wanglab/gogpt-training-data huggingface dataset:
Protein: Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPI-HBP1) (GPI-anchored HDL-binding protein 1) (High density lipoprotein-binding protein 1) (Q9D1N2)
Organism: Mus musculus (Mouse)
Function: Mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries. Anchors LPL on the surface of endothelial cells in the lumen of blood capillaries. Thereby, plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis. Binds chylomicrons and phospholipid particles that contain APOA5. Binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:20620994}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:25387803}. Basolateral cell membrane {ECO:0000269|PubMed:20620994}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:25387803}. Cell membrane {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:18340083, ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:25387803}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:18340083, ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:25387803}.
Interaction partners:
- Lipoprotein lipase
- Angiopoietin-related protein 4
- Apolipoprotein C-II
- Angiopoietin-related protein 3
- Angiopoietin-like protein 8
- Lipase maturation factor 1
- Apolipoprotein A-V
- Apolipoprotein C-III
- Hepatic triacylglycerol lipase
- Proprotein convertase subtilisin/kexin type 5
Sequence:
MKALRAVLLILLLSGQPGSGWAQEDGDADPEPENYNYDDDDDEEEEEETNMIPGSRDRAPLQCYFCQVLHSGESCNQTQSCSSSKPFCITLVSHSGTDKGYLTTYSMWCTDTCQPIIKTVGGTQMTQTCCQSTLCNIPPWQNPQVQNPLGGRADSPLESGTRHPQGGKFSHPQVVKAAHPQSDGANLPKSGKANQPQGSGAGYPSGWTKFGNIALLLSFFTCLWASGA
Protein: Protein transport protein SEC16A homolog (Protein MAIGO 5) (Q9FGK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for efficient protein export from the endoplasmic reticulum (ER) to the Golgi by regulating COPII coat dynamics at the ER. Functions as a scaffold and regulator of COPII coat assembly at ER exit sites.
Subcellular location: Golgi apparatus, Golgi stack {ECO:0000269|PubMed:24280388}. Endoplasmic reticulum {ECO:0000269|PubMed:24280388}. Note=Localizes at Golgi-associated cup-shaped endoplasmic reticulum exit sites. {ECO:0000269|PubMed:24280388}.
Interaction partners:
- Protein transport protein SEC13 homolog A
- Protein transport protein SEC13 homolog B
- Protein transport protein SEC23 D
- Protein transport protein SEC31 homolog B
- Protein transport protein SEC24 A
- Protein transport protein SEC24 C
- Protein transport protein SEC31 homolog A
- Protein transport protein SEC24 B
- Small COPII coat GTPase SAR1B
- small monomeric GTPase
Sequence:
