wanglab/gogpt-training-data huggingface dataset:
Protein: Synaptotagmin-6 (Synaptotagmin VI) (SytVI) (Q5T7P8)
Organism: Homo sapiens (Human)
Function: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. May mediate Ca(2+)-regulation of exocytosis in acrosomal reaction in sperm (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q9R0N8}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R0N8}.; SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000250|UniProtKB:Q9R0N8}; Single-pass membrane protein {ECO:0000250}. Note=Localized predominantly to endoplasmic reticulum (ER) and/or Golgi-like perinuclear compartment (By similarity). {ECO:0000250|UniProtKB:Q9R0N8}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9R0N8}. Cell membrane {ECO:0000250|UniProtKB:Q9R0N8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9R0N8}.
Interaction partners:
- Synaptotagmin-10
- Synaptotagmin-3
Sequence:
MSGVWGAGGPRCQEALAVLASLCRARPPPLGLDVETCRSFELQPPERSPSAAGAGTSVSLLAVVVIVCGVALVAVFLFLFWKLCWMPWRNKEASSPSSANPPLEALQSPSFRGNMADKLKDPSTLGFLEAAVKISHTSPDIPAEVQMSVKEHIMRHTRLQRQTTEPASSTRHTSFKRHLPRQMHVSSVDYGNELPPAAEQPTSIGRIKPELYKQKSVDGEDAKSEATKSCGKINFSLRYDYETETLIVRILKAFDLPAKDFCGSSDPYVKIYLLPDRKCKLQTRVHRKTLNPTFDENFHFPVPYEELADRKLHLSVFDFDRFSRHDMIGEVILDNLFEASDLSRETSIWKDIQYATSESVDLGEIMFSLCYLPTAGRLTLTVIKCRNLKAMDITGYSDPYVKVSLLCDGRRLKKKKTTIKKNTLNPVYNEAIIFDIPPENMDQVSLLISVMDYDRVGHNEIIGVCRVGITAEGLGRDHWNEMLAYPRKPIAHWHSLVEVKKSFKEGNPRL
Protein: Rab-like protein 3 (Q9D4V7)
Organism: Mus musculus (Mouse)
Function: Required for KRAS signaling regulation and modulation of cell proliferation. Regulator of KRAS prenylation, and probably prenylation of other small GTPases (By similarity). Required for lymphocyte development and function. Not required for myeloid cell development.
Interaction partners:
Sequence:
MASLDRVKVLVLGDSGVGKSSLVHLLCHNQVLGNPSWTVGCSVDIRVHDYKEGTPEEKTYYIELWDVGGSVGSASSVKSTRAVFYNSVNGIILVHDLTNKKSSQNLYRWSLEVLNRDAVPTGVLVTNGDYDREQFADNQIPLLVIGTKLDQIHETKRHEVLIRTAFLAEDFNAEEINLDCTNPRSSAAGSSNAVKLSRFFDKVIEKRYFFREGNQIPGFSDRKRFGGGALKNFHCD
Protein: Protein-serine O-palmitoleoyltransferase porcupine (EC 2.3.1.250) (Q9VWV9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Protein-serine O-palmitoleoyltransferase that acts as a key regulator of the Wnt signaling pathway by mediating the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins. Serine palmitoleoylation of Wnt proteins is required for efficient binding to frizzled receptors (By similarity). Also facilitates the glycosylation of Wnt family members, including wg and Wnt5. The cotranslational disulfide bond formation of wg competes with the N-glycosylation. Porc stimulates the post-translational N-glycosylation by anchoring wg at the ER membrane, probably through acylation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11821428, ECO:0000269|PubMed:8985181}; Multi-pass membrane protein {ECO:0000269|PubMed:11821428, ECO:0000269|PubMed:8985181}.
