wanglab/gogpt-training-data huggingface dataset:
Protein: Crossover junction endonuclease MMS4 (EC 3.1.22.-) (P38257)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably occurs approximately half a helical turn upstream of the free 5'-end in these structures. May be required in mitosis for the processing of stalled replication fork intermediates arising spontaneously or subsequent to treatment with DNA damaging agents such as methylmethane sulfonate (MMS), camptothecin (CPT) or UV. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). This involves consecutive cleavage of D-loops and nicked Holliday junctions leading to sister chromatid crossover. In contrast to MSH4-MSH5 dependent crossover, double Holliday junctions do not seem to be involved. Spore formation and viability are severely impaired in deletion strains.
Subcellular location: Nucleus {ECO:0000269|PubMed:14642571}.
Interaction partners:
- Crossover junction endonuclease MUS81
- ATP-dependent helicase SGS1
- Holliday junction resolvase YEN1
- ATP-dependent DNA helicase SRS2
- RecQ-mediated genome instability protein 1
- DNA topoisomerase 3
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- ATP-dependent DNA helicase MPH1
- Structure-specific endonuclease subunit SLX4
- Regulator of Ty1 transposition protein 107
Sequence:
MSQIVDFVEDKDSRNDASIQIIDGPSNVEIIALSESMDQDECKRAHVSSAEMIPSSPQRKSVSNDVENVDLNKSIELSAPFFQDISISKLDDFSTTVNSIIDSSLRNENNAKGNAKKLLDDLISDEWSADLESSGKKHNKSQYNLRDIAEKWGVQSLKNPEPIAVDCEYKTQGIGKTNSDISDSPKSQIGAADILFDFPLSPVKHENPTEEKHNSIANENSSPDNSLKPAGKQNHGEDGTSMAKRVYNKGEDEQEHLPKGKKRTIALSRTLINSTKLPDTVELNLSKFLDSSDSITTDVLSTPAKGSNIVRTGSQPIFSNANCFQEAKRSKTLTAEDPKCTKNTAREVSQLENYIAYGQYYTREDSKNKIRHLLKENKNAFKRVNQIYRDNIKARSQMIIEFSPSLLQLFKKGDSDLQQQLAPAVVQSSYNDSMPLLRFLRKCDSIYDFSNDFYYPCDPKIVEENVLILYYDAQEFFEQYTSQKKELYRKIRFFSKNGKHVILILSDINKLKRAIFQLENEKYKARVEQRLSGTEEALRPRSKKSSQVGKLGIKKFDLEQRLRFIDREWHVKIHTVNSHMEFINSLPNLVSLIGKQRMDPAIRYMKYAHLNVKSAQDSTETLKKTFHQIGRMPEMKANNVVSLYPSFQSLLEDIEKGRLQSDNEGKYLMTEAVEKRLYKLFTCTDPNDTIE
Protein: BMK1/ERK5 protein (O89037)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
DNTKAALKAALLKSLRSRLRDGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERGAGTLGGPSTDPLAGLVLSDNDRSLLERWTRMARPPVPAPAPAPAPAPTPTPTPTPTPTQSSAQPTSPPNGPVSQTTAPLQPAGSIPGPASQPACPPPGPVPQPAGPVPAPLQTAPSTSLLASQSLVPPSGLPGSGAPEVLPYFPSGPPPPDPGLTPQPSTSESPDVNLVTQQLSKSQVEDPLPPVFSGTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDSQADSASLSASLLADWLEGHGMNPADIESLQREIQMDSPMLLSDLPDLQEP
Protein: RNA polymerase II subunit A C-terminal domain phosphatase SSU72 (CTD phosphatase SSU72) (EC 3.1.3.16) (Q9C9T0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU369031}.
Interaction partners:
Sequence:
MRFRYAMVCSSNQNRSMEAHALLKRQGLDVASYGTGSHVKLPGPSLREPNVYDFGTPYKQMFDELRRKDPELYKRNGILQMIKRNLSVKLAPQRWQDNAGDGVFDVVMTFEEKVFDSVLEDLNNREQSLTKTILVMNLEVKDNHEEAAIGGRLALELCQEIEGNETWEDTIDDIVAGFEKQHRRKLVYSISFY
Protein: Rifin (O97326)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLLYSNILLFALALNILLTSYYAHNKNKPSITPHHTRTTTSRLLSECDTESSIYDSDEEINSVKEIFERQTSRRFEEYEERMITQRQKYKEQRDKDIQKIIHKDKMEKNLAEKIEKGCLRCGCGLGSVAGSIGLFGAVAINIWKPAALDAAIAKAITEGTANISAAGVKAGEATGKVLVISGLKKMGISTLGGKNLESYFATTSYKKVASIAQAVYEQHFEKCEFGYLKEGFTPVGDPSRDIHFCQSVWQQTSVVSKTGHYISPKDVIKRTVETMVSKAEGPANAAAEFVKATETATIKAAEEKTIETASTQLYSAIGYSILAILIIVLIMLIIYLILRYRRKKKMKKKAQYTKLLNE
Protein: GH01528p (Q8T0V5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MDKGTMKRKQRRYRTTFNTLQLQELERAFQRTHYPDVFFREELAVRIDLTEARVQVWFQNRRAKWRKQEKIGGLGGDYKEGALDLDVSYDDSAVLGQLDSALGGGGTLLPDTPPQSSNSLDNELKASYGTGAMSPSRLSPNIFLNLNIDHLGLERGGSGLSMEWSTYPPQTQAQTHPQMDSDNQLQQHPPQQHASDPIHAGSSSHHQQQQQQHQQEQHNPQLHPGLEFAASLSLDMTDGSSAYDEMKFLSADVDQFTIDSFKADCILSMEQSQMQAYGGHSQLVGSSNELCLDGIGMSSFGMEEGEPKSPPSLLVLDKSLPSLSIGVEGIADLVEQLHHHQHEGGPVGGGVITGDVM
Protein: Copine-8 (Copine VIII) (Q86YQ8)
Organism: Homo sapiens (Human)
Function: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes.
Interaction partners:
Sequence:
MDSRYNSTAGIGDLNQLSAAIPATRVEVSVSCRNLLDRDTFSKSDPICVLYVQGVGNKEWREFGRTEVIDNTLNPDFVRKFILDYFFEERENLRFDLYDVDSKSPNLSKHDFLGQVFCTLGEIVGSQGSRLEKPIVGIPGKKCGTIILTAEELNCCRDAVLMQFCANKLDKKDFFGKSDPFLVFYRSNEDGSFTICHKTEVVKNTLNPVWQAFKISVRALCNGDYDRTIKVEVYDWDRDGSHDFIGEFTTSYRELSRGQSQFNVYEVVNPKKKGKKKKYTNSGTVTLLSFLVETEVSFLDYIKGGTQINFTVAIDFTASNGNPAQPTSLHYMNPYQLNAYGMALKAVGEIVQDYDSDKMFPALGFGAKLPPDGRISHEFALNGNPQNPYCDGIEGVMEAYYRSLKSVQLYGPTNFAPVINHVARYASSVKDGSQYFVLLIVTDGVISDMAQTKESIVNASKLPMSIIIVGVGPAEFDAMVELDGDDVRVSSRGKYAERDIVQFVPFRDYIDRSGNHILSMARLAKDVLAEIPEQFLSYMRARGIKPSPAPPPYTPPTHVLQTQI
Protein: Protein wntless homolog (Integral membrane protein GPR177) (Protein evenness interrupted homolog) (EVI) (Putative NF-kappa-B-activating protein 373) (Q5T9L3)
Organism: Homo sapiens (Human)
Function: Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins. Plays also an important role in establishment of the anterior-posterior body axis formation during development (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16678095}; Multi-pass membrane protein {ECO:0000269|PubMed:16678095}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16678095}; Multi-pass membrane protein {ECO:0000269|PubMed:16678095}. Cell membrane {ECO:0000269|PubMed:18160347}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18160347}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18160347}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:18160347}; Multi-pass membrane protein {ECO:0000255}. Note=Co-localizes with the adaptin AP2A2 at distinct punctae. {ECO:0000269|PubMed:18160347}.