MASTADFLLDDQTDEDFFDKLVDDSYTPTASSSAKELKFDDGSDSDDAKAFANLSVVDDVLGDGDVALNEAGLGNDVANEGTSGSVGKEEPSSSIAPEAVQFVNSDANRLRDVDVVRSEVDDMALTETGKESNIVDGSGSPGVKEVDWGSFYADSSVNDGGGFGSYSDFFTELDATAGNVQGQAEVAVATGGNLVANDTINTSVGLDNSAGFEQHQGQVQHDSGSGQYVDNSQSWENLYPGWKYDASTGQWYQVDGQDATVNSQESYINSTGNWESVAADNSDVAYLKQSTTSAMAGTAESVSTWNQVSQVGNGYPEHMVFDAQYPGWYYDTIAQEWRSLDSYNQASQTTVTGQAHDQQVQNGHARTTTYHNNSQSSVYDVNNKNQTFKAQDFAIQGQHGSWDESYYANNQQAGNTWQPVNVGKAEPAVTSDSLSRFGGNQQVNNLYSTESVAEQFKPNTIGAQSFIPQHMNVASATQNGPLSFSNDLYNRQQSVDHAQKSFQNNQLFSPSVGRSSDRRPPHALVSFGFGGKLIVMKDNNGSLQNTSFGSQGIGGSSITVLNLAEVISGSASYSSPGEDSLSYFRCLHQQSLPGPLVGGNVGSKELHKWIDERLLHCESSNMDFSRGKLLKMLLSLLRISCQYYGKLRSPFGSDASQKETDTPEAAVAKLFAFAKKDGIQNGYAPISQCLQHLPPESQMQVTASEVQNLLASGRKMEALQCAQEGHLWGPALVIAAQLGDQFYVDTVKQMALRQLIPGSPLRTLCLLVAGQPAEVCPTGSSSSMLDNWEENLGIITANRTTDDDLVIIHLGDSMWKERGEIIAAHICYLIADKNFDPYSESARLCLVGADHWKCPRTYASPDAIQRTELYEYSKTLGNSQYILLPFQPYKIIYAHMLAEVGKLSTAQKYCQAVIRCLKTSRSSEVEMWKQFASSLEERIRSHQEGGNLAPAKLVGKLLNSLWGMPPPAPHSTTGNPQVNEYQHQQQEAAKLSYSQSANTMSSLMPPASIEPVHEWGGNGRTMAAHSRSVSEPDFSRTPIQDQTDSSKDKAPDGVTQVKSTRKVPSSRFSRFGIGILKNTVGKVFPSRSSNEAKLGNENQFYYDDNLKRWVERGVEPPAEEAALPPPPTSVPFRSNSLGHENKSEIKNEMSPSSGSWSSGSPTPSENSPGIPPVSQGSNQFSARGRMGVRARYVDTYNQGSSSMYQSPPVQSSKPPIPAKAKFFVPAAPASFANDQVMESVSAETRQENSGDEAVVGSAGAPGPSQASFQSPTPSPIAMQRFPSVDNIRRSGSGTSLNGDLPQSVSRRTASWSGSVNSSSFMSPTSASTFRPSPLNSSSSSLGEELQEVEL
Protein: Prohibitin-2 (B-cell receptor-associated protein BAP37) (BAP-37) (Q5XIH7)
Organism: Rattus norvegicus (Rat)
Function: Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors and sex steroid hormones in the nucleus.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11302691}. Cytoplasm {ECO:0000269|PubMed:11302691}. Nucleus {ECO:0000269|PubMed:11302691}. Cell membrane {ECO:0000250|UniProtKB:Q99623}.
Interaction partners:
- Prohibitin 1
- Prohibitin.
- Complement component 1 Q subcomponent-binding protein, mitochondrial
- Elongation factor Tu, mitochondrial
- ARFGEF family member 3
- Estrogen receptor
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Mitochondrial-processing peptidase subunit beta
- Serine/threonine-protein kinase PINK1, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
Sequence:
MAQNLKDLAGRLPSGPRGMGTALKLLLGAGAVAYGVRESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLRKIRAAQNISKTIATSQNRIYLTADNLVLNLQDESFTRGSDSLIKGKK
Protein: Nociceptin receptor (Kappa-type 3 opioid receptor) (KOR-3) (Orphanin FQ receptor) (P41146)
Organism: Homo sapiens (Human)
Function: G-protein coupled opioid receptor that functions as receptor for the endogenous neuropeptide nociceptin. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling via G proteins mediates inhibition of adenylate cyclase activity and calcium channel activity. Arrestins modulate signaling via G proteins and mediate the activation of alternative signaling pathways that lead to the activation of MAP kinases. Plays a role in modulating nociception and the perception of pain. Plays a role in the regulation of locomotor activity by the neuropeptide nociceptin.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle. Note=Ligand binding leads to receptor internalization into cytoplasmic vesicles, decreasing the amount of available receptor at the cell surface. Internalization requires phosphorylation at Ser-363. Can recycle to the cell membrane.
Interaction partners:
Sequence:
MEPLFPAPFWEVIYGSHLQGNLSLLSPNHSLLPPHLLLNASHGAFLPLGLKVTIVGLYLAVCVGGLLGNCLVMYVILRHTKMKTATNIYIFNLALADTLVLLTLPFQGTDILLGFWPFGNALCKTVIAIDYYNMFTSTFTLTAMSVDRYVAICHPIRALDVRTSSKAQAVNVAIWALASVVGVPVAIMGSAQVEDEEIECLVEIPTPQDYWGPVFAICIFLFSFIVPVLVISVCYSLMIRRLRGVRLLSGSREKDRNLRRITRLVLVVVAVFVGCWTPVQVFVLAQGLGVQPSSETAVAILRFCTALGYVNSCLNPILYAFLDENFKACFRKFCCASALRRDVQVSDRVRSIAKDVALACKTSETVPRPA
Protein: Exonuclease 1 (EC 3.1.-.-) (Q54ED2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch-containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA 3'-5' helicase
- DNA mismatch repair protein Mlh1
- Mismatch repair endonuclease pms1
- ATP-dependent DNA helicase ku70
- DNA mismatch repair protein Msh6
- X-ray repair cross-complementing protein 5
- DNA ligase 4
- Double-strand break repair protein
- DNA mismatch repair protein Msh2
- MutL DNA mismatch repair protein
Sequence:
MGISGLLPALSPVTKAIHVKDYANKRVAIDGYSWLHKGAYSCSQEIVLGIPTRNYINYFISRIKMLISYKVIPVVIFDGGPLPNKKLKEQERLRHREEYKNKAKAYLLEGNKSQANICFQKAVDITPRMAFLLIKELRALKVEYLVAPYEADAQLTYLSITGQVDAIITEDSDLVAFGATHIIFKMDKYGYAQEIKTEDLGSCKKDGYDFIDFNQTMLRQMCILSGCDYLPSLSGMGLKTSFKLLKQHRDIEKVFKYLKREKSNFSQEYEQQFYKADFTFKHQRVFDPVSRILTTLLPLPTIIDSRFLNDNNNNTNDGDSNGDGSSGGSGSGGGFLDFIGPVIDDEIAEKIALGIIDPETHEQFDKTQPYPKNTFTPQPKKLLSPISFNTKEFKNQTNNNNNNNNNIKSNNGTNNKNGMILNEGKLVQKGRNLNDQFTFASNKITQYMTTTTTTTTTTTTTKNNNNNQKQQPMIEDDTGYDFQIDSFEIDDCLNDDDDDESIILSNNLNNQENVLESDCEFDDDDDQRGIDVDDSEKKDSFVLDSDYEDEKEEEEVKSSTFNSSSSISSGNSSKIKKTLVSSKFFVSSESSVLESDDDDGGDDDDDSFNHNQNFSSSGNNIQPNSNIFHNGELSSYGYQKNQKNFKNVNSNSSSNSSNSSNSSSGNSNSGNRIFNSGNSSNKNNTNGGIVKSTLLSSNDRVSLNFFDQFQFDGKKKQSILVSQSRKSFSSPTLSNNEDYDSSFVSSTIPSSIGDDYDQMNSCSNNNNFNYNNSSNFNNNNINNSNNNRNSGFSGFLKRKSSSQTAAPTTPTTPTTPKTSSSSSSTLTNSTITTEHSSYILKKPKYQATSNSPISTLDSSQNYNDQSFISKKAHSFSSLDSDLIFKEDDVDNLIFNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNDNNNKITTPSNKSFNSIVLTTTSATTSITQQDNEIYTTPKKKLPSTPISSSSNDIISKYFSSPSKVGPKSEGAPPTPVNLEGMSLRSVLSLRYQQTMASSPTK
Protein: At5g37530 (NAD(P)-binding Rossmann-fold superfamily protein) (Q08A97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEEKSKYLSLVGAGALIGSISTVALLKLLSRSSLKQLNENPETNFLAGNGIESETRPDTVANGQDLLKDEIVSEHLTRNIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSRSVRHRLRRKHGIEGGIPVVFSLEKPKAKLLPFEGTNGEDENPLDYQVVPGFRVRIIPVLGTIPAIFGQIMASYVITQLAGVQVQMEPIVNLDLDHYRLLHQRLIEHEETVYGTSAEVEVDVEEVMYIVKELWHGRSARDETAKDVGRGMWRAMNELMLVRWDAKKPATVSNLVLLKFKEADEHETKTLEEVKESETEFFERVSCVLKKAELDFYG