Interaction partners:
- Protein wingless
- Protein Wnt-5
- Wnt inhibitor of Dorsal protein
- Protein Wnt
- Protein Wnt
- Protein wntless
Sequence:
MDYQYFEEESDYIDLDEEEEDDDVVTAGSLDHRFGQPNGEEDYYFGGDDVEEELVVDGHGVLELAGRLLESLQSCVQPSVLQVMQYVAPMLLLCLLCRLLCLLYSQRRRLTSLAPLHLFHFACGLIILQITVGYRLLLLLLLAAVGYLLLQLLRLGRRGAQVLAVLTVGSQFLYELLIWRRRSDWPQLRGIQMVVNMKLISLGFDLTASGQLQARIPGPFAYLGYIYSPATCALGPWVSFGCYMDCLVPRNSWLVSLRRLLPNVVICVLAVTVSNCVAPALSDFFGDSSHFLVMYWDALSVRSSHYFVGMMAQALLVASDQRLDGATKESDMLGPLISQPWRIEWPRSISSLVRSWNIPMHEWLKRYIYAPCKPTASTSRGRILVVVLSTYLVSSLLHGMDLRIYLVLISLAFLAEGESLLRRQLASLLNACITANLCPGKERCRYSHCPSKRRLNSLSYWLARLTNLAFTALAIFHLAYLGVVLLGDDLEVGEDGDSFLWHWQQAGYLSHYIGLGTFVLYLFIS
Protein: Putative guanine nucleotide exchange factor RhoGEF2 (O44113)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MDDPSIKKRLLDLYTDEHEYDEVQEIPEESSIQPPETSTSHTSTNGSSHSGPGTATGPGATSAGPSAGAPQSPVIVVDSVPELPAPKQKSVKNSKSKQKQKQLANKSKIPRSPSLASSLSSLASSLSGHRDRDKDRDKDRENQNAVPPQTPPLPPSYKQNQMNGDSTAAAGGGVSAPATPTTANNNNASHNNGSIMGGGVQLNQSDNSNPVLQAPGERSSLNLTPLSRDLSGGHTQESTTPATTPSTPSLALPKNFQYLTLTVRKDSNGYGMKVSGDNPVFVESVKPGGAAEIAGLVAGDMILRVNGHEVRLEKHPTVVGLIKASTTVELAVKRSQKLTRPSSVSVVTPSTPILSGRDRTASITGPQPVDSIKRREMETYKIQTLQKMLEQEKLNLERLKSDQNNPSYKLSEANIRKLREQLHQVGAEDAPTVKLQAAAGNKNTALLTPNQIQHLSASATHSNQQFHHLHHHHNLHNNNYPPQQQPASTSPAFLSLLPRSLSSLSLGTRKNKTEKDLTTSSPFGLTTDFLQQQRMSHQAESMSQSMHQHTSTPTSQQFFHPHQQQHRFKETGPTSKGKNKFLISRSLIEEDVPPPLPQRNPPRQLNLDLKNGNASPGGSHLVAPVSDLDRATSPQLNRSQQQQLPRSTDNSPSNAKSKRSKIKTKALSDPKMSTQMFLQMESASAAGAAGGSIEVDGGPPPLPPRLPGMMTEDMSRGSCQNLAQPNSVGTAFNYPLVSTTTAVQNDNLNIAFPLSQRPNIVQQLQQYQQQQQHQMSGGQATGALGQTPNLGKNKHRRVGSSPDNMHPRHPDRITKTTSGSWEIVEKDGESSPPGTPPPPYLSSSHMTVLEDPNENNRGAAAAGPGVFIESHQFTPMAGASSPIPISLHSNHMHAAQSNDTQKEIISMEDENSDLDEPFIDENGPFNNLTRLLEAENVTFLAIFLNYVISNSDPAPLLFYLITELYKEGTSKDMRKWAYEIHSTFLVPRAPLSWYRQDESLAREVDNVLQLEYDKVEILRTVFLRSRKRAKDLISEQLREFQQKRTAGLGTIYGPTDDKLAEAKTDKLREQIIDKYLMPNLHALIEDENGSPPEDVRKVALCSALSTVIYRIFNTRPPPSSIVERVHHFVSRDKSFKSRIMGKNRKMNVRGHPLVLRQYYEVTHCNHCQTIIWGVSPQGYHCTDCKLNIHRQCSKVVDESCPGPLPQAKRLAHNDKISKFMGKIRPRTSDVIGNEKRSRQDEELNVELTPDRGQASIVRQPSDRRPDANISIRSNGNTSCNTSGLNTTDLQSSFHGSCANDSINPGGGAGCNMDLSTSVASTTPSTSGSVAAGLSAFAELNALDTVDKEARRERYSQHPKHKSAPVSVNWSESYKERLSNKRNRNSRRKTSDPSLSSRPNDEQLDLGLSNATYVGSSNSSLSSAGGTESPSTSMEHFAAPGAAGGVQVPPMGLNQNQHPHLLIQQHAQQYCQQDSFQAGLAGAAGSSAASNSSFWNAGHPLPVARWTLESEDEDDVNEADWSSMVAAEVSAALTDAEKKRQEIINEIYQTERNHVRTLKLLDRLFFLPLYESGLLSQDHLLLLFPPALLSLREIHGAFEQSLKQRRIEHNHVVNTIGDLLADMFDGQSGVVLCEFAAQFCARQQIALEALKEKRNKDEMLQKLLKKSESHKACRRLELKDLLPTVLQRLTKYPLLFENLYKVTVRLLPENTTEAEAIQRAVESSKRILVEVNQAVRTAEDAHKLQNIQRKLDRSSYDKEEFKKLDLTQHHLIHDGNLTIKKNPSVQLHGLLFENMIVLLTKQDDKYYLKNLHTPLSITNKPVSPIMSIDADTLIRQEAADKNSFFLIKMKTSQMLELRAPSSSECKTWFKHFSDVAARQSKNRSKNASSNHDTSISDPALAAIPHSNTKESLELSTDTVQPLAATATLTTTPLAPMLPIATVTPAPATNNSNVSSLTGVQLRNPQRDATASESDADYVNTPKPRSSQNEVNRTMSIRSTGEPIQKYSANGTEANDVTLRHSQSTRESVRPGSTGEERNSTYGMVGGNSKRDSASIVCSNNSNNTRTLLMQSPLVDPTAIQVSISPAHTAEPVLTPGEKLRRLDASIRNDLLEKQKIICDIFRLPVEHYDQIVDIAMMPEAPKDSADIALAAYDQIQTLTKMLNEYMHVTPEQEVSAVSTAVCGHCHEKEKLRKKVAPSSSFSSSPPPLPPPNRQHAQAQAQIPPSRLMPKLQTLDLDEVAIHEDDDGYCEIDELRLPAIPSKPHERPTTPLAPFNTEPKTSQSVIDASKRQSTDAVPEGLLEQEPLEGDKTETKGEDNEVKTVPSDKLSESCNEERQCVEADITKEVADPTTSKNEAAASVDELPSQSREIKTAENASKSVADKKEDNEETIEEGVASTVDSSTQTSPTESPKETDKLTGGSSSTCGPNRIQHASVLEPSVPCHALSSIVTILNEQISMLLPKINERDMERERLRKENQHLRELLSALHDRQRVDEVKETPFDLKKLMHAEDVEFDDDIDAISNSSLTPTPTPIPTASPSASGQVETAEAMRITSTEDEE
Protein: ATP synthase subunit alpha (EC 7.1.2.2) (ATP synthase F1 sector subunit alpha) (F-ATPase subunit alpha) (P27179)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
Interaction partners:
- ATP synthase subunit b
- ATP synthase epsilon chain
- ATP synthase gamma chain
- ATP synthase subunit delta
- ATP synthase subunit a
- ATP synthase subunit c
- ATP synthase subunit b'
- ATP synthase subunit beta
- Hydrogenase subunit
- Elongation factor Tu
Sequence:
MVSIRPDEISSIIRQQIESYDQSVQVSNVGTVLQVGDGTARIYGLEQVMSQELLEFEDGTIGIALNLEEDNVGAVLMGDGFGIQEGSTVKTTGQIAQIPIGDAMVGRVVDSLGRPIDGKGPISSTATRLLESPAPGIIERKSVCEPMQTGITAIDAMIPIGRGQRELIIGDRKTGKTAIAIDTIINQKSEDVICVYVAIGQKASTVAQIIDTLTEKGAMAYTIVVAANANDPATLQYLAPYTGATLAEHFMYQGKSTLVIYDDLSKQAQAYRQMSLLMRRPPGREAYPGDVFYIHSRLLERAAKLSDALGGGSMTALPVIETQAGDVSAYIPTNVISITDGQIFLSTDLFNAGFRPAINAGISVSRVGSAAQTKAMKKVAGKLKLELAQFAELEAFSQFASDLDAATQAQLARGQRLRQLLKQPENSPLSVWEQVAISYAGLNGYIDTIPVDKVTEFAQGLRDYLKANKAKYVEIINSSKALTDEAETLLKEGIKEFTQGFAA
Protein: Carboxypeptidase O (EC 3.4.17.-) (B8JLQ9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Carboxypeptidase which preferentially cleaves C-terminal acidic residues from peptides and proteins. Can also cleave C-terminal hydrophobic amino acids, with a preference for small residues over large residues.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q8IVL8}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8IVL8}.
