Miscellaneous transport and binding events (Homo sapiens)

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3, 131, 9, 22, 23, 272647, 1115, 19, 252, 5, 10, 20, 21186, 12, 17, 246, 12, 17, 248, 2614, 16cytosolmitochondrial matrixlysosomal lumenGolgi lumenMAGT1ADD1:ADD3:DMTNCaPO4H+Mg2+CSN polymer:CaPO4CaPO4 ADD3(2-706) DMTN H+ADD2 Mg2+NIPAsMg2+CSN polymerPPiDMTN ADD1:ADD2:DMTNPIPCTNSADD1:ADD3PPiADD1 CySS-ANKHADD1 ADD3(2-706) Mg2+AZGP1 CySS-PIP ADD2 AZGP1:PIPAZGP1MMGT1ADD1:ADD2DMTNTUSC3(1-348)ADD1 ADD1 MRS2


Description

This section contains known transport and binding events that as of yet cannot be placed in exisiting pathways (Purves 2001, He et al. 2009, Rees et al. 2009). Source:Reactome.

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Bibliography

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  1. Rasmussen LK, Due HA, Petersen TE.; ''Human alpha s1-casein: purification and characterization.''; PubMed Europe PMC Scholia
  2. Goytain A, Quamme GA.; ''Identification and characterization of a novel family of membrane magnesium transporters, MMgT1 and MMgT2.''; PubMed Europe PMC Scholia
  3. Khan AA, Hanada T, Mohseni M, Jeong JJ, Zeng L, Gaetani M, Li D, Reed BC, Speicher DW, Chishti AH.; ''Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1.''; PubMed Europe PMC Scholia
  4. Brignon G, Chtourou A, Ribadeau-Dumas B.; ''Preparation and amino acid sequence of human kappa-casein.''; PubMed Europe PMC Scholia
  5. Goytain A, Hines RM, El-Husseini A, Quamme GA.; ''NIPA1(SPG6), the basis for autosomal dominant form of hereditary spastic paraplegia, encodes a functional Mg2+ transporter.''; PubMed Europe PMC Scholia
  6. Goytain A, Quamme GA.; ''Identification and characterization of a novel mammalian Mg2+ transporter with channel-like properties.''; PubMed Europe PMC Scholia
  7. Town M, Jean G, Cherqui S, Attard M, Forestier L, Whitmore SA, Callen DF, Gribouval O, Broyer M, Bates GP, van't Hoff W, Antignac C.; ''A novel gene encoding an integral membrane protein is mutated in nephropathic cystinosis.''; PubMed Europe PMC Scholia
  8. Christianson JC, Olzmann JA, Shaler TA, Sowa ME, Bennett EJ, Richter CM, Tyler RE, Greenblatt EJ, Harper JW, Kopito RR.; ''Defining human ERAD networks through an integrative mapping strategy.''; PubMed Europe PMC Scholia
  9. Williams CJ, Zhang Y, Timms A, Bonavita G, Caeiro F, Broxholme J, Cuthbertson J, Jones Y, Marchegiani R, Reginato A, Russell RG, Wordsworth BP, Carr AJ, Brown MA.; ''Autosomal dominant familial calcium pyrophosphate dihydrate deposition disease is caused by mutation in the transmembrane protein ANKH.''; PubMed Europe PMC Scholia
  10. Myal Y, Robinson DB, Iwasiow B, Tsuyuki D, Wong P, Shiu RP.; ''The prolactin-inducible protein (PIP/GCDFP-15) gene: cloning, structure and regulation.''; PubMed Europe PMC Scholia
  11. Rees DC, Johnson E, Lewinson O.; ''ABC transporters: the power to change.''; PubMed Europe PMC Scholia
  12. He L, Vasiliou K, Nebert DW.; ''Analysis and update of the human solute carrier (SLC) gene superfamily.''; PubMed Europe PMC Scholia
  13. Syeda R, Qiu Z, Dubin AE, Murthy SE, Florendo MN, Mason DE, Mathur J, Cahalan SM, Peters EC, Montal M, Patapoutian A.; ''LRRC8 Proteins Form Volume-Regulated Anion Channels that Sense Ionic Strength.''; PubMed Europe PMC Scholia
  14. Zsurka G, Gregán J, Schweyen RJ.; ''The human mitochondrial Mrs2 protein functionally substitutes for its yeast homologue, a candidate magnesium transporter.''; PubMed Europe PMC Scholia
  15. Debily MA, Marhomy SE, Boulanger V, Eveno E, Mariage-Samson R, Camarca A, Auffray C, Piatier-Tonneau D, Imbeaud S.; ''A functional and regulatory network associated with PIP expression in human breast cancer.''; PubMed Europe PMC Scholia
  16. Russell ST, Russell ST, Zimmerman TP, Domin BA, Tisdale MJ.; ''Induction of lipolysis in vitro and loss of body fat in vivo by zinc-alpha2-glycoprotein.''; PubMed Europe PMC Scholia
  17. Azim AC, Knoll JH, Beggs AH, Chishti AH.; ''Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily.''; PubMed Europe PMC Scholia
  18. Sánchez LM, López-Otín C, Bjorkman PJ.; ''Biochemical characterization and crystalization of human Zn-alpha2-glycoprotein, a soluble class I major histocompatibility complex homolog.''; PubMed Europe PMC Scholia
  19. Hassan MI, Bilgrami S, Kumar V, Singh N, Yadav S, Kaur P, Singh TP.; ''Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal plasma.''; PubMed Europe PMC Scholia
  20. Elmonem MA, Veys KR, Soliman NA, van Dyck M, van den Heuvel LP, Levtchenko E.; ''Cystinosis: a review.''; PubMed Europe PMC Scholia
  21. Chiaverini C, Sillard L, Flori E, Ito S, Briganti S, Wakamatsu K, Fontas E, Berard E, Cailliez M, Cochat P, Foulard M, Guest G, Niaudet P, Picardo M, Bernard FX, Antignac C, Ortonne JP, Ballotti R.; ''Cystinosin is a melanosomal protein that regulates melanin synthesis.''; PubMed Europe PMC Scholia
  22. Citterio L, Tizzoni L, Catalano M, Zerbini G, Bianchi G, Barlassina C.; ''Expression analysis of the human adducin gene family and evidence of ADD2 beta4 multiple splicing variants.''; PubMed Europe PMC Scholia
  23. Johnsen LB, Rasmussen LK, Petersen TE, Berglund L.; ''Characterization of three types of human alpha s1-casein mRNA transcripts.''; PubMed Europe PMC Scholia
  24. Jézégou A, Llinares E, Anne C, Kieffer-Jaquinod S, O'Regan S, Aupetit J, Chabli A, Sagné C, Debacker C, Chadefaux-Vekemans B, Journet A, André B, Gasnier B.; ''Heptahelical protein PQLC2 is a lysosomal cationic amino acid exporter underlying the action of cysteamine in cystinosis therapy.''; PubMed Europe PMC Scholia
  25. Voss FK, Ullrich F, Münch J, Lazarow K, Lutter D, Mah N, Andrade-Navarro MA, von Kries JP, Stauber T, Jentsch TJ.; ''Identification of LRRC8 heteromers as an essential component of the volume-regulated anion channel VRAC.''; PubMed Europe PMC Scholia
  26. Qiu Z, Dubin AE, Mathur J, Tu B, Reddy K, Miraglia LJ, Reinhardt J, Orth AP, Patapoutian A.; ''SWELL1, a plasma membrane protein, is an essential component of volume-regulated anion channel.''; PubMed Europe PMC Scholia
  27. Williams CJ, Pendleton A, Bonavita G, Reginato AJ, Hughes AE, Peariso S, Doherty M, McCarty DJ, Ryan LM.; ''Mutations in the amino terminus of ANKH in two US families with calcium pyrophosphate dihydrate crystal deposition disease.''; PubMed Europe PMC Scholia
  28. Nürnberg P, Thiele H, Chandler D, Höhne W, Cunningham ML, Ritter H, Leschik G, Uhlmann K, Mischung C, Harrop K, Goldblatt J, Borochowitz ZU, Kotzot D, Westermann F, Mundlos S, Braun HS, Laing N, Tinschert S.; ''Heterozygous mutations in ANKH, the human ortholog of the mouse progressive ankylosis gene, result in craniometaphyseal dysplasia.''; PubMed Europe PMC Scholia
  29. Zhou H, Clapham DE.; ''Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and vertebrate embryonic development.''; PubMed Europe PMC Scholia
  30. Mongin AA.; ''Volume-regulated anion channel--a frenemy within the brain.''; PubMed Europe PMC Scholia
  31. Anikster Y, Shotelersuk V, Gahl WA.; ''CTNS mutations in patients with cystinosis.''; PubMed Europe PMC Scholia
  32. Joshi R, Gilligan DM, Otto E, McLaughlin T, Bennett V.; ''Primary structure and domain organization of human alpha and beta adducin.''; PubMed Europe PMC Scholia
  33. Reichenberger E, Tiziani V, Watanabe S, Park L, Ueki Y, Santanna C, Baur ST, Shiang R, Grange DK, Beighton P, Gardner J, Hamersma H, Sellars S, Ramesar R, Lidral AC, Sommer A, Raposo do Amaral CM, Gorlin RJ, Mulliken JB, Olsen BR.; ''Autosomal dominant craniometaphyseal dysplasia is caused by mutations in the transmembrane protein ANK.''; PubMed Europe PMC Scholia
  34. Pendleton A, Johnson MD, Hughes A, Gurley KA, Ho AM, Doherty M, Dixey J, Gillet P, Loeuille D, McGrath R, Reginato A, Shiang R, Wright G, Netter P, Williams C, Kingsley DM.; ''Mutations in ANKH cause chondrocalcinosis.''; PubMed Europe PMC Scholia
  35. Jentsch TJ, Lutter D, Planells-Cases R, Ullrich F, Voss FK.; ''VRAC: molecular identification as LRRC8 heteromers with differential functions.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
114650view16:11, 25 January 2021ReactomeTeamReactome version 75
113098view11:16, 2 November 2020ReactomeTeamReactome version 74
112332view15:25, 9 October 2020ReactomeTeamReactome version 73
101231view11:12, 1 November 2018ReactomeTeamreactome version 66
100769view20:39, 31 October 2018ReactomeTeamreactome version 65
100313view19:16, 31 October 2018ReactomeTeamreactome version 64
99859view15:59, 31 October 2018ReactomeTeamreactome version 63
99416view14:35, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99100view12:39, 31 October 2018ReactomeTeamreactome version 62
93843view13:40, 16 August 2017ReactomeTeamreactome version 61
93399view11:22, 9 August 2017ReactomeTeamreactome version 61
87935view13:03, 25 July 2016RyanmillerOntology Term : 'transport pathway' added !
87932view13:03, 25 July 2016RyanmillerOntology Term : 'regulatory pathway' added !
86484view09:19, 11 July 2016ReactomeTeamreactome version 56
83279view10:37, 18 November 2015ReactomeTeamVersion54
81397view12:55, 21 August 2015ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
ADD1 ProteinP35611 (Uniprot-TrEMBL)
ADD1:ADD2:DMTNComplexR-HSA-5226996 (Reactome)
ADD1:ADD2ComplexR-HSA-420433 (Reactome)
ADD1:ADD3:DMTNComplexR-HSA-5226961 (Reactome)
ADD1:ADD3ComplexR-HSA-5227016 (Reactome)
ADD2 ProteinP35612 (Uniprot-TrEMBL)
ADD3(2-706) ProteinQ9UEY8 (Uniprot-TrEMBL)
ANKHProteinQ9HCJ1 (Uniprot-TrEMBL)
AZGP1 ProteinP25311 (Uniprot-TrEMBL)
AZGP1:PIPComplexR-HSA-5251992 (Reactome)
AZGP1ProteinP25311 (Uniprot-TrEMBL)
CSN polymer:CaPO4ComplexR-HSA-5340155 (Reactome)
CSN polymerR-HSA-5340146 (Reactome)
CTNSProteinO60931 (Uniprot-TrEMBL)
CaPO4 MetaboliteCHEBI:77635 (ChEBI)
CaPO4MetaboliteCHEBI:77635 (ChEBI)
CySS-MetaboliteCHEBI:16283 (ChEBI)
DMTN ProteinQ08495 (Uniprot-TrEMBL)
DMTNProteinQ08495 (Uniprot-TrEMBL)
H+MetaboliteCHEBI:15378 (ChEBI)
MAGT1ProteinQ9H0U3 (Uniprot-TrEMBL)
MMGT1ProteinQ8N4V1 (Uniprot-TrEMBL)
MRS2ProteinQ9HD23 (Uniprot-TrEMBL)
Mg2+MetaboliteCHEBI:18420 (ChEBI)
NIPAsR-HSA-5336426 (Reactome)
PIP ProteinP12273 (Uniprot-TrEMBL)
PIPProteinP12273 (Uniprot-TrEMBL)
PPiMetaboliteCHEBI:29888 (ChEBI)
TUSC3(1-348)ProteinQ13454 (Uniprot-TrEMBL)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
ADD1:ADD2:DMTNArrowR-HSA-5226979 (Reactome)
ADD1:ADD2R-HSA-5226979 (Reactome)
ADD1:ADD3:DMTNArrowR-HSA-5226999 (Reactome)
ADD1:ADD3R-HSA-5226999 (Reactome)