Interaction partners:
- Protein Wnt-3a
- Protein Wnt-8a
- Protein Wnt-5a
- Proto-oncogene Wnt-1
- Protein Wnt-4
- Sorting nexin-3
- Protein Wnt-7a
- Protein Wnt-16
- Proto-oncogene Wnt-3
- Protein Wnt-7b
Sequence:
MAGAIIENMSTKKLCIVGGILLVFQIIAFLVGGLIAPGPTTAVSYMSVKCVDARKNHHKTKWFVPWGPNHCDKIRDIEEAIPREIEANDIVFSVHIPLPHMEMSPWFQFMLFILQLDIAFKLNNQIRENAEVSMDVSLAYRDDAFAEWTEMAHERVPRKLKCTFTSPKTPEHEGRYYECDVLPFMEIGSVAHKFYLLNIRLPVNEKKKINVGIGEIKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRRITMMSRPPVLLEKVIFALGISMTFINIPVEWFSIGFDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQHERNHIAGYWKQVGPIAVGSFCLFIFDMCERGVQLTNPFYSIWTTDIGTELAMAFIIVAGICLCLYFLFLCFMVFQVFRNISGKQSSLPAMSKVRRLHYEGLIFRFKFLMLITLACAAMTVIFFIVSQVTEGHWKWGGVTVQVNSAFFTGIYGMWNLYVFALMFLYAPSHKNYGEDQSNGDLGVHSGEELQLTTTITHVDGPTEIYKLTRKEAQE
Protein: Superkiller complex protein 8 (WD repeat-containing protein 61) (H0YN81)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTNQYGILFKQEQAHDDAIWSVAWGTNKKENSETVVTGSLDDLVKVWKWRDERLDLQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQIKSIDAGPVDAWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHTFFDHQDQVWGVKYNGNGSKIVSVGD
Protein: Protein-arginine N-acetylglucosaminyltransferase SseK3 (Arginine GlcNAcyltransferase SseK3) (EC 2.4.1.-) (Salmonella secreted effector K3) (P0DUJ7)
Organism: Salmonella typhimurium (strain SL1344)
Function: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling and apoptosis. Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as TRADD, TNFRSF1A/TNFR1 and TNFRSF10B/TRAILR2: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling. Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host small Rab GTPase (Rab1, Rab5 and Rab11), thereby preventing GTPase activity and leading to impaired host vesicular protein transport. Also mediates auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins.
Subcellular location: Secreted {ECO:0000269|PubMed:21445262}. Host Golgi apparatus {ECO:0000269|PubMed:26394407, ECO:0000269|PubMed:32432056, ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215}. Note=Secreted via type III secretion system 2 (SPI-2 T3SS) (PubMed:21445262). Localizes to host Golgi apparatus via lipid-binding (PubMed:32504010). {ECO:0000269|PubMed:21445262, ECO:0000269|PubMed:32504010}.
Interaction partners:
Sequence:
MFSRVRGFLSCQNYSHTATPAITLPSSGSANFAGVEYPLLPLDQHTPLLFQWFERNPSRFGENQIPIINTQQNPYLNNIINAAIIEKERTIGVLVDGNFSAGQKKALAKLEKQYENIKVIYNSDLDYSMYDKKLSDIYLENIAKIEAQPANVRDEYLLGEIKKSLNEVLKNNPEESLVSSHDKRLGHVRFDFYRNLFLLKGSNAFLEAGKHGCHHLQPGGGCIYLDADMLLTGKLGTLYLPDGIAVHVSRKGNSMSLENGIIAVNRSEHPALKKGLEIMHSKPYGDPYIDGVCGGLRHYFNCSIRHNYEEFCNFIEFKHEHIFMDTSSLTISSWR
Protein: Potassium-transporting ATPase alpha chain 1 (EC 7.2.2.19) (Gastric H(+)/K(+) ATPase subunit alpha) (Proton pump) (P09626)
Organism: Rattus norvegicus (Rat)
Function: The catalytic subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Uses ATP as an energy source to pump H(+) ions to the gastric lumen while transporting K(+) ion from the lumen into the cell. Remarkably generates a million-fold proton gradient across the gastric parietal cell membrane, acidifying the gastric juice down to pH 1 (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). The release of the H(+) ion in the stomach lumen is followed by binding of K(+) ion converting the pump conformation back to the E1 state (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P20648}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the apical canalicular membrane of parietal cells (By similarity). {ECO:0000250|UniProtKB:P20648}.