Interaction partners:
- Kinectin 1
Sequence:
MMQASITSILVVLTLVAQDRLAGGLEHKSYDYTKYHTMDEISAWMNQMQRENPDVVSTMTYGQTYEKRNITLLKIGFSSTTPKKAIWMDCGIHAREWIAPAFCQHFVKEVLGSYKTDSRVNMLFKNLDFYITPVLNMDGYIYSWLNNSTRLWRKSRSPCHENSTCSGTDLNRNFYANWGMVGISRNCCSEVYNGATALSEPEAEAVTDFLGAHQNHLLCYLTIHSYGQLILVPYGHPNISAPNYDELMEVGLAAAKAIKAVHGKSYKVGSSPDVLYPNSGSSRDFARLIGIPYSFTFELRDEGQHGFILPEDQIQPTCQEAYEGAMSIINYVHDKNFKNTAITVTATLWTTLMALWISTSHVF
Protein: Polyadenylate-binding protein 1 (PABP-1) (Poly(A)-binding protein 1) (Q9EPH8)
Organism: Rattus norvegicus (Rat)
Function: Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11940}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P11940}. Nucleus {ECO:0000250|UniProtKB:P11940}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P11940}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). Shuttles between the cytoplasm and the nucleus (By similarity). During stress and in the absence of DDX3X, localizes to the nucleus (By similarity). At the leading edge of migrating fibroblasts, colocalizes with DDX3X (By similarity). Relocalizes to cytoplasmic stress granules upon cellular stress where it colocalizes with ENDOV (By similarity). {ECO:0000250|UniProtKB:P11940}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Polyadenylate-binding protein-interacting protein 1
- Eukaryotic translation initiation factor 4B
- Y-box-binding protein 1
- RNA helicase
- Eukaryotic translation initiation factor 4 gamma 1
- Regulator of nonsense transcripts 1
- Heat shock cognate 71 kDa protein
- U6 snRNA-associated Sm-like protein LSm1
- Heterogeneous nuclear ribonucleoprotein A3
Sequence:
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKELFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAATAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPSLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV
Protein: DASH complex subunit DUO1 (Death upon overproduction protein 1) (Outer kinetochore protein DUO1) (P53168)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A, and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9817759}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9817759}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:9817759}. Note=Associates with the mitotic spindle and the kinetochore. {ECO:0000269|PubMed:9817759}.
Interaction partners:
- DASH complex subunit DAD2
- DASH complex subunit DAD4
- DASH complex subunit SPC34
- DASH complex subunit DAD1
- DASH complex subunit SPC19
- DASH complex subunit DAD3
- DASH complex subunit DAM1
- DASH complex subunit ASK1
- DASH complex subunit HSK3
- Inner kinetochore subunit CHL4
Sequence:
MSEQSQLDDSTIDKLIPQIFNEMRSNLNNTTNKFPKSTGGGASDNISANSNSIRSFNSITTQSLLKESESLDKITAMIKNVTAALKNNLPVYVNQVHEVCKSTNSILDSWINIHSQAGYIHKLMSDQTYLKLINDRLHNENVNTNDEDGSTLHNVIALKKKEILDLRQKLENRKGEKDAAPAKPPNQGLNPRYGVQSGRRPVPSAGISNNGRVRKTHVPASKRPSGIPRVTNRWTKPTASSSRKMFR
Protein: L-type lectin-domain containing receptor kinase I.7 (LecRK-I.7) (EC 2.7.11.1) (Q9LSS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9LSR8}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Early nodulin-like protein 12
- Beta-glucosidase 19
- UDP-glycosyltransferase 74E1
- Purine permease 3
- Probable 3'
- 3',5'-bisphosphate nucleotidase 2
- BTB/POZ and MATH domain-containing protein 1
- Probable 3'
- Histone-lysine N-methyltransferase ATX3
- Putative purine permease 15
Sequence:
MIRGLLLGIIWMIFCVCSSFQQETPFVYNNFGHVDHLHLDGSARIIPSGGILQLTNATNSQIGHVFYEKPIEFKSSESVSFSTYFVCALLPAGDPSGHGMTFFVSHSTDFKGAEATRYFGIFNRNGSTSTRVLAVELDTSLASDVKDISDNHVGIDVNSAESITSANASYFSDKEGKKIDIKLLSGDPIQVWVDYEGTTLNVSLAPLRNKKPSRPLLSSTSINLTDILQGRRMFVGFSGSTGSSMSYQYILGWSFSKSMASLPNIDISKLPKVPHSSTKKKSTSPVLSVLLGLIAFIVLGILVVAYLYRRNLYSEVREEWEKEYGPIRYSYKSLYKATKGFNRSEFLGRGGFGEVYKGTLPRSRELREVAVKRVSHDGEHGMKQFVAEIVSMRSLKHRSLVPLLGYCRRKHELLLVSEYMPNGSLDHYLFNHDRLSLPWWRRLAILRDIASALSYLHTEADQVVIHRDIKAANVMLDAEFNGRLGDFGMSRLYDRGADPSTTAAVGTVGYMAPELTTMGASTGTDVYAFGVFLLEVTCGRRPVEPGLPEAKRFLIKWVSECWKRSSLIDARDPRLTEFSSQEVEKVLKLGLLCANLAPDSRPAMEQVVQYLNGNLALPEFWPNSPGIGVLSPMALSPAPLVIPSLSFSSSSSNNSMFITHSVLYGSGR
Protein: Auxilin (EC 3.1.3.-) (DnaJ homolog subfamily C member 6) (Q27974)
Organism: Bos taurus (Bovine)
Function: Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Plays a role in clathrin-mediated endocytosis in neurons (By similarity).
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:20826345, ECO:0000269|PubMed:31962345}. Note=Appears on coated vesicles in successive transient bursts, immediately after the vesicle release from the plasma membrane (PubMed:31962345). Recruitment to clathrin-coated vesicles depends on temporal variations in phosphoinositide composition of clathrin-coated vesicles (PubMed:31962345). {ECO:0000269|PubMed:31962345}.
Interaction partners:
- Clathrin heavy chain 1
- DnaJ heat shock protein family
- Clathrin heavy chain linker domain containing 1.