ANKHmim-catalysisR-HSA-5226964 (Reactome)
AZGP1:PIPArrowR-HSA-5252072 (Reactome)
AZGP1R-HSA-5252072 (Reactome)
CSN polymer:CaPO4ArrowR-HSA-5340124 (Reactome)
CSN polymerR-HSA-5340124 (Reactome)
CTNSmim-catalysisR-HSA-5340130 (Reactome)
CaPO4R-HSA-5340124 (Reactome)
CySS-ArrowR-HSA-5340130 (Reactome)
CySS-R-HSA-5340130 (Reactome)
DMTNR-HSA-5226979 (Reactome)
DMTNR-HSA-5226999 (Reactome)
H+ArrowR-HSA-5340130 (Reactome)
H+R-HSA-5340130 (Reactome)
MAGT1mim-catalysisR-HSA-5339538 (Reactome)
MMGT1mim-catalysisR-HSA-5336454 (Reactome)
MRS2mim-catalysisR-HSA-5336466 (Reactome)
Mg2+ArrowR-HSA-5336453 (Reactome)
Mg2+ArrowR-HSA-5336454 (Reactome)
Mg2+ArrowR-HSA-5336466 (Reactome)
Mg2+ArrowR-HSA-5339528 (Reactome)
Mg2+ArrowR-HSA-5339538 (Reactome)
Mg2+R-HSA-5336453 (Reactome)
Mg2+R-HSA-5336454 (Reactome)
Mg2+R-HSA-5336466 (Reactome)
Mg2+R-HSA-5339528 (Reactome)
Mg2+R-HSA-5339538 (Reactome)
NIPAsmim-catalysisR-HSA-5336453 (Reactome)
PIPR-HSA-5252072 (Reactome)
PPiArrowR-HSA-5226964 (Reactome)
PPiR-HSA-5226964 (Reactome)
R-HSA-5226964 (Reactome) Progressive ankylosis protein homolog (ANKH) is a putative transmembrane pyrophosphate (PPi) transport channel protein found in osteoblasts of various bones. It mediates the transport of cytosolic PPi to the extracellular matrix. Abnormal transport of PPi is implicated in familial calcium pyrophosphate dihydrate deposition (CPPD) disease. There are two forms of CPPD disease: CCAL1 and CCAL2. Defects in ANKH can cause chondrocalcinosis (CCAL2; MIM:118600), a chronic condition in which PPi crystals deposit in the joint fluid, cartilage, and periarticular tissues and there is calcium deposition in articular cartilage (Pendleton et al. 2002, Williams et al. 2002, Williams et al. 2003). Defects in ANKH can also cause craniometaphyseal dysplasia, autosomal dominant (CMDD; MIM:123000), an osteochondrodysplasia characterised by progressive thickening and increased mineral density of craniofacial bones and abnormal modelling of metaphyses in long bones (Nurnberg et al. 2001, Reichenberger et al. 2001).
R-HSA-5226979 (Reactome) Alpha-adducin (ADD1 aka ADDA) (Joshi et al. 1991) is a ubiquitously expressed, membrane-cytoskeletal protein that can promote the assembly of the spectrin-actin network. It is functional in a heterodimeric form, in complex with either a beta (ADD2 aka ADDB) (Khan et al. 2008) or a gamma (ADD3 aka ADDL) subunit (Citterio et al. 2003). Either complex is able to bind dematin (DMTN) (Azim et al. 1995), a membrane-cytoskeletal protein that can induce F-actin bundles formation and stabilization. It can also bind the erythrocyte membrane glucose transporter 1 (SLC2A1 aka GLUT1), and hence stabilise the spectrin-actin network to the erythrocytic plasma membrane (Khan et al. 2008).
R-HSA-5226999 (Reactome) Alpha-adducin (ADD1 aka ADDA) (Joshi et al. 1991) is a ubiquitously expressed, membrane-cytoskeletal protein that can promote the assembly of the spectrin-actin network. It is functional in a heterodimeric form, in complex with either a beta (ADD2 aka ADDB) (Khan et al. 2008) or a gamma (ADD3 aka ADDL) subunit (Citterio et al. 2003). Either complex is able to bind dematin (DMTN) (Azim et al. 1995), a membrane-cytoskeletal protein that can induce F-actin bundles formation and stabilization. It can also bind the erythrocyte membrane glucose transporter 1 (SLC2A1 aka GLUT1), and hence stabilise the spectrin-actin network to the erythrocytic plasma membrane (Khan et al. 2008).
R-HSA-5252072 (Reactome) Zinc-alpha-2-glycoprotein (AZGP1) (Sanchez et al. 1997), a 41 kDa protein secreted in many bodily fluids, is thought to stimulate lipolysis and be the cause of the excessive fat loss seen in cancer cachexia (Russell et al. 2004). AZGP1 is able to bind prolactin-inducible protein (PIP) (Myal et al. 1991), another secreted protein overexpressed in certain breast cancers (Hassan et al. 2008, Debily et al. 2009).
R-HSA-5336453 (Reactome) Magnesium (Mg2+) is required for the catalytic activity of numerous metalloenzymes within a variety of subcellular organelles. Magnesium transporters NIPA1, 2, 3, 4 (NIPA1,2,3,4) and NIPA-like proteins 2 and 2 (NIPAL2 and 3) can act as Mg2+ transporters. They may also transport other divalent cations such as Fe2+, Mn2+ and Ba2+ but to a lesser extent than Mg2+. Human NIPA1 mediates Mg2+ uptake when expressed in Xenopus oocytes (Goytain et al. 2007). The other NIPA members are included as candidates based on NIPA1 function.
R-HSA-5336454 (Reactome) Magnesium (Mg2+) is required for the catalytic activity of numerous metalloenzymes within a variety of subcellular organelles. Membrane magnesium transporter 1 (MMGT1) mediates the uptake of Mg2+ across the Golgi membrane. The human MMGT1 function is inferred from mouse experiments using the orthologous Mmgt1 and 2 (Goytain & Quamme 2008). MMGT1 is also found on the ER membrane as a component of the ER membrane protein complex (EMC) which functions to degrade incorrectly folded or assembled proteins by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). MMGT1 is not implicated in this function of protein quality control (Christianson et al. 2011).
R-HSA-5336466 (Reactome) Magnesium (Mg2+) is required for the catalytic activity of numerous metalloenzymes within a variety of subcellular organelles. Magnesium transporter MRS2 homolog, mitochondrial (MRS2) mediates the influx of Mg2+ into the mitochondrial matrix (Zsurka et al. 2001). MRS2 is located on the inner mitochondrial membrane and its expression in yeast with a Mrs2-1 knock-out mutant partly restores mitochondrial magnesium concentrations that are otherwise much reduced (Zsurka et al. 2001).
R-HSA-5339528 (Reactome) Magnesium (Mg2+) is required for the catalytic activity of numerous metalloenzymes within a variety of subcellular organelles. Tumor suppressor candidate 3 (TUSC3) is expressed in most non-lymphoid cells and tissues and is an essential protein in Mg2+ uptake into cells (Zhou & Clapham 2009).
R-HSA-5339538 (Reactome) Magnesium (Mg2+) is required for the catalytic activity of numerous metalloenzymes within a variety of subcellular organelles. Magnesium transporter protein 1 (MAGT1) is ubiquitously expressed in all human tissues and is upregulated by low Mg2+ concentrations. It is an essential protein in Mg2+ uptake into cells (Zhou & Clapham 2009, Goytain & Quamme 2005).
R-HSA-5340124 (Reactome) In milk, caseins (CSNs) interact with calcium phosphate (CaPO4), forming large stable colloidal particles called micelles. These micelles make it possible to maintain a supersaturated CaPO4 concentration in milk, providing the newborn with sufficient calcium phosphate for the mineralisation of calcified tissues. Human alpha-S1-casein (CSN1S1) is able to bind CaPO4 in milk. CSN1S1 forms a disulfide cross-linked heteropolymer with kappa-casein (CSN3), another CSN that is thought to stabilise micelle formation and thus preventing casein precipitation in milk (Brignon et al. 1985, Rasmussen et al. 1995, Johnson et al. 1995).
R-HSA-5340130 (Reactome) Cystinosin (CTNS) is an integral lysosomal membrane protein which can transport L-cystine (CySS-, the oxidative product of two cysteine molecules linked via a disulfide bond) together with H+ out of lysosomes. Defects in CTNS cause cystinosis, lysosomal storage-type diseases due to defective transport of CySS- across the lysosomal membrane (Town et al. 1998, Anikster et al. 1999).
TUSC3(1-348)mim-catalysisR-HSA-5339528 (Reactome)
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