subcellular location: Rough endoplasmic reticulum {ECO:0000269|PubMed:10934207}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:20470363}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9R0E1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9R0E1}; Lumenal side {ECO:0000250|UniProtKB:Q9R0E1}. Secreted {ECO:0000269|PubMed:21465473}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q9R0E1}. Note=The majority of the secreted protein is associated with the extracellular matrix. {ECO:0000250|UniProtKB:Q9R0E1}.
Interaction partners:
- Procollagen galactosyltransferase 1
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
- Procollagen galactosyltransferase 2
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
- Calmodulin-lysine N-methyltransferase
- Collagen alpha-1
- Histone-lysine N-methyltransferase EHMT2
- Collagen alpha-1
- Collagen alpha-3
- Collagen alpha-2
Sequence:
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFLAVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLVGPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRDVFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDWKEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHEGLPTTWGTRYIMVSFVDP
Protein: Killer cell immunoglobulin-like receptor 2DL4 (CD158 antigen-like family member D) (G9P) (Killer cell inhibitory receptor 103AS) (KIR-103AS) (MHC class I NK cell receptor KIR103AS) (CD antigen CD158d) (Q99706)
Organism: Homo sapiens (Human)
Function: Receptor for non-classical major histocompatibility class Ib HLA-G molecules. Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide (peptide-bound HLA-G-B2M). In decidual NK cells, binds peptide-bound HLA-G-B2M complex and triggers NK cell senescence-associated secretory phenotype as a molecular switch to promote vascular remodeling and fetal growth in early pregnancy. May play a role in balancing tolerance and antiviral-immunity at maternal-fetal interface by keeping in check the effector functions of NK, CD8+ T cells and B cells. Upon interaction with peptide-bound HLA-G-B2M, initiates signaling from the endosomal compartment leading to downstream activation of PRKDC-XRCC5 and AKT1, and ultimately triggering NF-kappa-B-dependent pro-inflammatory response.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Early endosome membrane {ECO:0000269|PubMed:16366734}.
Interaction partners:
- Killer cell immunoglobulin-like receptor 2DL3
- HLA class I histocompatibility antigen, alpha chain G
- Killer cell immunoglobulin-like receptor 2DL1
- HLA class I histocompatibility antigen, alpha chain E
- Killer cell immunoglobulin-like receptor 3DL3
- Killer cell immunoglobulin-like receptor 3DL2
- TYRO protein tyrosine kinase-binding protein
- Killer cell immunoglobulin-like receptor 3DL1
- High affinity immunoglobulin epsilon receptor subunit gamma
- Natural cytotoxicity triggering receptor 2
Sequence:
MSMSPTVIILACLGFFLDQSVWAHVGGQDKPFCSAWPSAVVPQGGHVTLRCHYRRGFNIFTLYKKDGVPVPELYNRIFWNSFLISPVTPAHAGTYRCRGFHPHSPTEWSAPSNPLVIMVTGLYEKPSLTARPGPTVRAGENVTLSCSSQSSFDIYHLSREGEAHELRLPAVPSINGTFQADFPLGPATHGETYRCFGSFHGSPYEWSDPSDPLPVSVTGNPSSSWPSPTEPSFKTGIARHLHAVIRYSVAIILFTILPFFLLHRWCSKKKDAAVMNQEPAGHRTVNREDSDEQDPQEVTYAQLDHCIFTQRKITGPSQRSKRPSTDTSVCIELPNAEPRALSPAHEHHSQALMGSSRETTALSQTQLASSNVPAAGI
Protein: BEACH domain-containing protein lvsE (Q54RQ8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Lysosomal alpha-mannosidase
Sequence:
MSVYTQLISVTEMPMSVIHRPLPSELDEEKVLSLMETIKSGVEIPPIDVNWVKGKDENNNYYFSFGGCHRYEATKRLNLKTIRARIIKSTPSDIKVSPRLAQLPSDQSNYNMERLYVQDIFSKIKNKNQPDLSDLIILFDRLTSLAYQDVHSSKKVKFDYFYMFFNIMLDSPILSVTESTGNRVLHLLLLKKLNGLLFSNVLIQNYCHNEKWVYKLLNYLISRSKHDSDVIGELSITLQIICSFNITTKELKYFFKLLESINEERPYYWNVLIEILQFLFRKRVGPDIYFNFSNSNGGLMVPDKQPFDGGYSISFWMNTDDFTSLKYRPGLFSFFSDENVGFEVTFQQQSLIFQIRTKSKSPCIGSHYRFQPGKWYHVIISHEYFLLRKSQLSLYVNGKLEEKMPLLYPKSDRPFTRCHIGNSVSLQNGFLGRIGSILMIKDALEPAEATLLYQIDKNSTMLQEKVPKEGMTAIYDSQLFLASGRRNIPIIFTYHPRATDKALCFEISSGELPNAATIMDGVSILKSVSPLDQLVYIGGLKMIYPLFAQLGQPINGVEIEMPQDISDHMTTSPLPLSNLNDFISIPSSSGPTPIFPSSIGSGHSSCLFKILLSLLQHHPAFREQIIETHGFQVISFLLKSTPTSSPYWTPDDIDSLSRLISFCAGKQPLWSLAIQNLIMNNFQLWSQTNSLTQIALFETIHQRIQTNPQFWRNLVRVDQWLTILRKFYQLPSASSLSPLSLSSNSSSLSASLSPIINSGSWCKESIEKPIFKDLPTIEKIKKARVQIIVIIRETAQPRLSPSETRWLSLYLKESTIENHDDVIRMLEDIIQPLQSKDTWWDDVMASANLQDENLVLKSRKDFQSTQTKLPSHISYLWDIDCCEEVVKRLEEIKYQDRSNLILFKHWVHIRRVRAGNLNGIKTRLTNGNQTNTPILTKLKQMGIIQSPSTSLSTSSITPPPPNSRNTSTGILKNSSIKEKQLFQSNIDSLSFSLKETTTTTTTTTTTTTTSTTSNTGNDSPLSIESPISSPVLIENTTNTTNTTTTNTTNSSMLSIKDYDDGDEPEDTTVVHWKLDRTEGPLRMRRKLKRNYFGSDYKGLSKQNRFGRSRRTTLEKYSNEIETFYIDQDCGDGLGNIIITIVNEPPLPHQTTSYKEIEFFNESQSQSSSSSNIDNLNPNTGLPYNKSTNNLSNVNNVNNNNNNNSNNINVSGNNTIGPSSSKSPLRNSRSMSIGSSATKSPSRQNVKDVFNLDNNNSNSNNNNSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNFNNNLSPTLNSILPNLNNISINSGSNTIGPNSSMSSILSPRIGEFDENGVDVSSPNSSSLSSSSSNNQIEEEKFIGSWRCQMVVPVGVIPGQFTITSHYLTFDKDIQIVDQRTGRTFSPSLNGIQQQQQQQQDQDFGSVKIKNTYIWKVKDLVEIHRVRYLLRWNSIEIFLNHKSYMINFSKEQESIQIFNKIVALHPPNLRVKWSDHPSKIIKKSKLTMKWKNREISNFEYLMSLNTIAGRTYNDISQYPVFPQIISDYKSEFLDLNDSRSFRDLSKPMGALNQQRLDTLIKRYQSMQSAQDPTMPPFLYGSHYSNFGIVAYYQVRLEPFTSFHLSLQSGVFDHPQRMFESMDKMWDGVSGNNLADVKELIPEFFYMPEFINNGEGFNFGFTNSKSGDLILPNWAHQSPELFIQINREALESEYVSMNLHHWIDLIFGFKQNGPAAQEANNVFFHLTYENNAALQRDDPDERQSIASQIKEFGQTPPQLFSKPHPIRKTLQEISKPQKDLFARIAQNLFSPSNNGTINSSFSSTSTSTSTSSPPPSTLNSPQGPSLQYPFKVLKTKSSLPLVHISSCQDSDIVVLVYRDGVMAVNQFVPSPNGNLPFTFDIDKTLSTYKEKQIDTLFMSDSVTCISNCFAITPDGKFMFSCATWDSVFKCSNIQNGRVHRLYRDFHHDMVTCISLGSNGKHFATASSDTTILVWNDVDHLIKDSKAKPSYRLCSHDEPVHCLDINEEWDLIASGSMDKKLILHSLGKGHYQRSMIHNGAVEIVKISTVGQTIISYCSMSFLYVHSFNGKLLKIQQSDEKIYDAKLTGESVKKGGVLGVGSSTQYLVTGGTRGVKVRSLPDLNIVHAFDSPAAIKTIELVAHEKYMLIGLNDGNLVIIPFDVKDL
Protein: Erythrocyte membrane protein band 4.1 like 1 (Q4VXN7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTETGPDSEVKKAQEEAPQQPEAAAAVTTPVTPAGHGHPEANSNEKHPSQQDTRPAEQSLDMEEKDYSEADGLSERTTPSKAQKSPQKIAKKYKSAICRVTLLDASEYECEVE
Protein: TRM7 (A0A384KX90)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDVVERKRPRGAFLNLFDWHGKSRKKLFSSNLSQLSEESKQAKENVQNPSITPHSVFEVDQSVKNPTYNPRSDSSCCASSVTSDDGNVVRASVVARLMGLEGLPLPNVLEPRVNPDLDPYFLRSSRQANTWDANVDRQSDFDGVSWDHLDSRTSKGPRKRMIERFQTETLPPRSAKPISVTHNKLLSPIRNPGFVPSRNPAYVMEAASRMIEQSPRMIARTRMVSSSDSSSPVPLRIRDLKEKLEAAQKASTSVPQISNDTRNSRYLRGDQNEKKTTVLGKNSYDALKGGEVKPPSFAAQAKVSSNQKQDSLSMSSSGNKRMSSGQKEKVEAKNRAVKSQNSSKGSSLSTGKNVLRQNNQKQNCRDNQQSRRVMNKVVNKVLVESGSISKSSGFTMSSAEKPTSLPLSRKKSLPRSKKPRNGVQESGIYEDKRIKRGEKSIKCNISIDGDSSTSKDDQKRDMDVISFTFSSSIKGLSSPHSQGTKQDADSAIRFNVIGGDSLNALLEQKLRELTTKIESSSSSLIQEEPLSSISKDRANAMISSPSKYSGLTQSSLDRVLTESESVSDCTSFFNSQKVQKQKVIQGEEQEVSSITTLTEADDFALSCSKSISDCRHDREYGMKQSSSDQELTWGSSNESQHTLDETESATLDWELEYITEILNSGQLMFQDFASGTTTNESLLPSSLFDEMERSRGAATSMKTERKALFDCVNQCLAVKFERMLIGSCKGMMMSGGILLEHRDLLAEEVNREVKGLKKMREMMIDELVDHDMSCFEGRWIGYEREMFEEGIDMEGEIVSALVDDLVSDILSTSVLKRSLL
Protein: 3-mercaptopropionate dioxygenase (3MDO) (p3MDO) (EC 1.13.11.91) (Q9I0N5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Thiol dioxygenase that catalyzes the dioxygenation of 3-mercaptopropionate (3-MPA) to 3-sulfinopropionate (3-SPA). To a lesser extent (40-fold lower efficiency), is also able to oxidize cysteine to cysteine sulfinate (CSA). Cannot use N-acetyl-L-cysteine, homocysteine, and cysteamine as substrates. The physiological role of this enzyme is unclear.
Interaction partners:
- Probable thiosulfate sulfurtransferase
- Acyl-CoA dehydrogenase
Sequence:
MSSILRLDRLRQFIGELATLLDSRPDESTLLAQAHPLLAELVHQDDWLPEDCARPDPQRYQQYLLHVDSRQRFSVVSFVWGPGQITPVHDHRVWGLIGMLRGAEYSQPYAFDAGGRPHPSGARRRLEPGEVEALSPRIGDVHQVSNAFSDRTSISIHVYGANIGAVRRAVFSAEGEEKPFISGYSNSRLPNIWDLSKENPA