Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Radical S-adenosyl methionine domain-containing protein 1, mitochondrial

Gene

RSAD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May be involved in porphyrin cofactor biosynthesis.By similarity

Cofactori

[4Fe-4S] clusterCuratedNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431S-adenosyl-L-methionine 1By similarity
Metal bindingi49 – 491Iron-sulfur (4Fe-4S-S-AdoMet)Sequence analysis
Metal bindingi53 – 531Iron-sulfur (4Fe-4S-S-AdoMet)Sequence analysis
Binding sitei55 – 551S-adenosyl-L-methionine 2; via carbonyl oxygenBy similarity
Metal bindingi56 – 561Iron-sulfur (4Fe-4S-S-AdoMet)Sequence analysis
Binding sitei98 – 981S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei131 – 1311S-adenosyl-L-methionine 1By similarity
Binding sitei158 – 1581S-adenosyl-L-methionine 2By similarity
Binding sitei170 – 1701S-adenosyl-L-methionine 2By similarity
Binding sitei195 – 1951S-adenosyl-L-methionine 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Radical S-adenosyl methionine domain-containing protein 1, mitochondrial (EC:1.3.99.-)
Alternative name(s):
Oxygen-independent coproporphyrinogen-III oxidase-like protein RSAD1
Gene namesi
Name:RSAD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:25634. RSAD1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134945325.

Polymorphism and mutation databases

BioMutaiRSAD1.
DMDMi145566941.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1717MitochondrionSequence analysisAdd
BLAST
Chaini18 – 442425Radical S-adenosyl methionine domain-containing protein 1, mitochondrialPRO_0000284609Add
BLAST

Proteomic databases

EPDiQ9HA92.
MaxQBiQ9HA92.
PaxDbiQ9HA92.
PeptideAtlasiQ9HA92.
PRIDEiQ9HA92.

PTM databases

iPTMnetiQ9HA92.

Expressioni

Gene expression databases

BgeeiQ9HA92.
CleanExiHS_RSAD1.
ExpressionAtlasiQ9HA92. baseline and differential.
GenevisibleiQ9HA92. HS.

Organism-specific databases

HPAiHPA022436.
HPA022967.

Interactioni

Protein-protein interaction databases

BioGridi120598. 10 interactions.
IntActiQ9HA92. 1 interaction.
STRINGi9606.ENSP00000258955.

Structurei

3D structure databases

ProteinModelPortaliQ9HA92.
SMRiQ9HA92. Positions 38-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1002S-adenosyl-L-methionine 2 bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 187Poly-Ala
Compositional biasi20 – 234Poly-Arg

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IF9E. Eukaryota.
COG0635. LUCA.
GeneTreeiENSGT00390000011216.
HOGENOMiHOG000015381.
HOVERGENiHBG108421.
InParanoidiQ9HA92.
OMAiRTHSACD.
OrthoDBiEOG7TJ3JG.
PhylomeDBiQ9HA92.
TreeFamiTF332416.

Family and domain databases

Gene3Di3.80.30.20. 1 hit.
InterProiIPR004559. Coprogen_oxidase_HemN-rel.
IPR006638. Elp3/MiaB/NifB.
IPR010723. HemN_C.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF06969. HemN_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00539. hemN_rel. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HA92-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALPGARARG WAAAARAAQR RRRVENAGGS PSPEPAGRRA ALYVHWPYCE
60 70 80 90 100
KRCSYCNFNK YIPRRLEEAA MQKCLVTEAQ TLLRLSGVQR VESVFFGGGT
110 120 130 140 150
PSLASPHTVA AVLEAVAQAA HLPADLEVTL EANPTSAPGS RLAEFGAAGV
160 170 180 190 200
NRLSIGLQSL DDTELRLLGR THSACDALRT LAEARRLFPG RVSVDLMLGL
210 220 230 240 250
PAQQVGPWLG QLQELLHHCD DHLSLYQLSL ERGTALFAQV QRGALPAPDP
260 270 280 290 300
ELAAEMYQRG RAVLREAGFH QYEVSNFARN GALSTHNWTY WQCGQYLGVG
310 320 330 340 350
PGAHGRFMPQ GAGGHTREAR IQTLEPDNWM KEVMLFGHGT RKRVPLGRLE
360 370 380 390 400
LLEEVLALGL RTDVGITHQH WQQFEPQLTL WDVFGANKEV QELLERGLLQ
410 420 430 440
LDHRGLRCSW EGLAVLDSLL LTLLPQLQEA WQQRTPSPVP GG
Length:442
Mass (Da):48,714
Last modified:April 17, 2007 - v2
Checksum:iA450E02F3AE2D554
GO
Isoform 2 (identifier: Q9HA92-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-158: Missing.
     282-307: ALSTHNWTYWQCGQYLGVGPGAHGRF → PMDDLCPRGLEATPGRLGSRHWSLTT
     308-441: Missing.

Note: No experimental confirmation available.
Show »
Length:195
Mass (Da):21,317
Checksum:iC0A73AD8C1CC9EC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861R → G in BAB13962 (PubMed:14702039).Curated
Sequence conflicti213 – 2131Q → R in BAD96192 (Ref. 2) Curated
Sequence conflicti272 – 2721Y → C in BAB13962 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191A → T.1 Publication
Corresponds to variant rs2290862 [ dbSNP | Ensembl ].
VAR_031777
Natural varianti126 – 1261L → S.1 Publication
Corresponds to variant rs2290861 [ dbSNP | Ensembl ].
VAR_031778
Natural varianti354 – 3541E → Q.
Corresponds to variant rs9891176 [ dbSNP | Ensembl ].
VAR_061126

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei46 – 158113Missing in isoform 2. 1 PublicationVSP_056130Add
BLAST
Alternative sequencei282 – 30726ALSTH…AHGRF → PMDDLCPRGLEATPGRLGSR HWSLTT in isoform 2. 1 PublicationVSP_056131Add
BLAST
Alternative sequencei308 – 441134Missing in isoform 2. 1 PublicationVSP_056132Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002026 mRNA. Translation: BAA92043.1.
AK022105 mRNA. Translation: BAB13962.1.
AK297655 mRNA. Translation: BAG60022.1.
AK222472 mRNA. Translation: BAD96192.1.
AC021491 Genomic DNA. No translation available.
BC005854 mRNA. Translation: AAH05854.4.
BC050538 mRNA. Translation: AAH50538.1.
CCDSiCCDS11569.1. [Q9HA92-1]
RefSeqiNP_060816.1. NM_018346.2. [Q9HA92-1]
XP_011523279.1. XM_011524977.1. [Q9HA92-1]
UniGeneiHs.8033.

Genome annotation databases

EnsembliENST00000258955; ENSP00000258955; ENSG00000136444. [Q9HA92-1]
ENST00000515221; ENSP00000424558; ENSG00000136444. [Q9HA92-2]
GeneIDi55316.
KEGGihsa:55316.
UCSCiuc002iqw.2. human. [Q9HA92-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002026 mRNA. Translation: BAA92043.1.
AK022105 mRNA. Translation: BAB13962.1.
AK297655 mRNA. Translation: BAG60022.1.
AK222472 mRNA. Translation: BAD96192.1.
AC021491 Genomic DNA. No translation available.
BC005854 mRNA. Translation: AAH05854.4.
BC050538 mRNA. Translation: AAH50538.1.
CCDSiCCDS11569.1. [Q9HA92-1]
RefSeqiNP_060816.1. NM_018346.2. [Q9HA92-1]
XP_011523279.1. XM_011524977.1. [Q9HA92-1]
UniGeneiHs.8033.

3D structure databases

ProteinModelPortaliQ9HA92.
SMRiQ9HA92. Positions 38-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120598. 10 interactions.
IntActiQ9HA92. 1 interaction.
STRINGi9606.ENSP00000258955.

PTM databases

iPTMnetiQ9HA92.

Polymorphism and mutation databases

BioMutaiRSAD1.
DMDMi145566941.

Proteomic databases

EPDiQ9HA92.
MaxQBiQ9HA92.
PaxDbiQ9HA92.
PeptideAtlasiQ9HA92.
PRIDEiQ9HA92.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258955; ENSP00000258955; ENSG00000136444. [Q9HA92-1]
ENST00000515221; ENSP00000424558; ENSG00000136444. [Q9HA92-2]
GeneIDi55316.
KEGGihsa:55316.
UCSCiuc002iqw.2. human. [Q9HA92-1]

Organism-specific databases

CTDi55316.
GeneCardsiRSAD1.
HGNCiHGNC:25634. RSAD1.
HPAiHPA022436.
HPA022967.
neXtProtiNX_Q9HA92.
PharmGKBiPA134945325.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF9E. Eukaryota.
COG0635. LUCA.
GeneTreeiENSGT00390000011216.
HOGENOMiHOG000015381.
HOVERGENiHBG108421.
InParanoidiQ9HA92.
OMAiRTHSACD.
OrthoDBiEOG7TJ3JG.
PhylomeDBiQ9HA92.
TreeFamiTF332416.

Miscellaneous databases

ChiTaRSiRSAD1. human.
GenomeRNAii55316.
PROiQ9HA92.

Gene expression databases

BgeeiQ9HA92.
CleanExiHS_RSAD1.
ExpressionAtlasiQ9HA92. baseline and differential.
GenevisibleiQ9HA92. HS.

Family and domain databases

Gene3Di3.80.30.20. 1 hit.
InterProiIPR004559. Coprogen_oxidase_HemN-rel.
IPR006638. Elp3/MiaB/NifB.
IPR010723. HemN_C.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF06969. HemN_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00539. hemN_rel. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain, Embryo and Placenta.
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adipose tissue.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS THR-119 AND SER-126.
    Tissue: Blood and Colon.

Entry informationi

Entry nameiRSAD1_HUMAN
AccessioniPrimary (citable) accession number: Q9HA92
Secondary accession number(s): B4DMW0
, Q53HV8, Q86VC4, Q9BRY7, Q9NUS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: July 6, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.