Protein: Synaptojanin (N-terminal domain), putative (Q38DV2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVGDFFGNIVIDGESASFVPNDDSYPRLIWNLERQCFVLPSNVAADDAVSHVSKDSEKAVCDVVDDGVMSDASSSGFEEFTPVRCIPCYALFGVLRIGSASILLYVSERERITTLTIGETHDVFAVKQLSWLRLPETASDLSVNKSGDGGDGGSGEKDEASASQGSSQSHAREEMVLEYCRVVDSFCAQSEQHCGASYFYYSPTANLTLEPGDVVKGMKEVLTPSLNGSSVKGGGAFSLAISSEGQISQRVVFQWNSPLLGAFDEVVASLNCDYHVYVPAFIRGIVEATTSPEEGVQMLLINRLSYRWAGTRYNRRGLDNAGSGIAANFSASTLWVFPLASGNEGDKAANEKQRVAAFTILRGSVPRCWSQPANLTFIPTITISSPSSGVDELVLHLNALLALFDGMTSIHCLDTTSLSKAELPISKAFEAAALKLREGNGALSRPVDVYYTKYNVKERRAKNAPYNLMRMEVDTLLNRKNEGGSQFVDFWKFSNEGHPSPSSGSSPPSVPSTADADGATCELVLVHQQKHYVRVNCLDCLDRTNLVQSMIAINILPQMIRYVLGHGEEMNLSDDEDEYEDEDDGSDGARGNGEFHCSVERCKHMWVELGISLSRLYAGSDPHFVDFLLTGEWGPATFDVVRIALRRWWQQNFFDGQKQDAVSLLTCQHDPALFHTQFESPFSRNFSGLNRMVLGGMAAAVLATLVSFSMLFVPRYWMRGEILFFVIFWMSYIALTISRILKDGVSYTNYPLLK
Protein: NPHP1 protein (A7YWF3)
Organism: Bos taurus (Bovine)
Interaction partners:
- Nephrocystin 4
- RPGRIP1 like
- Transmembrane protein 67
- Centrosomal protein of 290 kDa
- Abelson helper integration site 1
- Tectonic family member 1
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- X-linked retinitis pigmentosa GTPase regulator
- Inversin.
- Nephrocystin-3
Sequence:
MLARRQRDPLQSLQRRNQELKQQVDGLLFESRLKGALEASKRRDMYQRCIQLKQAIDENKNALQKLKKADEPAPVGNYYQKKEEEHNLLDKLTHQLQELAVSISRENVPETGALAEREEEENSDEEDEEEDDDEEESEESGGEDEETEEEEEEKQEGESQPEATSGEYIALGDFTAQQVGDLTFKKGEILCIIKKNSDGWWMAKNAKGNEGLIPKTYLEPYNKEGGQESSEGGSEEDTEVGDGTVDGAEVKQRTDSHWSAVRKAISEINTVDVLTAMGAIPAGFRPSTLFQLLEEGNQFRASYFLQPELTPSQLAFRDLMWDAKTGSIRSRPSRVSLILTLWSCKMIPLPGVSIQVLSRHVRLCLFDGSEVLSNIHTVRATWQPKKPKTWTFSPQVTGILPCLLDGDCFIRSNSSSPDLGILFELGISYIRNSTGERGELSCGWVFLKLFDATGIPIPAKTYKLFLNGGTPYEKGVEVDPSVSRRAHGSVFHQLMTMRRQPQLLVKLRSLNRRSRSTLSLLPETLIGSMCCVHLLIFYRQILGDVLLKDRMSLNSADLISNPVLATFPKLLEESDIMDALRSSWAEKESTLKRSEKGDRELLKAVFLLVYHDCALPLLHSALLPPSRWAEEETEAARWKGIADFLKQNQENEGALQVLLSPEGVHEPFDISEQTYDFLGERRKNVT
Protein: Glutathione peroxidase (Q4V6H2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform C
- RE13973p
- 1-Cys peroxiredoxin
- Gamma-glutamyl transpeptidase, isoform A
- Peroxiredoxin-5
- Glutathione S transferase O3
- Pyrimidodiazepine synthase
- Glutathione peroxidase
- glutathione-specific gamma-glutamylcyclotransferase
- glutathione-specific gamma-glutamylcyclotransferase
Sequence:
MFDKEFLFPGLLVAVALVVVLQTRSRLQQDLQDMRWRLTIHALTVRDTFGNPVQLDTFAGHVLLIVNIASKCGLTLSQYNGLRYLLEEYEDQGLRILNFPCNQFGGQMPESDGQEMLDHLRREGANIGHLFAKIDVKGAQADPLYKLLTRHQHDIEWNFVKFLVDRKGNIHKRYGAELEPVALTDDIELLLGR
Protein: Copper-sensing transcriptional repressor CsoR (Copper-sensitive operon repressor) (O32222)
Organism: Bacillus subtilis (strain 168)
