A6NHR9 · SMHD1_HUMAN
- ProteinStructural maintenance of chromosomes flexible hinge domain-containing protein 1
- GeneSMCHD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2005 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Non-canonical member of the structural maintenance of chromosomes (SMC) protein family that plays a key role in epigenetic silencing by regulating chromatin architecture (By similarity).
Promotes heterochromatin formation in both autosomes and chromosome X, probably by mediating the merge of chromatin compartments (By similarity).
Plays a key role in chromosome X inactivation in females by promoting the spreading of heterochromatin (PubMed:23542155).
Recruited to inactivated chromosome X by Xist RNA and acts by mediating the merge of chromatin compartments: promotes random chromatin interactions that span the boundaries of existing structures, leading to create a compartment-less architecture typical of inactivated chromosome X (By similarity).
Required to facilitate Xist RNA spreading (By similarity).
Also required for silencing of a subset of clustered autosomal loci in somatic cells, such as the DUX4 locus (PubMed:23143600).
Has ATPase activity; may participate in structural manipulation of chromatin in an ATP-dependent manner as part of its role in gene expression regulation (PubMed:29748383).
Also plays a role in DNA repair: localizes to sites of DNA double-strand breaks in response to DNA damage to promote the repair of DNA double-strand breaks (PubMed:24790221, PubMed:25294876).
Acts by promoting non-homologous end joining (NHEJ) and inhibiting homologous recombination (HR) repair (PubMed:25294876).
Promotes heterochromatin formation in both autosomes and chromosome X, probably by mediating the merge of chromatin compartments (By similarity).
Plays a key role in chromosome X inactivation in females by promoting the spreading of heterochromatin (PubMed:23542155).
Recruited to inactivated chromosome X by Xist RNA and acts by mediating the merge of chromatin compartments: promotes random chromatin interactions that span the boundaries of existing structures, leading to create a compartment-less architecture typical of inactivated chromosome X (By similarity).
Required to facilitate Xist RNA spreading (By similarity).
Also required for silencing of a subset of clustered autosomal loci in somatic cells, such as the DUX4 locus (PubMed:23143600).
Has ATPase activity; may participate in structural manipulation of chromatin in an ATP-dependent manner as part of its role in gene expression regulation (PubMed:29748383).
Also plays a role in DNA repair: localizes to sites of DNA double-strand breaks in response to DNA damage to promote the repair of DNA double-strand breaks (PubMed:24790221, PubMed:25294876).
Acts by promoting non-homologous end joining (NHEJ) and inhibiting homologous recombination (HR) repair (PubMed:25294876).
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Barr body | |
Cellular Component | site of double-strand break | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | chromosome organization | |
Biological Process | dosage compensation by inactivation of X chromosome | |
Biological Process | double-strand break repair | |
Biological Process | negative regulation of double-strand break repair via homologous recombination | |
Biological Process | nose development | |
Biological Process | positive regulation of DNA repair | |
Biological Process | positive regulation of double-strand break repair via nonhomologous end joining |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStructural maintenance of chromosomes flexible hinge domain-containing protein 1
- EC number
- Short namesSMC hinge domain-containing protein 1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA6NHR9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Facioscapulohumeral muscular dystrophy 2, digenic (FSHD2)
- Note
- DescriptionA degenerative muscle disease characterized by slowly progressive weakness of the muscles of the face, upper-arm, and shoulder girdle. The onset of symptoms usually occurs in the first or second decade of life. Affected individuals usually present with impairment of upper extremity elevation. This tends to be followed by facial weakness, primarily involving the orbicularis oris and orbicularis oculi muscles.