- DnaJ heat shock protein family
- Synaptojanin-1
- Polyamine-transporting ATPase 13A2
- F-box only protein 7
- DnaJ homolog subfamily B member 6
- Vacuolar protein sorting-associated protein 35
- Clathrin light chain B
Sequence:
MDSSGASSPDMEPSYGGGLFDMVKGGAGRLFSNLKDNLKDTLKDTSSRVIQSVTSYTKGDLDFTYVTSRIIVMSFPLDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYMCDLLADKPYRPHFKPLTIKSITVSPVPFFNKQRNGCRPYCDVLIGETKIYTTCADFERMKEYRVQDGKIFIPLSITVQGDVVVSMYHLRSTIGSRLQAKVTNTQIFQLQFHTGFIPLDTTVLKFTKPELDACDVPEKYPQLFQVTLDVELQPHDKVMELTPPWEHYCTKDVNPSILFSSHQEHQDTLVLGGQAPIDIPPDNPRHFGQGGFFSTLCWQDQKSEKSFCEEDHAALVNQESEQSDDELLTLSSPHGNANGDKPHAARKPSKKQQEPAAPAPPEDVDLLGLEGSAVSKNFSSPAAPPSNSELLSDLFGGGGAAGPVQSGQSGVDDVFHPSGPTSTQSTPRRSATSTSASPTLRVGEGATFDPFGAPSKPSGQDLLGSFLNTASASSDPFLQPTRSPSPTVHASSTPAVNIQPDVSGAWDWHTKPGGFGMGSKSAATSPTGSSHGTPTHQNKPQTLDPFADLGTLGGSSFASKPSTPTGLGGGFPPLSSPQKASPQPMGGGWQQGGGYNWQQTQSKPQSSMPHSSPQNRPNYNVSFSSMPGGQNERGKAAANLEGKQKAADFEDLLSGQGFNAHKDKKGPRTIAEMRKEEMAKEMDPEKLKILEWIEGKERNIRALLSTMHTVLWAGETKWKPVGMADLVTPEQVKKVYRKAVLVVHPDKATGQPYEQYAKMIFMELNDAWSEFENQGQKPLY
Protein: Ornithine decarboxylase antizyme 3 (AZ3) (ODC-Az 3) (OAZ-t) (Q9R109)
Organism: Mus musculus (Mouse)
Function: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity. Stabilizes AZIN2 by interfering with its ubiquitination. Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol. Probably plays a key role in spermatogenesis by regulating the intracellular concentration of polyamines in haploid germ cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:15642376}. Cytoplasm {ECO:0000269|PubMed:15642376}.
Interaction partners:
- Ornithine decarboxylase
- Antizyme inhibitor 2
- Antizyme inhibitor 1
- Gene model 853
- Outer dense fiber protein 1
- Gametogenetin-binding protein 2
- Spermatogenesis-associated protein 6
- Gametogenetin-binding protein 1
- Spermatogenesis-associated protein 19, mitochondrial
Sequence:
MPCNRSRPSLYSLSYIKRGKTRNYLYPFWSPFAYYLYCYKYRITLREKMLPCCYKSITYKEQEDLTLRPHCCLPCSCLPCSCLQCSESLGGLQVGRSTAQEKDHSQLKELYSAGNLTVLSTDPLLHQDPVQLDFHFRLTPHSSAHWHGLLCDHRLFLDIPYQALDQGNRESLTATLEYVEEKTNVDSVFVNFQIDRKDRGALLRAFSYMGFEVVRPDHPALPPWDNVIFMVYPLERDLGHPGQ
Protein: Multidrug resistance protein MdtH (P69367)
Organism: Escherichia coli (strain K12)
Function: Confers resistance to norfloxacin and enoxacin.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Multidrug resistance protein MdtG
- Multidrug resistance protein MdtL
- Multidrug resistance protein MdtK
- Multidrug resistance protein MdtM
- Probable multidrug resistance protein EmrK
- Multidrug resistance protein D
- Multidrug resistance protein MdtA
- Multidrug resistance outer membrane protein MdtP
- DNA damage-inducible protein I
- Fosmidomycin resistance protein
Sequence:
MSRVSQARNLGKYFLLIDNMLVVLGFFVVFPLISIRFVDQMGWAAVMVGIALGLRQFIQQGLGIFGGAIADRFGAKPMIVTGMLMRAAGFATMGIAHEPWLLWFSCLLSGLGGTLFDPPRSALVVKLIRPQQRGRFFSLLMMQDSAGAVIGALLGSWLLQYDFRLVCATGAVLFVLCAAFNAWLLPAWKLSTVRTPVREGMTRVMRDKRFVTYVLTLAGYYMLAVQVMLMLPIMVNDVAGAPSAVKWMYAIEACLSLTLLYPIARWSEKHFRLEHRLMAGLLIMSLSMMPVGMVSGLQQLFTLICLFYIGSIIAEPARETLSASLADARARGSYMGFSRLGLAIGGAIGYIGGGWLFDLGKSAHQPELPWMMLGIIGIFTFLALGWQFSQKRAARRLLERDA
Protein: Membrane-associated guanylate kinase, WW and PDZ domain-containing 2a (Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2a) (F1Q897)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
- Myosin, light chain 12, genome duplicate 2
- TBC1 domain family, member 10Aa.
- Neuron navigator 2b.
- Tight junction-associated protein 1
- Si:ch211-242b18.1.
- Rab effector MyRIP
Sequence:
MAVVLSTTSNMSKSLKKKSHWTNRVHEVVLSRGPSGDLGFELQGGAENGQFPVIGEVKPDRRKLQQDELLLEVNDTPVAGLTIRDVWAVVRHCKDPVRFKCVKQGGVVDKDLRQYLNLRFQKGSLDHELQQIIRDNLYLRTVPCTTRQPREGEVPGVDYNFVTVERFVELERSGALLESGTYEDNYYGTPKPPAEPSPLLLNVAEQLLPGATPTSQGKRRRNKSVSNMEKAGIEPPEEEEEERPVINGNGVAITPESSEHEDKSTDASGEMATTCPSETSTDAPKEDTEPPKSPPKPDENDELGPLPDNWEMAYTEKGEVYFIDHNTKTTSWLDPRLAKKAKPPEECKENELPYGWEKIDDPIYGTYYVDHINRRTQFENPVLEAKRRLQHQQQMQSQGLSSLPLPAVYREKPLFTRDPTQLKGSFLSTPLQKSNMGFGFTIIGGDEPDEFLQVKSVIPDGPAAQDGKMATGDVIVYINDVCVLGTTHADVVKLFQSVPIGQSVTLVLCRGYPLPYDPEDAANTLLSPLGLIDRPLLVNGRNSYDSYMEYISRTARFVDPLQTTMVQPHPGDTHLDAGPLEDSVSMASSGAAGGELLTINMVKGADGFGFTIADSNGGQRVKQILEAQGCPGLCEGDLIVEINQQPALTLSHTQVVELLKECPIGTEATLVIQRGGTGHFSPWKTTKQVLEHWDPLSSPTTSLSVHALPHSAPYLHWPSGPEFDLAKPDPYDLYEKSRAIYENRQPGLPRASLPADPSAEFQEVEVHLRRQKSGFGFRILGGEEPGQPVSPKAQEKILIGAIIEKSPADKDGRLRPGDELISVDGIVVAGKPHRYVIDLMHGAARTGQVKLTVRRRVQPTGEPFPENGRSPGSTQHSSPRSDFNSRMFCNNSAPSQNSAPSTTGSSPPDTAANQNAQPNDVSIQRKETEGFGFVIISSLNRPETAAAAAVPHKIGRIIEGSPADHCGKLKVGDRILAVNNQSIVNMPHADIVKLIKDAGLSVTLRIIPQEETNSTPSAGSSEKQSPMAQPSPVCQPNTVNQTGAAPLANSNAQQNSAPQPSPIKQPISEAQPSLVTQNSPANHPSSVTQQNPQTQPVQTYSHDSSYRSEVKARQDVKPDIRQPFTDYRQPPVDYRHPPVADYRQPPTLDYRHPPLLDYRPLPADPRTFPLPDYRMPQDFDFFTVELEKGMKGFGFSIRGGREYKMDLFVLRLAEDGPAIRNGRMRVGDQIIEINGESTRDMTHARAIELIKSGGRRVRLLLKRGTGQVPEYADSPAPWDAHPTASPSLSEVAPPLDSLSNPSASSHVNPPTDPPHTSSLEAVGPDSCQGPRGSESRALEQASVGKRSALAGGVGGGTKQREGSRTNRRSSGGKGQQQYLDEFAGEPKSHKSSRAKSKERRRERSSTPSRKRDSPKTSLTDTSMNGGNGCLDGSNSQQGPLVPFKALPKEPEKGQMSQESNPSHNSKISSAAGRKATVSPGPWKIPGTDKLPSTLRSATSTISR
Protein: Caytaxin (Q1M168)
Organism: Rattus norvegicus (Rat)
Function: Functions in the development of neural tissues, particularly the postnatal maturation of the cerebellar cortex. May play a role in neurotransmission through regulation of glutaminase/GLS, an enzyme responsible for the production in neurons of the glutamate neurotransmitter. Alternatively, may regulate the localization of mitochondria within axons and dendrites.