Interaction partners:
- Potassium-transporting ATPase subunit beta
- Phospholysine phosphohistidine inorganic pyrophosphate phosphatase
- inorganic diphosphatase
- Potassium-transporting ATPase alpha chain 2
- Gastrin
- Sodium/potassium-transporting ATPase subunit beta-1
- Histamine H2 receptor
- V-type proton ATPase subunit d 2
- Vacuolar proton pump subunit B
Sequence:
MGKENYELYSVELGTGPGGDMAAKMSKKKAGGGGGKKKEKLENMKKEMEMNDHQLSVSELEQKYQTSATKGLKASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLALALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILSAQGCKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTAQGLVVSTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFVVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQLYLNEKDYPPGYTFDVEAMNFPSSGLCFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRMPVDQVNKKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPRNPRRDRLVNEPLAAYSYFQIGAIQSFAGFADYFTAMAQEGWFPLLCVGLRPQWEDHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEMCQIADVLIRKTRRLSAFQQGFFRNRILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPMPFGLLIFVYDEIRKLGVRCCPGSWWDQELYY
Protein: SHSP domain-containing protein (Q19228)
Organism: Caenorhabditis elegans
Interaction partners:
- DNaJ domain
- Thioredoxin domain-containing protein
- Heat shock 70 kDa protein 13
Sequence:
MSVSPFFNPKRDSQLGEMMRDMGGMQRRLMPISGTFNPMTDDSEIMNSNDKFAVNLNVSNFKPEELKVNLEGRQLSIQGEHDVENEHGASRKSFSRMILLPEDVDITSVATNLSNDGKLCIEAPKLEGVCGRSVPVKEASMDHHHIE
Protein: Serine hydroxymethyltransferase (EC 2.1.2.1) (Q5U3Z7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Methylenetetrahydrofolate dehydrogenase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Phosphoserine phosphatase
- Bifunctional purine biosynthesis protein ATIC
- Methylenetetrahydrofolate reductase
- Thymidylate synthase
- Dihydrofolate reductase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
Sequence:
MVPFSLLRTTRPLQRCGQLVCMAARAQHSEVAQKQAGEAAGGWTGQESLSDSDPEIWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLIDYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKYADIVTTTTHKTLRGARSGLIFYRKGVRTVDPKTGQEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKRKTAKLQDFKSFLLKDPETSQRLANLRQQVEQFARGFPMPGFDER
Protein: Uncharacterized protein (Q55BT6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MKLLYIVVFLLFAIKLCCSEYCGETYCVENRNCYSFIGCRNSTCLYETIDLDDEVDCTVDTCSDRYGVKNTPNNSLCPPENLCDMFLCDTQSGCVAIPKVNCPAPNPCQIPLGCNRETGICEYDEIDCHDDNECTNDYCDPILGECVHFSNDTICSNKASNFSTCVLSGVCGEFGCKYVEDNCNDGNPCTDDYCDFKNGCVSQKNDWNCDSLSACSEGICTDNGCVQQEVDCDDDNPCSEDFCHPLFGCGSILNDTICTNGNKCVNSTCTEDGCSLPVPIVCQDGNPCSDDTCNPSTGCQFTLNNSNCNDGKKCTIDQCGLNGCTHTNITCPPKRVVDIILIGLICRNHYCDQSTGNCVPDMNSVSLLCI
Protein: Protein FLX-like 2 (AtFLXL2) (Q84TD8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has no transcriptional activation activity.
Interaction partners:
- Organic cation/carnitine transporter 5
- Flowering time control protein FPA
- Flowering time control protein FCA
- UDP-N-acetylglucosamine transporter ROCK1
Sequence:
MESKGRIHPSHHHMRRPLPGPGGCIAHPETFGNHGAIPPSAAQGVYPSFNMLPPPEVMEQKFVAQHGELQRLAIENQRLGGTHGSLRQELAAAQHEIQMLHAQIGSMKSEREQRMMGLAEKVAKMETELQKSEAVKLEMQQARAEARSLVVAREELMSKVHQLTQELQKSRSDVQQIPALMSELENLRQEYQQCRATYDYEKKFYNDHLESLQAMEKNYMTMAREVEKLQAQLMNNANSDRRAGGPYGNNINAEIDASGHQSGNGYYEDAFGPQGYIPQPVAGNATGPNSVVGAAQYPYQGVTQPGYFPQRPGYNFPRGPPGSYDPTTRLPTGPYGAPFPPGPSNNTPYAGTHGNPSRR
Protein: BrlA (A0A166TJ10)
Organism: Aspergillus niger
Interaction partners:
Sequence:
MASGCGRVEVPPAPSRKDHLIEETEDMRSQGNMSDRLTIEVDCTSLGSNECPSMASSFSPMESPTPTPTSVYSQGSLASPTWHEGGSYPGQGYERHTGTTPMRSAFRLASMTSNDSMGMSYGQMEAQERMPMTDFLSGYDENVEHFWIPQEAQKAYEHGVPGLPYPQAMPQYSTMGRSSYRQHAAPYLPDSATNPCLSRSIFHQPERVPNSMSMGNVIPWMAPQPDSIAPQTIAPSQVAPVTPPPSYSEFSGSINTFKTHSPTTPVRSCSLGTTSGTDTPMSRLSGGMDYLDDFNQSPVYRDNLARVQRQPSRKVARKQSSKQSLSLENLPSIIKQVQFKCKEPGCKGRFKRQEHLKRHMKSHSKEKPHVCWVPGCERAFSRSDNLNAHYTKTHSKRGGRNRYVATLDENSPDYNPEYRGQLTADGRPVYNSKSQDLMPDARETSEEAWLE
Protein: Small nuclear ribonucleoprotein G (snRNP-G) (Q9CAX7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365052}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein SmD3a
- Small nuclear ribonucleoprotein SmD3b
- Small nuclear ribonucleoprotein E
- Probable small nuclear ribonucleoprotein F
- Sm protein F
- Small nuclear ribonucleoprotein SmD1b
- Small nuclear ribonucleoprotein SmD1a
- PHD finger-like domain-containing protein 5A
Sequence:
MSRSGQPPDLKKYMDKKLQIKLNANRMVVGTLRGFDQFMNLVVDNTVEVNGDDKTDIGMVVIRGNSIVTVEALEPVGRS
Protein: UmuC domain-containing protein (C1F5L8)
Organism: Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB 13165 / 161)
Interaction partners:
- Beta sliding clamp
- Error-prone DNA polymerase
- Protein RecA
- Pyruvate ferrodoxin oxidoreductase
Sequence:
MSRTAEIYACLCVREFPTQALLRLRPQLRNQPCVVMEGEPPLEQVCSLTRKARILGLLPGMTQVEVDTFSGVTVLQRSRKEEITTSEALLECAGSFSPRVEEVSYRHSFVCVVDIAGTQELFGPPNKLAQNLLTRVSALGIAACVGVSSNFHASIAVARAPLALSVRVIPPGEEGAALAALPLTVLNLSEQQAETFSSWGIRNLGMLAALPERELISRLGQPGKHLRQLARGEAPHLFLPVEPEFTLHERMELDSPVAVLDALMFVANLMLEQLIVRATARVLALAAVTVALTLEGGASCLRTIRPALPTNDRPLWIKLLHLDLEAHPPQAAVLAIRLEAEPGSTSQVQMGLFSPQLPEPSRLDVTLARIRSIVGDENVGRAVVADTHRPDGFRLEPFGLDAFENSSAQSKVPSTTTLRSALRRLRPPESVSVTLQGARPEAFFFRQQRYRVEHAYGPWLTTGEWWSAASWGYEQWDLVARNPSGTTLCGCLMRDLLRNQWQMAGLYD
Protein: Putative uncharacterized protein SNHG28 (Small nucleolar RNA host gene 2) (VSIG8 overlapping transcript protein) (VSIG8-OT1) (P0DPA3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGMLAPGPLQGRRPRKGHKGQEDAVAPGCKASGRGSRVTHLLGYPTQNVSRSLRRKYAPPPCGGPEDVALAPCTAAAACEAGPSPVYVKVKSAEPADCAEGPVQCKNGLLVSSPHCEEPCAHSCAHPGLPPHLVHKLPLSYLQTQDTDAASRRINAPLAAGWSWLRLWLVTLASGVDFPQVSAWMRALPSPDCPGLRTTGEQMQKLLLKENKVKTRKSKRRSGEGSHLTTSILEQ
Protein: Bone morphogenetic protein 1 (BMP-1) (EC 3.4.24.19) (Mammalian tolloid protein) (mTld) (Procollagen C-proteinase) (PCP) (P13497)
Organism: Homo sapiens (Human)
Function: Metalloprotease that plays key roles in regulating the formation of the extracellular matrix (ECM) via processing of various precursor proteins into mature functional enzymes or structural proteins. Thereby participates in several developmental and physiological processes such as cartilage and bone formation, muscle growth and homeostasis, wound healing and tissue repair. Roles in ECM formation include cleavage of the C-terminal propeptides from procollagens such as procollagen I, II and III or the proteolytic activation of the enzyme lysyl oxidase LOX, necessary to formation of covalent cross-links in collagen and elastic fibers. Additional substrates include matricellular thrombospondin-1/THBS1 whose cleavage leads to cell adhesion disruption and TGF-beta activation.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:12637569}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12637569}. Secreted {ECO:0000269|PubMed:33206546}. Note=Co-localizes with POSTN in the Golgi. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform BMP1-3]: Secreted {ECO:0000269|PubMed:21453682}.
Interaction partners:
- Chordin
- Periostin
- Complement C1r subcomponent
- Fibronectin
- Procollagen C-endopeptidase enhancer 1
- Bone morphogenetic protein 2
- Complement C1s subcomponent
- Lysyl oxidase homolog 2
- Lysyl oxidase homolog 3
- Protein-lysine 6-oxidase
Sequence:
MPGVARLPLLLGLLLLPRPGRPLDLADYTYDLAEEDDSEPLNYKDPCKAAAFLGDIALDEEDLRAFQVQQAVDLRRHTARKSSIKAAVPGNTSTPSCQSTNGQPQRGACGRWRGRSRSRRAATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCPACGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKLPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEAICGGDVKKDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEKPDDIKSTSSRLWLKFVSDGSINKAGFAVNFFKEVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRCEAACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCKEAGCDHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFMEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLATGSRMFLRFYSDNSVQRKGFQASHATECGGQVRADVKTKDLYSHAQFGDNNYPGGVDCEWVIVAEEGYGVELVFQTFEVEEETDCGYDYMELFDGYDSTAPRLGRYCGSGPPEEVYSAGDSVLVKFHSDDTITKKGFHLRYTSTKFQDTLHSRK
Protein: Lipopolysaccharide induced TNF factor (I3L1P1)
Organism: Homo sapiens (Human)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004125}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004414}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004630}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004630}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004630}.
Interaction partners:
Sequence:
MSVPGPYQAATGPSSAPSAPPSYEETVAVNSYYPTPPAPMPGPTTGLVTGPDGKGMNPPSYYTQPAPIPNNNPITVQTVYVQHPITFLDRPIQMCCPSCNKMIVSQLSYNAGALTWLSCGSLCLLGQECSGTIVAL
Protein: Prolactin (PRL) (P21993)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted.
Interaction partners:
Sequence:
MARRSQGTKLHLAVLCLVVSCHAIGLSDLMERASQRSDKLHSLSTSLTKDLDSHFPPMGRVMMPRPSMCHTSSLQTPKDKEQALKVSENELISLARSLLLAWNDPLLLLSSEAPTLPHPSNGDISSKIRELQDYSKSLGDGLDIMVNKMGPSSQYISSIPFKGGDLGNDKTSRLINFHFLMSCFRRDSHKIDSFLKVLRCRATKMRPEAC
Protein: UPF0654 protein C869.09 (Q9URZ2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized methyltransferase C70.08c
- Probable secreted beta-glucosidase C2G2.17c
- Uncharacterized amino-acid permease C74.04
- Zinc finger protein klf1
- Antisense-enhancing sequence 1
Sequence:
MPDPAHIIAGHKAALSNPHVSEEAKERARKYLKEHGSESHYTTGTTRGQKADADDAGELREEGFGTKNQFEDNESQAKNLGNVRGGYKAAMHNPKVSQKGRRHAKELLEEVDDESK
Protein: Mitochondrial succinate-fumarate antiporter (Eurofung) (C8VCR9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- Fructose-1,6-bisphosphatase
Sequence:
MSAKGGDGRKPASPAVNLIAGGGAGMMEALVCHPLDTIKVRMQLSRRSTAPGVSQASWFRENRCRDCQEGNRTRSVQGSGAVLGGIIPKMAIRFTSYEQYKQLLADKNTGAVSSKATFLAGLAAGVTEAVAVVNPMEVIKIRLQAQHHSLADPLDAPKYRSAPHALFTVIKEEGFMALYRGVSLTALRQGTNQAANFTAYTELKAFLQRSQPEYSNSQLPSYQTTVIGLISGAVGPFSNAPIDTIKTRLQKTRAEPGQSAVNRIMTIAKDMFKQEGASAFYKGITPRVMRVAPGQAVTFTVYEFLKGKLEASNWAFVGGKYEE
Protein: ATP-binding cassette sub-family G member 1 (EC 7.6.2.-) (ATP-binding cassette transporter 8) (White protein homolog) (P45844)
Organism: Homo sapiens (Human)
Function: Catalyzes the efflux of phospholipids such as sphingomyelin, cholesterol and its oxygenated derivatives like 7beta-hydroxycholesterol and this transport is coupled to hydrolysis of ATP. The lipid efflux is ALB-dependent. Is an active component of the macrophage lipid export complex. Could also be involved in intracellular lipid transport processes. The role in cellular lipid homeostasis may not be limited to macrophages. Prevents cell death by transporting cytotoxic 7beta-hydroxycholesterol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22042635}; Multi-pass membrane protein {ECO:0000269|PubMed:22042635}. Golgi apparatus membrane {ECO:0000269|PubMed:22042635}; Multi-pass membrane protein {ECO:0000269|PubMed:22042635}. Cell membrane {ECO:0000269|PubMed:16702602, ECO:0000269|PubMed:24576892}. Note=Predominantly localized in the intracellular compartments mainly associated with the endoplasmic reticulum (ER) and Golgi membranes.
Interaction partners:
- Apolipoprotein A-I
- Oxysterols receptor LXR-alpha
- Apolipoprotein E
- Oxysterols receptor LXR-beta
- Sterol regulatory element-binding protein 2
- Solute carrier family 53 member 1
- Scavenger receptor class B member 1
- Sterol regulatory element-binding protein 1
- Cytochrome P450 7A1
- Retinoic acid receptor RXR-alpha
Sequence:
MACLMAAFSVGTAMNASSYSAEMTEPKSVCVSVDEVVSSNMEATETDLLNGHLKKVDNNLTEAQRFSSLPRRAAVNIEFRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSRLVRAVREGMCDSDHKRDLGGDAEVNPFLWHRPSEEVKQTKRLKGLRKDSSSMEGCHSFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMGVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGLDREDLHCDIDETCHFQKSEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER