wanglab/gogpt-training-data huggingface dataset:
Protein: Dickkopf-related protein 1 (Dickkopf-1) (Dkk-1) (mDkk-1) (O54908)
Organism: Mus musculus (Mouse)
Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity. Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning.
Subcellular location: Secreted.
Interaction partners:
- Low-density lipoprotein receptor-related protein 5
- Kremen protein 1
- Low-density lipoprotein receptor-related protein 6
- Kremen protein 2
- Cytoskeleton-associated protein 4
- Proto-oncogene Wnt-1
- Protein Wnt-3a
- Protein Wnt-5a
- Dickkopf-related protein 2
- Dickkopf-related protein 4
Sequence:
MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH
Protein: Striatin, calmodulin binding protein 3 (cDNA FLJ77970, highly similar to Homo sapiens nuclear autoantigen GS2NA mRNA) (A0AV58)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDELAGGGGGGPGMAAPPRQQQGPGGNLGLSPGGNGAAGGGGPPASEGAGPAAGPELSRPQQYTIPGILHYIQHEWARFEMERAHWEVERAELQARIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDLKMPTFESEETKDTEAPTAPQNSQLTWKQGRQLLRQYLQEVGYTDTILDVRSQRVRSLLGLSNSEPNGSVETKNLEQILNGGESPKQKGQEIKRSSGDVLETFNFLENADDSDEDEENDMIEGIPEGKDKHRMNKHKIGNEGLAADLTDDPDTEEALKEFDFLVTAEDGEGAGEARSSGDGTEWAEPITFPSGGGKSFIMGSDDVLLSVLGLGDLADLTVTNDADYSYDLPANKDAFRKTWSPKYTLRSHFDGVRALAFHPVEPVLVTASEDHTLKLWNLQKTVPAKKSASLDVEPIYTFRAHIGPVLSLAISSNGEQCFSGGIDATIQWWNMPSPSVDPYDTYEPNVLAGTLVGHTDAVWGLAYSGIKNQLLSCSADGTVRLWNPQEKLPCICTYNGDKKHGIPTSVDFIGCDPAHMVTSFNTGSAVIYDLETSQSLVILSSQVDSGLQSNNHINRVVSHPTLPVTITAHEDRHIKFFDNKTGKMIHSMVAHLDAVTSLAVDPNGIYLMSGSHDCSIRLWNLDSKTCVQEITAHRKKLDESIYDVAFHSSKAYIASAGADALAKVFV
Protein: Polyamine transporter 2 (P53283)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Recognizes spermine, but not spermidine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12562762, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:12562762, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Polyamine transporter 3
- Quinidine resistance protein 2
- Transcriptional activator HAA1
- Putative vacuolar protein sorting-associated protein TDA6
- ATP-dependent permease PDR12
- Protein YRO2
- Serine/threonine-protein kinase HRK1
- Azole resistance protein 1
- ABC transporter ATP-binding protein/permease PDR18
- Protein YGP1
Sequence:
MSDQESVVSFNSQNTSMVDVEGQQPQQYVPSKTNSRANQLKLTKTETVKSLQDLGVTSAAPVPDINAPQTAKNNIFPEEYTMETPSGLVPVATLQSMGRTASALSRTRTKQLNRTATNSSSTGKEEMEEEETEEREDQSGENELDPEIEFVTFVTGDPENPHNWPSWVRWSYTVLLSILVICVAYGSACISGGLGTVEKKYHVGMEAAILSCSLMVIGFSLGPLIWSPVSDLYGRRVAYFVSMGLYVIFNIPCALAPNLGCLLACRFLCGVWSSSGLCLVGGSIADMFPSETRGKAIAFFAFAPYVGPVVGPLVNGFISVSTGRMDLIFWVNMAFAGVMWIISSAIPETYAPVILKRKAARLRKETGNPKIMTEQEAQGVSMSEMMRACLLRPLYFAVTEPVLVATCFYVCLIYSLLYAFFFAFPVIFGELYGYKDNLVGLMFIPIVIGALWALATTFYCENKYLQIVKQRKPTPEDRLLGAKIGAPFAAIALWILGATAYKHIIWVGPASAGLAFGFGMVLIYYSLNNYIIDCYVQYASSALATKVFLRSAGGAAFPLFTIQMYHKLNLHWGSWLLAFISTAMIALPFAFSYWGKGLRHKLSKKDYSIDSVEM
Protein: Uncharacterized protein AT4g25670 (Uncharacterized protein L73G19.50) (Q9SZZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGESKGCGNVGRMISKNKSANSYNLSLQLSPVVSFWDCIVRTMRYSYIPEWLEIYSQAIMDHTVCKQVQPVVRKAKKKHGKDEFDRIKQAEKKKRRLEKALATSAAIRAELEKKKQKRLEEQQRLDEEGAAIAEAVALHVLLGEDSDDSSRVKFGEEKGFTMDLFRDERTNYVPRQSCASYAVQGIGFVSNGYGLGDSNWSPFTRRGAWDNNMGISADLIAAQAVSALQISENADGNAFVFNGMFRG
Protein: Alpha-2,8-sialyltransferase 8B (N-glycan alpha 2,8-sialyltransferase) (Q8QH83)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
Sequence:
MSFEFRILMFGIGTALVIFVIIADISEVEEEIANIEDSRKFHLKSVALQSNRSSDLNAAPTSLVTYRKSKVSSLASPSDIKRKTSNSSSSEWTFNRTLSNLIRKNILKFLDAERDISILKSTFKPGDVIHYIFDRQSTTNISENLYHLLPTVSPMKNQHYRKCAIVGNSGILLNSSCGREIDSHDFVIRCNLAPVEEYAADVGLRTSLVTMNPSVVQRAFQDLNSEEWVQRFVQRPQSLSGSVLWIPAFMAKGGEERVEWAIRLILLHTVNVRTAFPSLRLLHAVRGYWLTNHVQIKRPTTGLLMYTMATRFCDEIHLYGFWPFAHDPDGKPVKYHYYDTLTYHYTSSASPHTMPLEFRTLSALHRQGALRLHTGPCKPPT
Protein: RE03226p (Q8SZE4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSAPIRYYYDLMSQPSRALFIIFRLSKMPFEDCVVALRNGEHLTEDFKKEINRFQRVPCIHDNGYKLAESVAILRYLSAKGKIPEHLYPKYFVDQSRVDEFLEWQHMSLRLTCAMYFRTVWLEPLLTGRTPSEAKIETFRMQMERNLDVVEEVWLEGKDFLTGSSLTVADIFAACEIEQTRMADYDVRIKYPKIRAWLKRVRQSCNPYYDVAHEFVYKISGTGPQAKL
Protein: Rga2p (Q5AMQ3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- GTP-binding protein RHO1
- Rho family GTPase
- Rho family GTPase
- Rho family GTPase
- GTP-binding protein RHO3
- Cell division control protein 42 homolog
- Rho family guanine nucleotide exchange factor
- Serine/threonine-protein kinase CST20
- Serine/threonine-protein kinase CLA4
- Fav1p
Sequence:
MPELVPPTNNRPHIHETPELSSQPSLDSNRQPRELCKKCNQLIVEGHAYELGDDRWHIHCFNCSKCNTSLGCNSNFLVLGNGNLICSNCSYNCKQCGRKIDDLAILTGDQAYCSNCFKCRSCKNKIEDLRYARTSKGLFCMDCHQKLMAKKKKYDAKKKHLALLQEKRVQLEREKDQRELQILEDHKRSVNSSRNSLIQSYMNNQNNQSGESLLYQQNNRSVTSVTSSKNKSLPLPPTSTSPARPTPYSANSYQSKESISGKNKTDTSLGSLSTSQTFSEHTNKGGSTMHSSTGLHNPPIFQSDNDFSIEEVQNSSDSDSNGDEKKSNSTSLRNKSSNRNSRVSPFVNQYSTPPLSSDHLNTDEISADTGERTVYLDVIDTPPESQADPLAGNQLKPALDVSPGRNTEQKSKSFLILSPNQFHDNEFHNTRSPMIDSPGTIISSNSNQNTKAVNLSVEDRPRSACPSPFAKVNRQARVVETNDEISTDGVDEDLAIGTPRQEHSRAGTLKSVSSPPPKVPLPSTPSRGEDISKKFSFVETPKGLGLEGVDYDNHEDQRSYIKSQQDQRQHDISEKTSPSSIMSTPKRVVGNFSPAVTNLEPKNSDLSNDQQHKHSQKNQNVSRTASLIKNLKHKRSTSGNQNKLAALFTTGSKEDHRNGHTRQTSDGSLFSSIANAYISPPITNGALGGRNHIRSTSDSTVLLSDEDHHYSNVAVKNDIEQLNSSKVLLEEDVKKLRDERHKLNEQLKMIQSKISSESIRYDNLVAEISELQIQKTKITNENKDLIEQQKNRQASGATGKLSTSSSNDSDPDASTLGKSVNTHLSPYKSSSDSTSVVSRENFEYSDHLSPDRHQGQFQQHQQYQQQYQQQQPQQQLIEDEQAHKATRLKFWRRPKVGTTQVISSNEYNNNGNGHNNGARIPNSFSTQALRIPAHNSGSSFNNNGANNNNQQNKFSKSKSSNVLDSLLSGDSSQVPLFNSTLQQRAEYEKSQVPIIITRCLAEVEKRGLDFEGIYRISGGNSAIVSIENAFSSLSNDPDEKQLNRVDETLDVDIHAVTSALKRYLRKLPDPVIPFDLYDDFIKVSTKASHSKEVRIAELQKIVNKLPPANRETLRLIVNHLHLVNSLKDINKMGYKNLSVVFAPTLAKDESGVKEMTDMGFRNDTTELLLTESHRIF
Protein: Nucleosome assembly protein 1-like 4 (Nucleosome assembly protein 2) (NAP-2) (Q99733)
Organism: Homo sapiens (Human)
Function: Acts as histone chaperone in nucleosome assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:10764593, ECO:0000269|PubMed:9325046}. Cytoplasm {ECO:0000269|PubMed:10764593, ECO:0000269|PubMed:9325046}. Note=Present in the cytoplasm and excluded from the nucleus during G0/G1 phase, then relocates to the nucleus by the time cells are in S phase (PubMed:9325046). Phosphorylated form localizes in the cytoplasm during the G0/G1 transition, whereas dephosphorylation leads to relocalization into the nucleus at the G1/S-boundary (PubMed:10764593). {ECO:0000269|PubMed:10764593, ECO:0000269|PubMed:9325046}.
Interaction partners:
- Nucleosome assembly protein 1-like 1
- Histone H2A.Z
- Pleckstrin homology-like domain family A member 2
- Melanoma-associated antigen D2
- Histone H2B type 2-E
- Nucleophosmin
- Nucleosome assembly protein 1-like 5
- Pescadillo homolog
- Diacylglycerol kinase zeta
- Histone H2A type 1-B/E
Sequence:
MADHSFSDGVPSDSVEAAKNASNTEKLTDQVMQNPRVLAALQERLDNVPHTPSSYIETLPKAVKRRINALKQLQVRCAHIEAKFYEEVHDLERKYAALYQPLFDKRREFITGDVEPTDAESEWHSENEEEEKLAGDMKSKVVVTEKAAATAEEPDPKGIPEFWFTIFRNVDMLSELVQEYDEPILKHLQDIKVKFSDPGQPMSFVLEFHFEPNDYFTNSVLTKTYKMKSEPDKADPFSFEGPEIVDCDGCTIDWKKGKNVTVKTIKKKQKHKGRGTVRTITKQVPNESFFNFFNPLKASGDGESLDEDSEFTLASDFEIGHFFRERIVPRAVLYFTGEAIEDDDNFEEGEEGEEEELEGDEEGEDEDDAEINPKV
Protein: Junctophilin-1 (JP-1) (Junctophilin type 1) (Q9HDC5)
Organism: Homo sapiens (Human)
Function: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH1 contributes to the construction of the skeletal muscle triad by linking the t-tubule (transverse-tubule) and SR (sarcoplasmic reticulum) membranes.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Sarcoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Localized predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic/sarcoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane. In skeletal muscle cells, it is predominantly localized at the junction of the A and I bands (By similarity). {ECO:0000250}.
Interaction partners:
- Ryanodine receptor 1
- Triadin
- Aspartyl/asparaginyl beta-hydroxylase
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Synaptophysin-like protein 2
- Calsequestrin-1
Sequence:
MTGGRFDFDDGGTYCGGWEEGKAHGHGICTGPKGQGEYSGSWSHGFEVVGGYTWPSGNTYQGYWAQGKRHGLGVETKGKWMYRGEWSHGFKGRYGVRQSLCTPARYEGTWSNGLQDGYGVETYGDGGTYQGQWAGGMRHGYGVRQSVPYGMATVIRSPLRTSLASLRSEQSNGSVLHDAAAAADSPAGTRGGFVLNFHADAELAGKKKGGLFRRGSLLGSMKLRKSESKSSISSKRSSVRSDAAMSRISSSDANSTISFGDVDCDFCPVEDHVDATTTETYMGEWKNDKRNGFGVSERSNGMKYEGEWANNKRHGYGCTVFPDGSKEEGKYKNNILVRGIRKQLIPIRHTKTREKVDRAIEGAQRAAAMARTKVEIANSRTAHARAKADAADQAALAARQECDIARAVARELSPDFYQPGPDYVKQRFQEGVDAKENPEEKVPEKPPTPKESPHFYRKGTTPPRSPEASPKHSHSPASSPKPLKKQNPSSGARLNQDKRSVADEQVTAIVNKPLMSKAPTKEAGAVVPQSKYSGRHHIPNPSNGELHSQYHGYYVKLNAPQHPPVDVEDGDGSSQSSSALVHKPSANKWSPSKSVTKPVAKESKAEPKAKKSELAIPKNPASNDSCPALEKEANSGPNSIMIVLVMLLNIGLAILFVHFLT
Protein: Transmembrane 6 superfamily member 1 (P58749)
Organism: Mus musculus (Mouse)
Function: May function as sterol isomerase.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:25422095}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Transmembrane protein 182
Sequence:
MSASAATGVFVLSLSAIPVTYIFNHLAAQHDSWTIVGVAALILLLVALLARVLVRRKPPRDPLFYVYAVFGFTSVVNLIIGLEQDGIIDGFMTHYLREGEPYLNTAYGHMICYWDGSVHYLMYLVMVAAIAWEESYRTIGLYWVGSIIMSIVVFVPGNIVGKYGTRICPAFFLSIPYTCLPVWAGFRIYNQPSENYNYPSKVLQEAQAKALLRRPFDLVLVLCLFLATGFCLFRGLIALDCPAELCRLYTQFQEPYLKDPAAYPKIQMLAYMFYSVPYFVIALYGLVVPGCSWMPDITLVHAGGLAQAQFSHIGASLHARTAYVYRVPEEAKIFFLALNIAYGVLPQLLAYRCTYNPEFFLRTKADEKLE
Protein: Kidins220 protein (Q80SX9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
AKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLLRNPKDGRLLYRPNKAGETPYNIDCSHQKSILTQIFGARHLSPTETDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGQQIEPLFQFSWLIVFLILLLCGGLGLVFAFTVDTNLAIAVSLSFLALLYIFFIVIYFGGRQEGESWNWAWALSTRLARHIGYLELLFKLMFVNPPELPEQTTKALPVRFLFTDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDSQGKKKWKKTCCLPSFIIFLFIVGCIIAGITLLAIFRVDPKHLTVNAILISIASIVGLAFVLNCRTWWQVLDSLLNSQRKRLHSAASKLHKLKSEGFMKVLKCEVELMARMAKTIDSFTQNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLRDSNINGHDYMRNIVHLPVFLNSRGLSNARKFLVTSATNGDISCSEATGVQEDADRRVSQNSLGEMTKLGSKTALNRRDTYRRRQMQRTITRQMSFDLTKLLVTEDWFSDISPQTMRRLLNIVSVTGRLLRANQITFNWDRLASWINLTEQWPYRTSWLILYLGETEGIPDQMTLKTIYERISKNIPTTKDVEPLLEIDGDIRNFEVFLSSRTPVLVARDVKTFLPCTVNLDPKLREIIADVRAAREQINIGGLAYPPLPLHEAPPRPPSGYSQPASVCSSSASFNGPFPGGVVSPQPHSSYYSGLSGPQHPFYNRASVPATGTSLLLSSMTVDIVCEKLRQIEGLDQGMLPQYCTTIKKANINGRVLAQCNIDELKKEMAMNFGDWHLFRSMVLEMRSVENQVVPEDPRFLNENSSAPVAHGESARRTSHSELPHTELSSQTPYTLNFSFEELNTLGLDEGAPRHSNLSWQSQTRRTPSLSSLNSQDSSIEISKLTDKVQAEYRDAYREYIAQMSQLEGGTGSSTISGRSSPHSTYYIGQSSSGGSIHSNLEQERGKENELKQEEGRKSFLMKRGDVLDYSSSGVSTNEASPLDPITEEDEKSDQSGSKLLPGKKSSERPSLFQTDLKLKGSGLRYQKLPSDEDESGTEESDNTPLLKDDKDKKAEGKAERVAKSPEHSVEPIRTFIKAKEYLSDALLDKKDSSDSGVRSNESSPNHSLHNEAADDSQLEKANLIELEDEGHSGKRGMPHSLSGLQDPVIARMSICSEDKKSPSECSLIASSPEESWPSCQKAYNLNRTPSTVTLNNNTAPTNRANQNFDEIEGVRETSQVILRPGPSPNPTAVQNENLKSMAHKRSQRSSYTRLSKDASELHAASSDSTGFGEERESIL
Protein: Cation channel sperm-associated auxiliary subunit beta (CatSper-beta) (Q9H7T0)
Organism: Homo sapiens (Human)
Function: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:A2RTF1}; Single-pass membrane protein {ECO:0000250|UniProtKB:A2RTF1}. Note=Predominantly located in the principal piece of the sperm tail. {ECO:0000250|UniProtKB:A2RTF1}.
Interaction partners:
- Cation channel sperm-associated protein 1
- Cation channel sperm-associated auxiliary subunit delta
- Cation channel sperm-associated protein 4
- Cation channel sperm-associated auxiliary subunit gamma
- Cation channel sperm-associated protein 3
- Cation channel sperm-associated auxiliary subunit epsilon
- Cation channel sperm-associated protein 2
- EF-hand calcium-binding domain-containing protein 9
- Cation channel sperm-associated auxiliary subunit zeta
- Heat shock-related 70 kDa protein 2
Sequence:
MESPLIYVSVLLLNIFEFSSGIVYNKDDTEKRFACSNKGFPQENEIIKLYLFLENLKIQCFFQTENEIASKAMLSVFTSGGLAPSLGIMNSTYNGIFHFNLTLFSDRILWLVDIPRENITQSTDIAAVEEWLVRITLHHGLNIYATEGTLLDVIREPILQWTPGDVIPESEISKLYPHVVDLKVTKCPCANDVALLGFIVDTIVDGVYIGITFGGFWHDYDTTWFNMTQTIYSQLQEEYEDLSLVDMVLTNHFLVILTSLGLFVSEDLRYPSRHSLSFSRADFCGFERVDYVKGKLWYNERCFANREHFEVDYVTVTFERNRTLSESSSCFYSQEPFLEWVPCLPHIFKGIKIFPTVLTFLVDQERGTGVYLFYNKVRKTAIASVSTLRNNEPNSQSKFPIFRFPSSFSSPVGMVFHPRSHFLYAYGNQIWLSVDGGNTFQLIANFHDDIIKKTFHSFYTSAITFVSQRGKVYSTKAGMGRYSAVGSVTERIFTLYYDHLGFLHKLTLGRFEASGPPTAFGNSRNLFGQPPDMGFETALAPQHTSLDEIIFFAYVPENEPQETIYSKKFGNIHYGKVIHSGKTGRAYIRKVLQHTTPKGFLSSVIAEMKEPFGLEEVNESSCLSSSLLINKAGNVYKLTLDSQVVQALFEDTDIEKTVVLPGYSSFLITSILDNKNALAIATMPESAPNNMTFLKSTWFLYNFGQRNGRTWKIYSKPCNYWFQHDDSPSLNIVKYIDLGNSYVLKAKVIRNAKGFRMLEIPLLTVFVGNPNLLEVTAEVTFDDTDSYVITISAASKVLHQGSTSLAFIMWSASTECFVTTMVPTLKSSCSYLRSMHHIPSKFIPFEDWISGVHKDSQGFNLIKTLPINYRPPSNMGIAIPLTDNFYHADPSKPIPRNMFHMSKKTGKFKQCANVSTREECNCTKDQKFSHAVAFSDCREKVPRFKFPITQYPVSLEIINEDGRVPLQSPYLVTVTEVNMRHNWKLKHTVPENIKRMKQLVEPILGAAVYNPSGLNLSIKGSELFHFRVTVISGVTFCNLIEEFQIYVDEAPLPFPGHTLIAVATAVVLGGLIFIAFMFQLQGIHPWRTFQRWIRRNQEKFSSISLSELIHRSKSEE
Protein: ShKT domain-containing protein (O16420)
Organism: Caenorhabditis elegans
Interaction partners:
- Flo11 domain-containing protein
- Selenoprotein F
- Helix-loop-helix protein 6
- Prion-like-
- SCP domain-containing protein
- EB domain-containing protein
- Soluble guanylate cyclase gcy-37
Sequence:
MIAIISILFASFLAPEVSAAIGGDLNCTVYNGTMFVWTPAAVACQNTISDASCAILYPTTDTLGLPAAGNAAGRPLACYTTATVTPAAVVLDMKTAALASCPKTCGFCCNTDAFNCKNADYPRLNCATITNSQCNSPAWRNIIAADCPSACGFCGQGGCVDAVTNCGNDLSICQNIGMQSFVNTYCQKSCGRCPSTTTSGYNNGGGSCTSYVADSSSNCASWAKNGFCTNNFYTVDQRRARCGSTCRIC
Protein: Polyubiquitin-C [Cleaved into: Ubiquitin; Ubiquitin-related 1; Ubiquitin-related 2] (P0CG50)
Organism: Mus musculus (Mouse)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P0CG48}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0CG48}.
Interaction partners:
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- E3 ubiquitin-protein ligase parkin
- Ubiquitin-conjugating enzyme E2 D3
- Vacuolar protein-sorting-associated protein 36
- Ubiquitin-like modifier-activating enzyme 1
- Proteasomal ubiquitin receptor ADRM1
- Ubiquitin-like modifier-activating enzyme 1 Y
- NF-kappa-B essential modulator
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLDVEPSVTTKKVKQEDRRTFLTTVSKKSPPCACSWV
Protein: Probable phospholipid-transporting ATPase IIA (EC 7.6.2.1) (ATPase class II type 9A) (O75110)
Organism: Homo sapiens (Human)
Function: Plays a role in regulating membrane trafficking of cargo proteins, namely endosome to plasma membrane recycling and endosome to trans-Golgi network retrograde transport. In complex with MON2 and DOP1B, regulates SNX3 retromer-mediated endosomal sorting of WLS, a transporter of Wnt morphogens in developing tissues. Participates in the formation of endosomal carriers that direct WLS trafficking back to Golgi, away from lysosomal degradation. Appears to be implicated in intercellular communication by negatively regulating the release of exosomes. The flippase activity towards membrane lipids and its role in membrane asymmetry remains to be proved.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620, ECO:0000269|PubMed:30213940}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:36604604}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620, ECO:0000269|PubMed:30213940}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30947313}; Multi-pass membrane protein. Note=Efficient exit from the endoplasmic reticulum does not require TMEM30A, nor TMEM30B (PubMed:21914794). Transiently expressed in the cell membrane (PubMed:30947313). {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:30947313}.
Interaction partners:
Sequence:
MTDNIPLQPVRQKKRMDSRPRAGCCEWLRCCGGGEARPRTVWLGHPEKRDQRYPRNVINNQKYNFFTFLPGVLFNQFKYFFNLYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTVIREAVEEIRCYVRDKEVNSQVYSRLTARGTVKVKSSNIQVGDLIIVEKNQRVPADMIFLRTSEKNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFVGTFTREDSDPPISESLSIENTLWAGTVVASGTVVGVVLYTGRELRSVMNTSNPRSKIGLFDLEVNCLTKILFGALVVVSLVMVALQHFAGRWYLQIIRFLLLFSNIIPISLRVNLDMGKIVYSWVIRRDSKIPGTVVRSSTIPEQLGRISYLLTDKTGTLTQNEMIFKRLHLGTVAYGLDSMDEVQSHIFSIYTQQSQDPPAQKGPTLTTKVRRTMSSRVHEAVKAIALCHNVTPVYESNGVTDQAEAEKQYEDSCRVYQASSPDEVALVQWTESVGLTLVGRDQSSMQLRTPGDQILNFTILQIFPFTYESKRMGIIVRDESTGEITFYMKGADVVMAGIVQYNDWLEEECGNMAREGLRVLVVAKKSLAEEQYQDFEARYVQAKLSVHDRSLKVATVIESLEMEMELLCLTGVEDQLQADVRPTLETLRNAGIKVWMLTGDKLETATCTAKNAHLVTRNQDIHVFRLVTNRGEAHLELNAFRRKHDCALVISGDSLEVCLKYYEYEFMELACQCPAVVCCRCAPTQKAQIVRLLQERTGKLTCAVGDGGNDVSMIQESDCGVGVEGKEGKQASLAADFSITQFKHLGRLLMVHGRNSYKRSAALSQFVIHRSLCISTMQAVFSSVFYFASVPLYQGFLIIGYSTIYTMFPVFSLVLDKDVKSEVAMLYPELYKDLLKGRPLSYKTFLIWVLISIYQGSTIMYGALLLFESEFVHIVAISFTSLILTELLMVALTIQTWHWLMTVAELLSLACYIASLVFLHEFIDVYFIATLSFLWKVSVITLVSCLPLYVLKYLRRRFSPPSYSKLTS
Protein: E3 ubiquitin-protein ligase FANCL (EC 2.3.2.27) (Fanconi anemia group L protein) (Fanconi anemia-associated polypeptide of 43 kDa) (FAAP43) (RING-type E3 ubiquitin transferase FANCL) (Q9NW38)
Organism: Homo sapiens (Human)
Function: Ubiquitin ligase protein that mediates monoubiquitination of FANCD2 in the presence of UBE2T, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCI. May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage, whereas it is probably not needed for spermatogonial proliferation after birth.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9CR14}. Nucleus {ECO:0000250|UniProtKB:Q9CR14}.
Interaction partners:
- Transcription factor HES-1
- Fanconi anemia core complex-associated protein 100
- Fanconi anemia group G protein
- Fanconi anemia group B protein
- Fanconi anemia group M protein
- Fanconi anemia group C protein
- Fanconi anemia group D2 protein
- Fanconi anemia core complex-associated protein 24
- Fanconi anemia group A protein
- Centromere protein S
Sequence:
MAVTEASLLRQCPLLLPQNRSKTVYEGFISAQGRDFHLRIVLPEDLQLKNARLLCSWQLRTILSGYHRIVQQRMQHSPDLMSFMMELKMLLEVALKNRQELYALPPPPQFYSSLIEEIGTLGWDKLVYADTCFSTIKLKAEDASGREHLITLKLKAKYPAESPDYFVDFPVPFCASWTPQSSLISIYSQFLAAIESLKAFWDVMDEIDEKTWVLEPEKPPRSATARRIALGNNVSINIEVDPRHPTMLPECFFLGADHVVKPLGIKLSRNIHLWDPENSVLQNLKDVLEIDFPARAILEKSDFTMDCGICYAYQLDGTIPDQVCDNSQCGQPFHQICLYEWLRGLLTSRQSFNIIFGECPYCSKPITLKMSGRKH
Protein: Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (Mad homolog 7) (SMAD family member 6) (SMAD 6) (Smad6) (O35182)
Organism: Mus musculus (Mouse)
Function: Transforming growth factor-beta superfamily receptors signaling occurs through the Smad family of intracellular mediators. SMAD6 is an inhibitory Smad (i-Smad) that negatively regulates signaling downstream of type I transforming growth factor-beta (By similarity). Acts as a mediator of TGF-beta and BMP anti-inflammatory activities. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of pro-inflammatory genes. Blocks the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory elements in target promoter regions (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase SMURF1
- E3 ubiquitin-protein ligase SMURF2
- Mothers against decapentaplegic homolog 1
- Mothers against decapentaplegic homolog 7
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 9
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 5
- Bone morphogenetic protein receptor type-1B
- Mothers against decapentaplegic homolog 3
Sequence:
MFRSKRSGLVRRLWRSRVVPDREEGSGGGGGVDEDGSLGSRAEPAPRAREGGGCSRSEVRSVAPRRPRDAVGPRGAAIAGRRRRTGGLPRPVSESGAGAGGSPLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDSGDPQARQSPEPEEGGGPRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFTAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPPDQYKPLDLSDSTLSYTETEATNSLITAPGEFSDASMSPDATKPSHWCSVAYWEHRTRVGRLYAVYDQAVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGFGILLSKEPDGVWAYNRGEHPIFVNSPTLDAPGGRALVVRKVPPGYSIKVFDFERSGLLQHADAAHGPYDPHSVRISFAKGWGPCYSRQFITSCPCWLEILLNNHR