Function: Copper-sensitive repressor that has a key role in copper homeostasis. Negatively regulates expression of the copZA operon and of ycnJ. In the absence of copper ions, binds with high affinity to the copZA promoter and represses the transcription. In the presence of copper ions, CsoR binds Cu(1+), which significantly decreases its DNA binding affinity and leads to the transcription of the genes.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Copper chaperone CopZ
- HTH-type transcriptional regulator CueR
- Copper transport protein CutJ
- HTH-type transcriptional repressor CzrA
- Arsenical resistance operon repressor
- Cadmium, zinc and cobalt-transporting ATPase
- HTH-type transcriptional repressor CutR
- Copper-exporting P-type ATPase
- HTH-type transcriptional regulator MntR
Sequence:
MEKHNEHKTLNHKSSKEKDQITNRLKRIEGQVRGIQNMVENDRYCVDILVQISAVQAAMKNVALHLLEDHAHHCVADAIKSGDGEQAISELLDVFKKFTKS
Protein: procollagen-lysine 5-dioxygenase (EC 1.14.11.4) (A4U7F9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004367}; Lumenal side {ECO:0000256|ARBA:ARBA00004367}. Rough endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004427}.
Interaction partners:
- Procollagen galactosyltransferase 1
- Collagen beta
- procollagen galactosyltransferase
- Cerebral endothelial cell adhesion molecule
- Si:ch211-13f8.2.
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
- procollagen-lysine 5-dioxygenase
- Calmodulin-lysine N-methyltransferase.
- Collagen, type I, alpha 1a.
- Collagen alpha-2
Sequence:
MERRRGFHAFVLMLVTCVHCTLGMETNKDIPTEKLLVLTVATQETDGFLRFMQSANYFNFNVKVLGMGEEWKGGDVGHSIGGGQKVRLLKEAMESLDQQEDLVVLFVDSYDLIFAGGAEEILRKFQQSNHKVVFAAEGIIWPDSQLAEKYPSVRSGKRFLNSGGIIGYAPYIQKLVSQWDLHDNDDDQLFYTKIYVDPIQREKLNMTLDHKCEIFQNLNGALDEVLLKFGTERVRVRNTIYNSLPAVIHGNVNTKVYFNYLANYIPNAWNYERGCTICDQDMVDLSQLKEFPQVTVGVYIEQPTPFLPEFLERLLSLDYPKDKLNIFIHNSEVYHEKHIQKFWEENKDVFGSFKAVGPEENLTQGEARNMGMDVCRRDPSCDYFFNIDADVMLTNRQTLKLLIEQNRKIIAPLVTRHGKLWSNFWGALSLDGYYARSEDYIDIVQGKRVGVWNIPFLAHVYLIKGQTLRNELKERNVFVLEKLDPDMAMCRNARDLTVHRERESPSPESFHMLRSPKGLFMYLTNRHEFGRLISTANYNTSHYNNDLWQIFENPLDWREKYIHANYTRIFTENLLEQPCPDVFWFPVLSEKACNELVEEMENHGTWSGGKHEDKRITGGYESVPTDDIHMKQINYDQEWLHFIREFISPVTLKVFSGYYTKGYAIMNFVVKYTPDRQAYLRPHHDSSTFTINIALNNKGLDFLGGGCRFHRYNCSIESPRKGWSFMHPGRLTHLHEGLPVTNGTRYIAVSFVDP
Protein: Transmembrane protein 230 (Q68EJ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000256|ARBA:ARBA00004419}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000256|ARBA:ARBA00004234}. Early endosome {ECO:0000256|ARBA:ARBA00004412}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}. Late endosome {ECO:0000256|ARBA:ARBA00004603}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Recycling endosome {ECO:0000256|ARBA:ARBA00004172}.
Interaction partners:
- RAB39B, member RAS oncogene family a
Sequence:
MMATRNNTAGAAPNNKVKYSRLADSDEGYIDLQFKRTPPKVPYKAIALATFLFLVGSLLIIVGSLLLAGYIEVTYPDRTIPVLIIGILIFLPGFYHLRIAYYASKGYRGYSYDDIPDFDD
Protein: PDZ domain-containing protein 7a (D6BNA9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MAHSSDTARKDMTNGAHPSAQPGPSGTSTLPRYLHKKQQRQRGVRSSSPMGRVILINAPVDGGDDSEDIHTITVDKSEDGHLGFSVRGGSEHGLGIFVSKVEDDSTAEMAGLCVGDKLVEVNGISLESITMSSAVKVLTGNNRLRMVVRRVGKVPGIRYSKEKTTWVDLIHRRMVVEESGRTPSEASSDGALRRIVHLYTTSDDYCLGFNIRGGKEFGLGIYVSKLDPGGLAEQNGIKMGDQILAANGVSFEDITHSNAVEVLKSHTHVMLTIKEAGRYPAYKEMVAEYSWLNKLANGGQPSSSQGSDSYSSTSSLSSGTPVSSLSGLSQVTFPPAFGSEMVDVCISTEDRSRRPSSERIETAIQTDPQDPDTISRTSRVMSTETSRMVGETVLLKDTVIRRGTAHSRTRTFSAGDKETLDSPKTAVLMALSKPRKAIRRSQSHITVSEFWFATERASCLCGCTSRSRQEDKQKKRKHQKGKVETEGSTLQRSKTFVTLPFKSGRRRERSSSRDRKDTGREDGHKGRSKSPKHLDNEPGKERGRPIINLLSSPRETRAGLREQSPMPSPETMALLEDVARKLLNEDEVAAVMRHCKRFLVDRVVEDLVRPLLAILDKPEKLLLLREVRMIIPATDLGRFDSMVLPFELEAYDILKSRSVRSPVLRSPRHGGTPRRHLITPIPDYRGGFHLQPVQDLERERQLIEDLERMRLAGLPTGRLPPPRAFTPLLDVPVDTYITDSLRNRSLSPARSGFSHSESPYSTERTGRSPLRRDNGFPHDSLSSRGDSVPERGRSPYRNGHRMKTDKSLNGKEVKYTVMSAHRRSRTPLSQVFAPSPEQHWKEPVNGHSDSQDRTEQDYVLTTVTISKTKQSLGISISGGIESKVQPMVKIEKIFPGGAASTSDVLKAGFELVSVDGESLQGVTHQHAVDAIRRAFSNKAKEPMEFIVKVPKRLT
Protein: PDCD10 and GCKIII kinases-associated protein 1 (Q8IY42)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000269|PubMed:38517886}; Peripheral membrane protein {ECO:0000269|PubMed:38517886}.
Interaction partners:
- Programmed cell death protein 10
- Serine/threonine-protein kinase 24
- Serine/threonine-protein kinase 25
- Serine/threonine-protein kinase 26
Sequence:
MGCRCCKIIQSYLFDPVQVPSPGYVNEVNSCKLDEDDTDKLKGKWSSEVLVQKNDPQRQGSKKTESSSRTADPWEPCWPHQGPLPQGDAGGEHHACGVNGIGPAATPQPTGNSSPTQDDRGSWASTANTVPPTQPFLEGGGTRKQDCVLLASEGTQVMRNGDSRAPSEAESFALEVQDHVFQIPAPDYLQHWGPAGDNVDHNEKDCVFKNHTEDESLEGIQPPVGEHGLNTPFSVRRSWDSLNEDVETEVLSICFNEKGPVHAMPVVDSGNRQEDTHGSDGDGDGEIVDEDAAVAEALAALEAATAGEDLDETD
Protein: Centromere/kinetochore protein zw10 homolog (O43264)
Organism: Homo sapiens (Human)
Function: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex. Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15029241}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15029241}; Peripheral membrane protein {ECO:0000269|PubMed:15029241}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11590237}. Lipid droplet {ECO:0000269|PubMed:30970241}. Note=Dynamic pattern of localization during the cell cycle. In most cells at interphase, present diffusely in the cytoplasm (PubMed:15029241). In prometaphase, associated with the kinetochore. At metaphase, detected both at the kinetochores and, most prominently, at the spindle, particularly at the spindle poles. In very early anaphase, detected on segregating kinetochores. In late anaphase and telophase, accumulates at the spindle midzone (PubMed:11590237). {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15029241}.
Interaction partners:
- Syntaxin-18
- Protein zwilch homolog
- NBAS subunit of NRZ tethering complex
- Kinetochore-associated protein 1
- RAD50-interacting protein 1
- Outer kinetochore KNL1 complex subunit ZWINT
- Vesicle transport protein USE1
- Vesicle transport protein SEC20
- Zinc finger protein 787
- Vesicle-trafficking protein SEC22b
Sequence:
MASFVTEVLAHSGRLEKEDLGTRISRLTRRVEEIKGEVCNMISKKYSEFLPSMQSAQGLITQVDKLSEDIDLLKSRIESEVRRDLHVSTGEFTDLKQQLERDSVVLSLLKQLQEFSTAIEEYNCALTEKKYVTGAQRLEEAQKCLKLLKSRKCFDLKILKSLSMELTIQKQNILYHLGEEWQKLIVWKFPPSKDTSSLESYLQTELHLYTEQSHKEEKTPMPPISSVLLAFSVLGELHSKLKSFGQMLLKYILRPLASCPSLHAVIESQPNIVIIRFESIMTNLEYPSPSEVFTKIRLVLEVLQKQLLDLPLDTDLENEKTSTVPLAEMLGDMIWEDLSECLIKNCLVYSIPTNSSKLQQYEEIIQSTEEFENALKEMRFLKGDTTDLLKYARNINSHFANKKCQDVIVAARNLMTSEIHNTVKIIPDSKINVPELPTPDEDNKLEVQKVSNTQYHEVMNLEPENTLDQHSFSLPTCRISESVKKLMELAYQTLLEATTSSDQCAVQLFYSVRNIFHLFHDVVPTYHKENLQKLPQLAAIHHNNCMYIAHHLLTLGHQFRLRLAPILCDGTATFVDLVPGFRRLGTECFLAQMRAQKGELLERLSSARNFSNMDDEENYSAASKAVRQVLHQLKRLGIVWQDVLPVNIYCKAMGTLLNTAISEVIGKITALEDISTEDGDRLYSLCKTVMDEGPQVFAPLSEESKNKKYQEEVPVYVPKWMPFKELMMMLQASLQEIGDRWADGKGPLAAAFSSSEVKALIRALFQNTERRAAALAKIK
Protein: PBAN-type neuropeptides (Neo-PBAN) (Pheromone/pyrokinin biosynthesis-activating neuropeptide) [Cleaved into: Diapause hormone (DH) (DH-PBAN); Alpha-SG neuropeptide (Alpha-SGNP); Beta-SG neuropeptide (Beta-SGNP); Pheromone biosynthesis-activating neuropeptide I (Bom-PBAN-I) (PBAN-I) (Melanization and reddish coloration hormone I) (MRCH-I); Pheromone biosynthesis-activating neuropeptide II (PBAN-II); Gamma-SG neuropeptide (Gamma-SGNP)] (P09971)
Organism: Bombyx mori (Silk moth)
Function: A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity). Identical to MRCH which is implicated in the formation of both melanin in the cuticle and ommochrome in the epidermis of armyworm species.
Subcellular location: Secreted {ECO:0000269|PubMed:8475067}.
Interaction partners:
Sequence:
MYKTNIVFNVLALALFSIFFASCTDMKDESDRGAHSERGALWFGPRLGKRSMKPSTEDNRQTFLRLLEAADALKFYYDQLPYERQADEPETKVTKKIIFTPKLGRSVAKPQTHESLEFIPRLGRRLSEDMPATPADQEMYQPDPEEMESRTRYFSPRLGRTMSFSPRLGRELSYDYPTKYRVARSVNKTMDN
Protein: CXXC-type zinc finger protein 1 (CpG-binding protein) (PHD finger and CXXC domain-containing protein 1) (Q9P0U4)
Organism: Homo sapiens (Human)
Function: Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:12200428, ECO:0000269|PubMed:17355966}. Nucleus {ECO:0000250|UniProtKB:Q9CWW7}. Note=Associated with euchromatin. During mitosis, excluded from condensed chromosomes.
Interaction partners:
- Histone-lysine N-methyltransferase SETD1B
- WD repeat-containing protein 5
- Histone-lysine N-methyltransferase SETD1A
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Retinoblastoma-binding protein 5
- Protein dpy-30 homolog
- WD repeat-containing protein 82
- Host cell factor 1
- Histone-lysine N-methyltransferase PRDM9
- Biorientation of chromosomes in cell division protein 1-like 1
Sequence:
MEGDGSDPEPPDAGEDSKSENGENAPIYCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCRECREKDPKLEIRYRHKKSRERDGNERDSSEPRDEGGGRKRPVPDPDLQRRAGSGTGVGAMLARGSASPHKSSPQPLVATPSQHHQQQQQQIKRSARMCGECEACRRTEDCGHCDFCRDMKKFGGPNKIRQKCRLRQCQLRARESYKYFPSSLSPVTPSESLPRPRRPLPTQQQPQPSQKLGRIREDEGAVASSTVKEPPEATATPEPLSDEDLPLDPDLYQDFCAGAFDDHGLPWMSDTEESPFLDPALRKRAVKVKHVKRREKKSEKKKEERYKRHRQKQKHKDKWKHPERADAKDPASLPQCLGPGCVRPAQPSSKYCSDDCGMKLAANRIYEILPQRIQQWQQSPCIAEEHGKKLLERIRREQQSARTRLQEMERRFHELEAIILRAKQQAVREDEESNEGDSDDTDLQIFCVSCGHPINPRVALRHMERCYAKYESQTSFGSMYPTRIEGATRLFCDVYNPQSKTYCKRLQVLCPEHSRDPKVPADEVCGCPLVRDVFELTGDFCRLPKRQCNRHYCWEKLRRAEVDLERVRVWYKLDELFEQERNVRTAMTNRAGLLALMLHQTIQHDPLTTDLRSSADR
Protein: Uncharacterized protein (Q386N5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- BTB domain-containing protein
- Uncharacterized protein
- 3-hydroxyacyl-CoA dehydrogenase C-terminal domain-containing protein
Sequence:
MFPFDERSPSASRPATEVTSFYSSRDGSHTTNDSTDCSTVTSARGGSRLVAELRLELEMRDERIKELEGAYDELLRKSNFDQGQLQCDLQKTRDELASTLETLNALQKGTGKEGEGNLTQETGDHSVYKKNIASAGDNDPRSADYNPVTGKVAEEQLARLVNEFTDEKESLLAALKAAEDEREELRKVAEDDKKIITASECEKEKLVAALKAAEDEREELRKVAEDDKKIITASECEKEKLVAALKAAEDEREELRKVAEDDKKIITASECEKEKLVAALKAAEDEREELRKVAEDDKKIITASECEKEKLVAALKAAEDEREELRKVAEDDKKIITASECEKEKLVAALKAAEDEREELRKVAEDDKKIITASECEKEKLLAALKAAEDENVTLSTSLKETVESLEEIRRQNIWALKERDEALNSLKTERRRMHESSPSADPGDTEAPLLEPGKATNRRFRLYGMCPRCTVM