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:19861499}. Cell projection, dendrite {ECO:0000269|PubMed:19861499}. Presynapse {ECO:0000269|PubMed:19861499}. Mitochondrion {ECO:0000269|PubMed:19861499}. Cell projection, growth cone {ECO:0000269|PubMed:19861499}. Cytoplasm {ECO:0000250|UniProtKB:Q86WG3}.
Interaction partners:
- Uracil phosphoribosyltransferase homolog.
Sequence:
MGTTEATLRMENVDVRDEWQDEDLPRPLPEDTGEDHLGGTVEDSSSPPSTLNLSGAHRKRKTLVAPEINISLDQSEGSLLSDDFLDTPDDLDINVDDIETPDETDSLEFLGNGNELEWEDDTPVATAKNMPGDSADLFGDGSGEDGSAANGRLWRTVIIGEQEHRIDLHMIRPYMKVVTHGGYYGEGLNAIIVFAACFLPDSSSPDYHYIMENLFLYVISSLELLVAEDYMIVYLNGATPRRRMPGIGWLKKCYHMIDRRLRKNLKSLIIVHPSWFIRTVLAISRPFISVKFISKIQYVHSLEELEQLIPMEHVQLPACVLQYEEQRLRAKRESARPPQPEFLLPRSEEKPETVEEEDRAAEVTEDQETSMS
Protein: Rab5 GDP/GTP exchange factor (Rabex-5) (Q9JM13)
Organism: Mus musculus (Mouse)
Function: Rab effector protein acting as linker between gamma-adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A (By similarity). Can act as a ubiquitin ligase (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}.
Interaction partners:
- Rab GTPase-binding effector protein 1
- Ras-related protein Rab-21
- Rab GTPase-binding effector protein 2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ras-related protein Rab-5A
- Early endosome antigen 1
- Ras-related protein Rab-5C
- Ras-related protein Rab-5B
- Ras-related protein Rab-20
- Ras-related protein Rab-22A
Sequence:
MSLKSERRGIHVDQSELLCKKGCGYYGNPAWQGFCSKCWREEYHKARQRQIQEDWELAERLQREEEEAFASSQSSQGAQSLTFSKFEEKKTNEKTRKVTTVKKFFSASSRAGSKKEIQEAKAPSPSINRQTSIETDRVTKEFIDFLKTFHKTGQEVYKQTKMFLEAMPYKRDLSIEEQSECTQDFYQNVAERMQTRGKVPPEKVEKIMDQIEKHIMTRLYKFVFCPETTDDEKKDLAIQKRIRALHWVTPQMLCVPVNEEIPEVSDMVVKAITDIIEMDSKRVPRDKLACITRCSKHIFNAIKITKNEPASADDFLPTLIYIVLKGNPPRLQSNIQYITRFCNPSRLMTGEDGYYFTNLCCAVAFIEKLDAQSLNLSQEDFDRYMSGQTSPRKQESESWPPEACLGVKQMYKNLDLLSQLNERQERIMNEAKKLEKDLIDWTDGIAKEVQDIVEKYPLEIKPPNQPLAAIDSENVENDKLPPPLQPQVYAG