- See alsoMIM:158901
Natural variants in FSHD2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_080698 | 110 | A>T | in FSHD2 | |
VAR_078877 | 137 | G>E | in BAMS and FSHD2; no change in protein abundance; strongly increased ATPase activity; dbSNP:rs1057519644 | |
VAR_078878 | 138-2005 | missing | in FSHD2 | |
VAR_078882 | 194 | L>F | in FSHD2; decreased ATPase activity | |
VAR_078883 | 195-2005 | missing | in FSHD2 | |
VAR_078885 | 263 | H>D | in FSHD2; decreased ATPase activity | |
VAR_080699 | 275 | missing | in FSHD2; uncertain significance; dbSNP:rs746679988 | |
VAR_080700 | 283 | Y>C | in FSHD2; does not affect ATPase activity; dbSNP:rs886041921 | |
VAR_078887 | 344-2005 | missing | in FSHD2 | |
VAR_069067 | 353 | Y>C | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein; abolished ATPase activity | |
VAR_078892 | 425 | G>R | in FSHD2 | |
VAR_078893 | 434-2005 | missing | in FSHD2 | |
VAR_080701 | 478 | G>E | in FSHD2; abolished ATPase activity | |
VAR_069068 | 479 | R>P | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein | |
VAR_069069 | 492 | C>R | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein | |
VAR_078898 | 527 | T>M | in FSHD2; decreased ATPase activity; dbSNP:rs397518422 | |
VAR_080702 | 615 | V>D | in FSHD2 | |
VAR_069070 | 690 | P>S | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein; decreased ATPase activity; dbSNP:rs397514623 | |
VAR_078900 | 716 | G>S | in FSHD2 | |
VAR_078901 | 731-2005 | missing | in FSHD2 | |
VAR_078902 | 748 | L>P | in FSHD2 | |
VAR_078903 | 780-2005 | missing | in FSHD2 | |
VAR_078904 | 849 | D>N | in FSHD2 | |
VAR_069071 | 868 | S>N | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein | |
VAR_078905 | 1176-1177 | TD>MH | in FSHD2 | |
VAR_080703 | 1449 | R>K | in FSHD2 | |
VAR_080704 | 1463 | Q>P | in FSHD2 | |
VAR_078906 | 1468 | M>I | in FSHD2 | |
VAR_080705 | 1485 | P>L | in FSHD2 | |
VAR_078907 | 1487-1488 | QP>HQ | in FSHD2 | |
VAR_069072 | 1554 | F>S | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein | |
VAR_080706 | 1663-2005 | missing | in FSHD2 | |
VAR_078908 | 1795-2005 | missing | in FSHD2 | |
VAR_078909 | 1868-2005 | missing | in FSHD2 |
Bosma arhinia microphthalmia syndrome (BAMS)
- Note
- DescriptionAn autosomal dominant syndrome characterized by severe hypoplasia of the nose, palatal abnormalities, hypoplasia of the eyes, sensory abnormalities of taste and smell, hypogonadotropic hypogonadism with cryptorchidism, and normal intelligence.
- See alsoMIM:603457
Natural variants in BAMS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078869 | 107 | L>P | in BAMS; no change in protein abundance; dbSNP:rs1135402737 | |
VAR_078870 | 129 | M>K | in BAMS; no change in protein abundance; dbSNP:rs1135402738 | |
VAR_078871 | 134 | A>S | in BAMS; has an increased ATPase activity | |
VAR_078872 | 135 | S>C | in BAMS; has an increased ATPase activity; no change in protein abundance; dbSNP:rs1057519645 | |
VAR_078873 | 135 | S>I | in BAMS; no change in protein abundance; dbSNP:rs1057519646 | |
VAR_078874 | 135 | S>N | in BAMS; no change in protein abundance; does not affect ATPase activity; dbSNP:rs1057519646 | |
VAR_078875 | 136 | E>D | in BAMS; no change in protein abundance; dbSNP:rs1057519643 | |
VAR_078876 | 136 | E>G | in BAMS; has an increased ATPase activity | |
VAR_078877 | 137 | G>E | in BAMS and FSHD2; no change in protein abundance; strongly increased ATPase activity; dbSNP:rs1057519644 | |
VAR_078879 | 139 | N>H | in BAMS; no change in protein abundance; dbSNP:rs1135402739 | |
VAR_078880 | 141 | L>F | in BAMS; no change in protein abundance; dbSNP:rs1057519641 | |
VAR_078881 | 171 | F>V | in BAMS; no change in protein abundance; dbSNP:rs1135402740 | |
VAR_078884 | 242 | A>G | in BAMS; no change in protein abundance; dbSNP:rs1135402741 | |
VAR_078886 | 342 | W>S | in BAMS; slightly decreased ATPase activity | |
VAR_078888 | 345 | Q>R | in BAMS; no change in protein abundance; dbSNP:rs1057519639 | |
VAR_078889 | 348 | H>R | in BAMS; no change in protein abundance; does not affect ATPase activity; dbSNP:rs1057519640 | |
VAR_078890 | 400 | Q>L | in BAMS; no change in protein abundance; dbSNP:rs1057519642 | |
VAR_078891 | 420 | D>V | in BAMS; no change in protein abundance; slightly decreased ATPase activity; dbSNP:rs1135402742 | |
VAR_078894 | 473 | E>Q | in BAMS; no change in protein abundance; slightly decreased ATPase activity; dbSNP:rs1135402743 | |
VAR_078895 | 518 | K>E | in BAMS; increased ATPase activity | |
VAR_078896 | 523 | T>K | in BAMS; no change in protein abundance; slightly decreased ATPase activity; dbSNP:rs1135402744 | |
VAR_078897 | 524 | N>S | in BAMS; no change in protein abundance; dbSNP:rs1135402745 | |
VAR_078899 | 552 | R>Q | in BAMS; no change in protein abundance; does not affect ATPase activity; dbSNP:rs886042392 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_078869 | 107 | in BAMS; no change in protein abundance; dbSNP:rs1135402737 | |||
Sequence: L → P | ||||||
Natural variant | VAR_080698 | 110 | in FSHD2 | |||
Sequence: A → T | ||||||
Natural variant | VAR_078870 | 129 | in BAMS; no change in protein abundance; dbSNP:rs1135402738 | |||
Sequence: M → K | ||||||
Natural variant | VAR_078871 | 134 | in BAMS; has an increased ATPase activity | |||
Sequence: A → S | ||||||
Natural variant | VAR_078872 | 135 | in BAMS; has an increased ATPase activity; no change in protein abundance; dbSNP:rs1057519645 | |||
Sequence: S → C | ||||||
Natural variant | VAR_078873 | 135 | in BAMS; no change in protein abundance; dbSNP:rs1057519646 | |||
Sequence: S → I | ||||||
Natural variant | VAR_078874 | 135 | in BAMS; no change in protein abundance; does not affect ATPase activity; dbSNP:rs1057519646 | |||
Sequence: S → N | ||||||
Natural variant | VAR_078875 | 136 | in BAMS; no change in protein abundance; dbSNP:rs1057519643 | |||
Sequence: E → D | ||||||
Natural variant | VAR_078876 | 136 | in BAMS; has an increased ATPase activity | |||
Sequence: E → G | ||||||
Natural variant | VAR_078877 | 137 | in BAMS and FSHD2; no change in protein abundance; strongly increased ATPase activity; dbSNP:rs1057519644 | |||
Sequence: G → E | ||||||
Natural variant | VAR_078878 | 138-2005 | in FSHD2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_078879 | 139 | in BAMS; no change in protein abundance; dbSNP:rs1135402739 | |||
Sequence: N → H | ||||||
Natural variant | VAR_078880 | 141 | in BAMS; no change in protein abundance; dbSNP:rs1057519641 | |||
Sequence: L → F | ||||||
Natural variant | VAR_078881 | 171 | in BAMS; no change in protein abundance; dbSNP:rs1135402740 | |||
Sequence: F → V | ||||||
Natural variant | VAR_078882 | 194 | in FSHD2; decreased ATPase activity | |||
Sequence: L → F | ||||||
Natural variant | VAR_078883 | 195-2005 | in FSHD2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_078884 | 242 | in BAMS; no change in protein abundance; dbSNP:rs1135402741 | |||
Sequence: A → G | ||||||
Natural variant | VAR_078885 | 263 | in FSHD2; decreased ATPase activity | |||
Sequence: H → D | ||||||
Natural variant | VAR_080699 | 275 | in FSHD2; uncertain significance; dbSNP:rs746679988 | |||
Sequence: Missing | ||||||
Natural variant | VAR_080700 | 283 | in FSHD2; does not affect ATPase activity; dbSNP:rs886041921 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_078886 | 342 | in BAMS; slightly decreased ATPase activity | |||
Sequence: W → S | ||||||
Natural variant | VAR_078887 | 344-2005 | in FSHD2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_078888 | 345 | in BAMS; no change in protein abundance; dbSNP:rs1057519639 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_078889 | 348 | in BAMS; no change in protein abundance; does not affect ATPase activity; dbSNP:rs1057519640 | |||
Sequence: H → R | ||||||
Natural variant | VAR_069067 | 353 | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein; abolished ATPase activity | |||
Sequence: Y → C | ||||||
Natural variant | VAR_078890 | 400 | in BAMS; no change in protein abundance; dbSNP:rs1057519642 | |||
Sequence: Q → L | ||||||
Natural variant | VAR_078891 | 420 | in BAMS; no change in protein abundance; slightly decreased ATPase activity; dbSNP:rs1135402742 | |||
Sequence: D → V | ||||||
Natural variant | VAR_078892 | 425 | in FSHD2 | |||
Sequence: G → R | ||||||
Natural variant | VAR_078893 | 434-2005 | in FSHD2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_078894 | 473 | in BAMS; no change in protein abundance; slightly decreased ATPase activity; dbSNP:rs1135402743 | |||
Sequence: E → Q | ||||||
Natural variant | VAR_080701 | 478 | in FSHD2; abolished ATPase activity | |||
Sequence: G → E | ||||||
Natural variant | VAR_069068 | 479 | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein | |||
Sequence: R → P | ||||||
Natural variant | VAR_069069 | 492 | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein | |||
Sequence: C → R | ||||||
Natural variant | VAR_078895 | 518 | in BAMS; increased ATPase activity | |||
Sequence: K → E | ||||||
Natural variant | VAR_078896 | 523 | in BAMS; no change in protein abundance; slightly decreased ATPase activity; dbSNP:rs1135402744 | |||
Sequence: T → K | ||||||
Natural variant | VAR_078897 | 524 | in BAMS; no change in protein abundance; dbSNP:rs1135402745 | |||
Sequence: N → S | ||||||
Natural variant | VAR_078898 | 527 | in FSHD2; decreased ATPase activity; dbSNP:rs397518422 | |||
Sequence: T → M | ||||||
Natural variant | VAR_078899 | 552 | in BAMS; no change in protein abundance; does not affect ATPase activity; dbSNP:rs886042392 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_080702 | 615 | in FSHD2 | |||
Sequence: V → D | ||||||
Natural variant | VAR_069070 | 690 | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein; decreased ATPase activity; dbSNP:rs397514623 | |||
Sequence: P → S | ||||||
Natural variant | VAR_042959 | 708 | in dbSNP:rs2276092 | |||
Sequence: V → I | ||||||
Natural variant | VAR_078900 | 716 | in FSHD2 | |||
Sequence: G → S | ||||||
Natural variant | VAR_078901 | 731-2005 | in FSHD2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_078902 | 748 | in FSHD2 | |||
Sequence: L → P | ||||||
Natural variant | VAR_078903 | 780-2005 | in FSHD2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_078904 | 849 | in FSHD2 | |||
Sequence: D → N | ||||||
Natural variant | VAR_069071 | 868 | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein | |||
Sequence: S → N | ||||||
Natural variant | VAR_042960 | 879 | in dbSNP:rs633422 | |||
Sequence: K → N | ||||||
Natural variant | VAR_051365 | 960 | in dbSNP:rs9961682 | |||
Sequence: I → V | ||||||
Natural variant | VAR_078905 | 1176-1177 | in FSHD2 | |||
Sequence: TD → MH | ||||||
Natural variant | VAR_080703 | 1449 | in FSHD2 | |||
Sequence: R → K | ||||||
Natural variant | VAR_080704 | 1463 | in FSHD2 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_078906 | 1468 | in FSHD2 | |||
Sequence: M → I | ||||||
Natural variant | VAR_080705 | 1485 | in FSHD2 | |||
Sequence: P → L | ||||||
Natural variant | VAR_078907 | 1487-1488 | in FSHD2 | |||
Sequence: QP → HQ | ||||||
Natural variant | VAR_069072 | 1554 | in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein | |||
Sequence: F → S | ||||||
Natural variant | VAR_080706 | 1663-2005 | in FSHD2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_078908 | 1795-2005 | in FSHD2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_078909 | 1868-2005 | in FSHD2 | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,894 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000332144 | 2-2005 | UniProt | Structural maintenance of chromosomes flexible hinge domain-containing protein 1 | |||
Sequence: AAADGGGPGGASVGTEEDGGGVGHRTVYLFDRREKESELGDRPLQVGERSDYAGFRACVCQTLGISPEEKFVITTTSRKEITCDNFDETVKDGVTLYLLQSVNQLLLTATKERIDFLPHYDTLVKSGMYEYYASEGQNPLPFALAELIDNSLSATSRNIGVRRIQIKLLFDETQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTRQGDFESDHSGYVRPVPVPRSLNSDISYFGVGGKQAVFFVGQSARMISKPADSQDVHELVLSKEDFEKKEKNKEAIYSGYIRNRKPSDSVHITNDDERFLHHLIIEEKEKDSFTAVVITGVQPEHIQYLKNYFHLWTRQLAHIYHYYIHGPKGNEIRTSKEVEPFNNIDIEISMFEKGKVPKIVNLREIQDDMQTLYVNTAADSFEFKAHVEGDGVVEGIIRYHPFLYDRETYPDDPCFPSKLKDEDDEDDCFILEKAARGKRPIFECFWNGRLIPYTSVEDFDWCTPPKKRGLAPIECYNRISGALFTNDKFQVSTNKLTFMDLELKLKDKNTLFTRILNGQEQRMKIDREFALWLKDCHEKYDKQIKFTLFKGVITRPDLPSKKQGPWATYAAIEWDGKIYKAGQLVKTIKTLPLFYGSIVRFFLYGDHDGEVYATGGEVQIAMEPQALYDEVRTVPIAKLDRTVAEKAVKKYVEDEMARLPDRLSVTWPEGDELLPNEVRPAGTPIGALRIEILNKKGEAMQKLPGTSHGGSKKLLVELKVILHSSSGNKEIISHISQHGGKWPYWFKKMENIQKLGNYTLKLQVVLNESNADTYAGRPLPSKAIKFSVKEGKPEKFSFGLLDLPFRVGVPFNIPLEFQDEFGHTSQLVTDIQPVLEASGLSLHYEEITKGPNCVIRGVTAKGPVNSCQGKNYNLKVTLPGLKEDSQILKIRLLPGHPRRLKVKPDSEILVIENGTAFPFQVEVLDESDNITAQPKLIVHCKFSGAPNLPVYVVDCSSSGTSILTGSAIQVQNIKKDQTLKARIEIPSCKDVAPVEKTIKLLPSSHVARLQIFSVEGQKAIQIKHQDEVNWIAGDIMHNLIFQMYDEGEREINITSALAEKIKVNWTPEINKEHLLQGLLPDVQVPTSVKDMRYCQVSFQDDHVSLESAFTVRPLPDEPKHLKCEMKGGKTVQMGQELQGEVVIIITDQYGNQIQAFSPSSLSSLSIAGVGLDSSNLKTTFQENTQSISVRGIKFIPGPPGNKDLCFTWREFSDFIRVQLISGPPAKLLLIDWPELKESIPVINGRDLQNPIIVQLCDQWDNPAPVQHVKISLTKASNLKLMPSNQQHKTDEKGRANLGVFSVFAPRGEHTLQVKAIYNKSIIEGPIIKLMILPDPEKPVRLNVKYDKDASFLAGGLFTDFMISVISEDDSIIKNINPARISMKMWKLSTSGNRPPANAETFSCNKIKDNDKEDGCFYFRDKVIPNKVGTYCIQFGFMMDKTNILNSEQVIVEVLPNQPVKLVPKIKPPTPAVSNVRSVASRTLVRDLHLSITDDYDNHTGIDLVGTIIATIKGSNEEDTDTPLFIGKVRTLEFPFVNGSAEIMSLVLAESSPGRDSTEYFIVFEPRLPLLSRTLEPYILPFMFYNDVKKQQQMAALTKEKDQLSQSIVMYKSLFEASQQLLNEMKCQVEEARLKEAQLRNELKIHNIDIPTTQQVPHIEALLKRKLSEQEELKKKPRRSCTLPNYTKGSGDVLGKIAHLAQIEDDRAAMVISWHLASDMDCVVTLTTDAARRIYDETQGRQQVLPLDSIYKKTLPDWKRSLPHFRNGKLYFKPIGDPVFARDLLTFPDNVEHCETVFGMLLGDTIILDNLDAANHYRKEVVKITHCPTLLTRDGDRIRSNGKFGGLQNKAPPMDKLRGMVFGAPVPKQCLILGEQIDLLQQYRSAVCKLDSVNKDLNSQLEYLRTPDMRKKKQELDEHEKNLKLIEEKLGMTPIRKCNDSLRHSPKVETTDCPVPPKRMRREATRQNRIITKTDV | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 67 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 293 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 756 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1349 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 1374 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1496 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1499 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1697 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1709 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1802 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 1974 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1974 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Sumoylated with SUMO1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer; homodimerizes via its SMC hinge domain (By similarity).
Interacts with LRIF1 (PubMed:23542155).
Interacts with LRIF1 (PubMed:23542155).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | A6NHR9 | LRIF1 Q5T3J3 | 9 | EBI-2801919, EBI-473196 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-23 | Disordered | ||||
Sequence: MAAADGGGPGGASVGTEEDGGGV | ||||||
Region | 111-702 | ATPase activity domain | ||||
Sequence: TKERIDFLPHYDTLVKSGMYEYYASEGQNPLPFALAELIDNSLSATSRNIGVRRIQIKLLFDETQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTRQGDFESDHSGYVRPVPVPRSLNSDISYFGVGGKQAVFFVGQSARMISKPADSQDVHELVLSKEDFEKKEKNKEAIYSGYIRNRKPSDSVHITNDDERFLHHLIIEEKEKDSFTAVVITGVQPEHIQYLKNYFHLWTRQLAHIYHYYIHGPKGNEIRTSKEVEPFNNIDIEISMFEKGKVPKIVNLREIQDDMQTLYVNTAADSFEFKAHVEGDGVVEGIIRYHPFLYDRETYPDDPCFPSKLKDEDDEDDCFILEKAARGKRPIFECFWNGRLIPYTSVEDFDWCTPPKKRGLAPIECYNRISGALFTNDKFQVSTNKLTFMDLELKLKDKNTLFTRILNGQEQRMKIDREFALWLKDCHEKYDKQIKFTLFKGVITRPDLPSKKQGPWATYAAIEWDGKIYKAGQLVKTIKTLPLFYGSIVRFFLYGDHDGEVYATGGEVQIAMEPQALYDEVRTVPIAKLDRTVAEKAVKKYVEDEMARLPDRLSVTWPEGDE | ||||||
Domain | 1720-1847 | SMC hinge | ||||
Sequence: GDVLGKIAHLAQIEDDRAAMVISWHLASDMDCVVTLTTDAARRIYDETQGRQQVLPLDSIYKKTLPDWKRSLPHFRNGKLYFKPIGDPVFARDLLTFPDNVEHCETVFGMLLGDTIILDNLDAANHYR |
Domain
Atypical member of the structural maintenance of chromosomes (SMC) protein family. Like other members of the SMC family, has ATPase activity, which is probably necessary for its engagement with chromatin, and a SMC hinge domain. However, the SMC hinge domain adopts an unconventional homodimeric arrangement augmented by an intermolecular coiled coil formed between the two monomers. This suggests that protein may assemble as a head-to-head parallel dimer without adopting a hairpin shape at the hinge domain, unlike the dimeric arrangement conventionally found in other members of the SMC protein family. The SMC hinge domain binds DNA and RNA.
Sequence similarities
Belongs to the SMC family. Highly divergent.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
A6NHR9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length2,005
- Mass (Da)226,374
- Last updated2008-04-29 v2
- ChecksumB662C681424241B7
A6NHR9-2
- Name2
- Differences from canonical
- 1907-1917: DLLQQYRSAVC → VHACVPSYSGG
- 1918-2005: Missing
A6NHR9-3
- Name3
- Differences from canonical
- 1-1065: Missing
- 1826-1827: VF → GC
- 1828-2005: Missing
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3KRK8 | J3KRK8_HUMAN | SMCHD1 | 49 | ||
J3KTL8 | J3KTL8_HUMAN | SMCHD1 | 1388 | ||
A0A2R8YE92 | A0A2R8YE92_HUMAN | SMCHD1 | 212 | ||
A0A2R8YCU7 | A0A2R8YCU7_HUMAN | SMCHD1 | 308 | ||
A0A8I5KRS9 | A0A8I5KRS9_HUMAN | SMCHD1 | 1961 | ||
A0A8I5KQZ7 | A0A8I5KQZ7_HUMAN | SMCHD1 | 385 | ||
A0A8I5KW02 | A0A8I5KW02_HUMAN | SMCHD1 | 748 | ||
J3QSH1 | J3QSH1_HUMAN | SMCHD1 | 150 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_033344 | 1-1065 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 1278 | in Ref. 3; CAB45732 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 1384 | in Ref. 3; CAH10538 | ||||
Sequence: G → E | ||||||
Alternative sequence | VSP_033345 | 1826-1827 | in isoform 3 | |||
Sequence: VF → GC | ||||||
Alternative sequence | VSP_033346 | 1828-2005 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_033347 | 1907-1917 | in isoform 2 | |||
Sequence: DLLQQYRSAVC → VHACVPSYSGG | ||||||
Alternative sequence | VSP_033348 | 1918-2005 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK025646 EMBL· GenBank· DDBJ | BAB15202.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK126324 EMBL· GenBank· DDBJ | BAC86525.1 EMBL· GenBank· DDBJ | mRNA | ||
AP001011 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP005061 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL080138 EMBL· GenBank· DDBJ | CAB45732.1 EMBL· GenBank· DDBJ | mRNA | ||
CR627458 EMBL· GenBank· DDBJ | CAH10538.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB014550 EMBL· GenBank· DDBJ | BAA31625.1 EMBL· GenBank· DDBJ | mRNA | ||
BC035774 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |