wanglab/gogpt-training-data huggingface dataset:
Protein: Coatomer subunit zeta (Q8IQP2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU366053}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|RuleBase:RU366053}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|RuleBase:RU366053}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|RuleBase:RU366053}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000256|RuleBase:RU366053}; Peripheral membrane protein {ECO:0000256|RuleBase:RU366053}; Cytoplasmic side {ECO:0000256|RuleBase:RU366053}.
Interaction partners:
Sequence:
MCIMDNDGNRILAKYYDKNILSTLKEQKAFEKNLFNKTHRSNTEIIMLDGLTCVYKSNVDLFFYVMGNAYENELILLSVLNCLYDSISLILKKNVEKRLVLENLEIIMLAFDEICDGGIILDADPSSVVKRVDLRNDDIPIAEQTVAQVLQSAREQLKWSILK
Protein: Kelch-like protein 20 (Q9BS75)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVSCTWCSNAPICWRAIWVHILLNNTCLGISC
Protein: Transmembrane protein 120A (Protein TACAN) (Transmembrane protein induced by tumor necrosis factor alpha) (Q9BXJ8)
Organism: Homo sapiens (Human)
Function: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli (By similarity). May also be required for efficient adipogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:35013224}; Multi-pass membrane protein {ECO:0000269|PubMed:34374645}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000269|PubMed:34374645}. Endoplasmic reticulum {ECO:0000269|PubMed:35013224}.
Interaction partners:
Sequence:
MQPPPPGPLGDCLRDWEDLQQDFQNIQETHRLYRLKLEELTKLQNNCTSSITRQKKRLQELALALKKCKPSLPAEAEGAAQELENQMKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILILISFTCRFLLNSRVTDAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYYQSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLAQDPQCKEWQVLMCGFPFLLLFLGNFFTTLRVVHHKFHSQRHGSKKD
Protein: Envelope glycoprotein B (gB) (P12640)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Function: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04032}.
Interaction partners:
Sequence:
MAARGGAERAAGAGDGRRGQRRHLRPGRVLAALRGPAAPGAGGARAALAAALLWATWALLLAAPAAGRPATTPPAPPPEEAASPAPPASPSPPGPDGDDAASPDNSTDVRAALRLAQAAGENSRFFVCPPPSGATVVRLAPARPCPEYGLGRNYTEGIGVIYKENIAPYTFKAYIYKNVIVTTTWAGSTYAAITNQYTDRVPVGMGEITDLVDKKWRCLSKAEYLRSGRKVVAFDRDDDPWEAPLKPARLSAPGVRGWHTTDDVYTALGSAGLYRTGTSVNCIVEEVEARSVYPYDSFALSTGDIIYMSPFYGLREGAHREHTSYSPERFQQIEGYYKRDMATGRRLKEPVSRNFLRTQHVTVAWDWVPKRKNVCSLAKWREADEMLRDESRGNFRFTARSLSATFVSDSHTFALQNVPLSDCVIEEAEAAVERVYRERYNGTHVLSGSLETYLARGGFVVAFRPMLSNELAKLYLQELARSNGTLEGLFAAAAPKPGPRRARRAAPSAPGGPGAANGPAGDGDAGGRVTTVSSAEFAALQFTYDHIQDHVNTMFSRLATSWCLLQNKERALWAEAAKLNPSAAASAALDRRAAARMLGDAMAVTYCHELGEGRVFIENSMRAPGGVCYSRPPVSFAFGNESEPVEGQLGEDNELLPGRELVEPCTANHKRYFRFGADYVYYENYAYVRRVPLAELEVISTFVDLNLTVLEDREFLPLEVYTRAELADTGLLDYSEIQRRNQLHELRFYDIDRVVKTDGNMAIMRGLANFFQGLGAVGQAVGTVVLGAAGAALSTVSGIASFIANPFGALATGLLVLAGLVAAFLAYRYISRLRSNPMKALYPITTRALKDDARGATAPGEEEEEFDAAKLEQAREMIKYMSLVSAVERQEHKAKKSNKGGPLLATRLTQLALRRRAPPEYQQLPMADVGGA
Protein: Uncharacterized protein (F4K6Z1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein NPGR1
- Protein NPGR2
- Hyccin
- At5g64090
- Protein NPG1
- Phosphatidylinositol 4-kinase alpha 1
- Phosphatidylinositol 4-kinase alpha 2
Sequence:
MGVVSRTVFPVCESLCCFCPALRARSRHPVKRYKHLLADIFPRSQDEQPNDRKIGKLCEYAAKNPLRIPKITTSLEQRCYKELRMEQFHSVKIVMSIYKKLLVSCNEQMLLFASSYLGLIHILLDQTRYDEMRILGCEALYDFVTSQAEGTYMFNLDGLIPKICPLAHELGEEDSTTNLCAAGLQALSSLVWFMGEFSHISVEFDNVVSVVLENYGGHSQSSTSAVNQDNKVASIDKELSPAEAETRIASWTRIVDDRGKAIVSVEDAKNPKFWSRVCLHNLAKLAKEATTVRRVLESLFRYFDFNEVWSTENGLAVYVLQDVQLLIERSGQNTHFLLSILIKHLDHKNVLKKPRMQLEIVYVATALAQQTKVLPSVAIIGALSDMIRHLRKSIHCSLDDSNLGNEMIQYNLKFEAVVEQCLLQLSQKVGDAGPILDIMAVMLESMSNITVMARTLIAAVFRTAQIIAAIPNLSYENKAFPDALFHQLLQAMVCADHESRMGAHRIFSVVLVPSSVSPSSVLNSRRPADMQRTLSRTVSVFSSSAALFRKLKLESDNSVDDTAKMERVSTLSRSTSKFIRGESFDDEEPKNNTSSVLSRLKSSYSRSQSVKRNPSSMVADQNSSGSSPEKPVIPLRLSSHQICLLLSSIWVQSLSPHNMPQNYEAIANTFSLVLLFGRTKHSSNEVLVWSFQLAFSLRNLSLGGPLQPSRRRSLFTLATSMIIFSAKAFNIPPLVNSAKTSLQEKTVDPFLQLVEDCKLDAVFYGQADQPAKNYGSKEDDDDASRSLVTIEEASQNQSREHYASMIMKFLGKLSDQESSAIKEQLVSDFIPIDGCPVGTQLTESPVQVYRSEEKNNKPRENAETQLLIPENDAVPSPPEEQFSLDIQPNAKTAFLLSIDELLNAVSQTTAQLGRYSVSDPPDMTYTEMAGHCEALLMGKQEKMSFMSAKSNKFSSSQTKEAVALPCSGGNPFVDQRSSWEMMGLGAPAASNICVTEYQNQPPFFNPPSSTPFDNFLTAKPLVPLD
Protein: Protein POLLENLESS 3 (Protein MALE STERILE 5) (Protein THREE-DIVISION MUTANT 1) (Q9SUC3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential for male fertility, especially for microspore and pollen grain production. Involved in the regulation of cell division after male meiosis I and II to facilitate exit from meiosis and transition to G1.
Subcellular location: Nucleus {ECO:0000303|PubMed:9750346}.
Interaction partners:
- Nonsense-mediated mRNA decay factor SMG7
- Cell division cycle 20.1, cofactor of APC complex
- Protein GIGAS CELL1
- Cyclin-A1-2
- Seed dormancy control protein
- Meiosis-specific protein ASY1
- Myosin heavy chain-related protein
- Cyclin-SDS
- Protein PATRONUS 1
- Putative F-box protein At1g26510
Sequence:
MCPCVERRAPPGVYYTPPPARTSDHVAAMPMTERRRPPYSCSSSSERRDPFHIVHKVPSGDSPYVRAKHAQLIDKDPNRAISLFWTAINAGDRVDSALKDMAVVMKQLGRSDEGIEAIKSFRYLCSFESQDSIDNLLLELYKKSGRIEEEAVLLEHKLQTLEQGMGFGGRVSRAKRVQGKHVIMTIEQEKARILGNLGWVHLQLHNYGIAEQHYRRALGLERDKNKLCNLAICLMRMSRIPEAKSLLDDVRDSPAESECGDEPFAKSYDRAVEMLAEIESKKPEADLSEKFYAGCSFVNRMKENIAPGTANKNYSDVSSSPASVRPNSAGLYTQPRRCRLFEEETRGAARKLLFGKPQPFGSEQMKILERGEEEPMKRKKLDQNMIQYLHEFVKDTADGPKSESKKSWADIAEEEEAEEEEEERLQGELKTAEM
Protein: Ras-related protein Rab-11B (EC 3.6.5.2) (GTP-binding protein YPT3) (Q15907)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The small Rab GTPase RAB11B plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis.
Subcellular location: Recycling endosome membrane {ECO:0000250|UniProtKB:P46638}; Lipid-anchor {ECO:0000250|UniProtKB:P46638}; Cytoplasmic side {ECO:0000250|UniProtKB:P46638}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:O35509}; Lipid-anchor {ECO:0000250|UniProtKB:O35509}; Cytoplasmic side {ECO:0000250|UniProtKB:O35509}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305|PubMed:21255211}; Lipid-anchor {ECO:0000305|PubMed:21255211}; Cytoplasmic side {ECO:0000305|PubMed:21255211}. Cytoplasmic vesicle {ECO:0000269|PubMed:26032412}. Note=Recruited to phagosomes containing S.aureus. Colocalizes with RAB11AFIP1 on punctate vesicles (PubMed:26032412). {ECO:0000269|PubMed:26032412, ECO:0000305|PubMed:21255211}.
Interaction partners:
- Rab11 family-interacting protein 1
- Rab11 family-interacting protein 2
- Ras-related protein Rab-11A
- Rab11 family-interacting protein 5
- Rab GDP dissociation inhibitor alpha
- Phosphatidylinositol 4-kinase beta
- Ras-related protein Rab-1B
- cGMP-dependent protein kinase 2
- TBC1 domain family member 1
- Rab GDP dissociation inhibitor beta
Sequence:
MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNNLSFIETSALDSTNVEEAFKNILTEIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQKPNKLQCCQNL
Protein: N-substituted formamide deformylase (EC 3.5.1.91) (Q68AP4)
Organism: Arthrobacter pascens
Function: Hydrolyzes N-substituted formamides, but not amides. N-benzylformamide is the preferred substrate, while N-butylformamide is hydrolyzed at a much lower rate. Has very low activity towards allylformamide, N-(2-cyclohex-1-enylethyl)formamide and N-(alpha-methylbenzyl)formamide.
Interaction partners:
Sequence:
MTQMRDLMIINANVRTVDARNSCAQAVLVSGGRIAIVGTETEVRGAAAPDAEVLDVSGKTVVPGFIDAHNHLSVAAFAPDSVDCSTPPLATLDEVLEVIERHCRNIPPGQWVRGINFHASHIREQRNPTRYELDEVAPNNPFFLIDASCHAGFANSAALDLVGIGAHTPEPWGGEIERDLSGKPTGTLLEAAANLLHSASWNDYAERDWDRAVELLHSKMNDYLAVGLTGVGDAMVTAKSAELYRRADAAGKMPFTLQQLHGGDHFFSMQDLGRSDTVDRIMEPESYLLRGGAMKIFVDRAYPSPAIDQIHDGCKTHVGANFYSKSEVHDLAVRASKLGINLAIHGMGNCAIDIVLDAYEAVRRQSNADTVLRLEHAFIAETGQGQRMADLGIDLVANPGLAFGWGEVFNMWRGENQEHLKLFPVRSMLDAGVRVSLASDHPCGTYSPAEIMWTAVARETMAGAPLEPDEAVTADEALRMYTINPAHASGRGSEEGSIEAGKRANLLVLDRDPVDCATGELRELQVLRTYVDGVLRYERTGS
Protein: Gb|AAD14519.1 (Octicosapeptide/Phox/Bem1p family protein) (Q9LXC6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDKFSYNSYPDSAESSPRSRDVEFENPSPWEDQQQQNYKVKLMCSYGGKIQPRPHDNQLTYVNGDTKIMSVDRGIRFPALVSKLSAVCSGGGDGGEISFKYQLPGEDLDALISVTNDEDLEHMMHEYDRLLRLSTKPARMRLFLFPSSPISGGFGSEGSTKSDRDTLNPIPSRPESEKSVTAPPNNADFLFGSEKVAPIPPSPVKVPQPVPEPVVLEPPQMFVDQRMLQPEHGVNPAEIQRQIQEFQMIQIRDQEQQMLHQNQLHQQQQQQEAIHQNQLHHQQEVIHQNQLLQQEAIHQNQMLQQQQQQEAMYRRKTEDEAGRYFPPTYTQNPAPVTNQQPPVGYWQGNTNNSNIQGNIYTTTSQNLPEQQQQQQQVYMIPAQSQAPGTLYQSVMRPTVQGNQGYYPSPVQRLHHPDAYMEQQNQPGYNVVQPQPTFSGGPQVMTSVGPQVMTSVGPPMGLQEPYSQMGKPVYYTVAGEGMMVQPPPAQPQQQQQQYQGMGQPVSGMTDLRTGPDGKVAVNMAAPQVSDSV
Protein: HTH-type transcriptional regulator CmtR (P9WMI9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Metal-responsive transcriptional repressor for the cmt operon. Binding of cadmium or lead causes the repressor to dissociate from the DNA.
Interaction partners:
- Uncharacterized protein Rv1993c
- Probable cation-transporting ATPase G
- HTH-type transcriptional repressor SmtB
- Uncharacterized protein Rv1995
Sequence:
MLTCEMRESALARLGRALADPTRCRILVALLDGVCYPGQLAAHLGLTRSNVSNHLSCLRGCGLVVATYEGRQVRYALADSHLARALGELVQVVLAVDTDQPCVAERAASGEAVEMTGS
Protein: Rifin (C0H4Q7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLLYSNILLFALALNILLTSYYAHNKNKPSITSHHTPRYTSRVLSECDTESSIYDNDEEINSVKEIFERQASQRLREYDERLQEKRQKRKEQRDKNIQKIIHKDKMEKNLAEKIEKGCLMCGCGLGSVAGSIGLFGAVAINIWKPAALDAAIAKAITEGTANISAAGVKAGEATGKVLVISGLKRIGISTLDNQILESYFATTSYKKVASIAQAVYEQHFEKCEFGYLKDGFIPVGDRSRDIHFCQSMWNQTSAVSQPRQYISTEEVIKRTVQNMVSDAEGPANTAAEIAEAIETAKIKAAEEKTIEAASTQLYGAIGYSILAILIIVLIMLIIYLILRYRRKKKMKKKAQYTKLLNE
Protein: Monopolar spindle protein 2 (P53159)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:10397772}; Single-pass membrane protein {ECO:0000269|PubMed:10397772}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10397772}.
Interaction partners:
- Spindle pole component BBP1
- Spindle pole body assembly component MPS3
- NAP1-binding protein
- Chromosome segregation in meiosis protein 4
- Spindle pole body component SPC42
- Spindle pole body component 110
- Kinetochore protein SPC24
- Protein SFI1
- Myosin-2
- Spindle pole component 29
Sequence:
MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHKEEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKNKNTEGAGISTPRKKLTESPIKLLSRNNIGKALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQKAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALLAGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
Protein: Zinc finger and SCAN domain containing 26 (Zinc finger protein 187, isoform CRA_b) (A0A087X2F1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATALDPDQPKKQKILVEEMAPLKGVQEQQVRHECEVTKPEKEKGEETRIENGKLIVVTDSCGRVESSGKISEPMEAHNEGSNLERHQAKPKEKIEYKCSEREQRFIQHLDLIEHASTHTGKKLCESDVCQSSSLTGHKKVLSREKGHQCHECGKAFQRSSHLVRHQKIHLGEKPYQCNECGKVFSQNAGLLEHLRIHTGEKPYLCIHCGKNFRRSSHLNRHQRIHSQEEPCECKECGKTFSQALLLTHHQRIHSHSKSHQCNECGKAFSLTSDLIRHHRIHTGEKPFKCNICQKAFRLNSHLAQHVRIHNEEKPYQCSECGEAFRQRSGLFQHQRYHHKDKLA
Protein: Vacuolar protein sorting-associated protein 51 homolog (Protein fat-free homolog) (Q3UVL4)
Organism: Mus musculus (Mouse)
Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome-derived carriers to the TGN. Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9UID3}. Recycling endosome {ECO:0000250|UniProtKB:Q9UID3}. Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex. {ECO:0000250|UniProtKB:Q9UID3}.
Interaction partners:
- Vacuolar protein sorting-associated protein 54
- Vacuolar protein sorting-associated protein 53 homolog
- Vacuolar protein sorting-associated protein 52 homolog
- Syndetin
- EARP and GARP complex-interacting protein 1
- Syntaxin-6
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 5
- Syntaxin-16
- Conserved oligomeric Golgi complex subunit 4
Sequence:
MAAAAAVGPGLGSGPGDSPEGPEADAPERRRKAHGMLKLYYGLSEGEVAGHPAGPDPLDPTDLNGAHFDPEVYLDKLRRECPLAQLMDSETDMVRQIRALDSDMQTLVYENYNKFISATDTIRKMKNDFRKMEDEMDRLATNMAVITNFSARISATLQDRHERITKLAGVHALLRKLQFLFELPSRLTKCVELGAYGQAVRYQGRARAVLQQYQHLPSFRAIQDDCQVITARLAQQLRQRFREGCSGAPEQAECVELLLALGEPAEELCEEFLAHARGRLEEELSSLEAELGPSPPAPDVLEFTDRGGNGFVGGLCQVAAAYQELFAAQGPAGAEKLAAFAQELGGRYFALVERRLAQEQGGSDNSLLVRALDRFHRRLRAPGALLAAAGLSESATEIVERVARERLSHHLQGLKAAFLSSLTDVRQALAAPRLAGKEGPSLAELLANVASSILSHIKTSLASVHLFTAKEVSFSNKPYFRGEFCSQGVREGLIVGFIRSMCQTAQSFCDSPGEKGGATPPALLLLLSRLCLDYETATISYILTLTDEQFLVQDQSPVTPVSTLCAEARETARRLLTHYVKVQGLVISQMLRKSVETRDWLSTLEPRNVRAVMKRVVEDTTAIDVQVGLLYEEGVRKAQSSDSSKRTFSVYSSSRQQGRYAPSYTPSAPMDTNLLSNIQKLFSERIDVFSPVEFNKVSVLTGIIKISLKTLLECVRLRTFGRFGLQQVQVDCHFLQLYLWRFVADEELVHLLLDEVVASAALRCPDPVPMEPSVVEVICERG
Protein: Ras-related protein Rap-1b (EC 3.6.5.2) (GTP-binding protein smg p21B) (P61223)
Organism: Bos taurus (Bovine)
Function: GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P61224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61224}. Cell junction {ECO:0000250|UniProtKB:P61224}. Note=May shuttle between plasma membrane and cytosol (By similarity). Presence of KRIT1 and CDH5 is required for its localization to the cell junction (By similarity). {ECO:0000250|UniProtKB:P61224}.
Interaction partners:
- Rap guanine nucleotide exchange factor 2
- RAS guanyl-releasing protein 2
- Ral guanine nucleotide dissociation stimulator
- RAP1 GTPase activating protein
- Krev interaction trapped protein 1
- non-specific serine/threonine protein kinase
- Transforming protein RhoA
- RAS guanyl releasing protein 3
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- RAF proto-oncogene serine/threonine-protein kinase
Sequence:
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL
Protein: X-ray repair cross complementing 1 (M0R1U8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XVTPQTSQRGSLAAPLGYFQVLFKLEKEEQIHSVDIGNDGSAFVEVLVGSSAGGAGEQDYEVLLVTSSFMSPSESRSGSNPNRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYSKDSPFGLSFVRFHSPPDKDEAEAPSQKVTVTKLGQFRVKEEDESANSLRPGALFFSRINKTSPVTASDPAGPSYAAATLQASSAASSASPVSRAIGS
Protein: ARF guanine-nucleotide exchange factor GNL1 (Protein ENDOPLASMIC RETICULUM MORPHOLOGY 1) (Protein GNOM-like 1) (Q9FLY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activates the ARF proteins by exchanging bound GDP for free GTP. Plays a role in vesicular protein sorting. Acts as the major regulator of retrograde Golgi to endoplasmic reticulum trafficking but is also involved in the endocytosis process. Could function redundantly with GNOM. Regulates vesicle trafficking required for the coordinated polar localization of auxin efflux carriers which in turn determines the direction of auxin flow. Mediates the endocytosis of PIN2 from plasma membrane to endosomal compartments. Required for maintenance of endoplasmic reticulum morphology.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17653190}. Golgi apparatus membrane {ECO:0000269|PubMed:17653190}; Peripheral membrane protein {ECO:0000269|PubMed:17653190}; Cytoplasmic side {ECO:0000269|PubMed:17653190}. Note=Soluble and partially membrane-bound.
Interaction partners:
- Coatomer subunit gamma
- ADP-ribosylation factor 1
- ADP-ribosylation factor 2-B
- Probable ADP-ribosylation factor At2g15310
- Protein transport protein SEC24 A
- ADP-ribosylation factor
- ADP-ribosylation factor
- Ras-related protein RABA1b
- V-type proton ATPase subunit a1
- Structural molecule
Sequence:
MGYQNHPSGSNSFHGEFKRCHSKPSKGAVASMINSEIGAVLAVMRRNVRWGVRYIADDDQLEHSLIHSLKELRKQIFSWQSNWQYVDPRLYIQPFLDVILSDETGAPITGVALSSVYKILTLEVFTLETVNVGEAMHIIVDAVKSCRFEVTDPASEEVVLMKILQVLLACVKSKASNGLSNQDICTIVNTCLRVVHQSSSKSELLQRIARHTMHELIRCIFSQLPFISPLANECELHVDNKVGTVDWDPNSGEKRVENGNIASISDTLGTDKDDPSSEMVIPETDLRNDEKKTEVSDDLNAAANGENAMMAPYGIPCMVEIFHFLCTLLNVGENGEVNSRSNPIAFDEDVPLFALGLINSAIELGGPSFREHPKLLTLIQDDLFCNLMQFGMSMSPLILSTVCSIVLNLYLNLRTELKVQLEAFFSYVLLRIAQSKHGSSYQQQEVAMEALVDLCRQHTFIAEVFANFDCDITCSNVFEDVSNLLSKNAFPVNGPLSAMHILALDGLISMVQGMAERVGEELPASDVPTHEERYEEFWTVRCENYGDPNFWVPFVRKVKHIKKKLMLGADRFNRDPNKGLQYLQGVHLLPEKLDPKSVACFFRYTCGLDKNVMGDFLGNHDQFCIQVLHEFAKTFDFQNMNLATALRLFVGTFKLSGEAQKIHRVLEAFSERYYEQSPHILIDKDAAFVLAYSIILLNTDQHNAQVKTRMTEEDFIRNNRTINGGADLPREYLSEIYHSIRHSEIQMDEDKGTGFQLMTASRWISVIYKSKETSPYIQCDAASHLDRDMFYIVSGPTIAATSVVFEQAEQEDVLRRCIDGLLAIAKLSAYYHLNSVLDDLVVSLCKFTPFFAPLSADEAVLVLGEDARARMATEAVFLIANKYGDYISAGWKNILECVLSLNKLHILPDHIASDAADDPELSTSNLEQEKPSANPVPVVSQSQPSAMPRKSSSFIGRFLLSFDSEETKPLPSEEELAAYKHARGIVKDCHIDSIFSDSKFLQAESLQQLVNSLIRASGKDEASSVFCLELLIAVTLNNRDRILLIWPTVYEHILGIVQLTLTPCTLVEKAVFGVLKICQRLLPYKENLTDELLKSLQLVLKLKAKVADAYCERIAQEVVRLVKANASHVRSRTGWRTIISLLSITARHPEASEAGFEALRFIMSEGAHLLPSNYELCLDAASHFAESRVGEVDRSISAIDLMSNSVFCLARWSQEAKNSIGETDAMMKLSEDIGKMWLKLVKNLKKVCLDQRDEVRNHAISMLQRAIAGADGIMLPQPLWFQCFDSAVFILLDDVLTFSIENSRKTLKKTVEETLVLATKLMSKAFLQSLQDISQQPSFCRLWVGVLNRLETYMSTEFRGKRSEKVNELIPELLKNTLLVMKATGVLLPGDDIGSDSFWQLTWLHVNKISPSLQSEVFPQEELDQFQRRNAKPEDPPVPGNEV
Protein: Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Neural apoptosis-regulated convertase 1) (NARC-1) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9) (Q8NBP7)
Organism: Homo sapiens (Human)
Function: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways.
Subcellular location: Cytoplasm. Secreted. Endosome. Lysosome. Cell surface. Endoplasmic reticulum. Golgi apparatus. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation.
Interaction partners:
- Low-density lipoprotein receptor
- Apolipoprotein B-100
- Very low-density lipoprotein receptor
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Immunoglobulin lambda-like polypeptide 5
- Immunoglobulin kappa variable 1-33
- Probable non-functional immunoglobulin heavy variable 3-16
- Golgi phosphoprotein 3
- Proprotein convertase subtilisin/kexin type 5
- Sortilin
Sequence:
MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEGAVTAVAICCRSRHLAQASQELQ