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Protein

Sulfatase-modifying factor 2

Gene

SUMF2

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

Functioni

Lacks formyl-glycine generating activity and is unable to convert newly synthesized inactive sulfatases to their active form. Inhibits the activation of sulfatases by SUMF1.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi194 – 1941Calcium 1; via carbonyl oxygen
Metal bindingi195 – 1951Calcium 1; via carbonyl oxygen
Metal bindingi208 – 2081Calcium 1
Metal bindingi210 – 2101Calcium 1; via carbonyl oxygen
Metal bindingi229 – 2291Calcium 2; via carbonyl oxygen
Metal bindingi232 – 2321Calcium 2; via carbonyl oxygen
Metal bindingi234 – 2341Calcium 2; via carbonyl oxygen
Metal bindingi236 – 2361Calcium 2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-1663150. The activation of arylsulfatases.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfatase-modifying factor 2
Alternative name(s):
C-alpha-formylglycine-generating enzyme 2
Gene namesi
Name:SUMF2
ORF Names:PSEC0171, UNQ1968/PRO4500
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:20415. SUMF2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi156 – 1561C → A: Abolishes interaction with and inhibition of SUMF1. Can still form homodimers. 1 Publication
Mutagenesisi290 – 2901C → A: Abolishes interaction with and inhibition of SUMF1. Can still form homodimers. 1 Publication

Organism-specific databases

PharmGKBiPA134921869.

Polymorphism and mutation databases

BioMutaiSUMF2.
DMDMi296452916.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 301276Sulfatase-modifying factor 2PRO_0000033459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi156 ↔ 2902 Publications
Glycosylationi191 – 1911N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ8NBJ7.
MaxQBiQ8NBJ7.
PaxDbiQ8NBJ7.
PRIDEiQ8NBJ7.

2D gel databases

REPRODUCTION-2DPAGEIPI00171412.

PTM databases

iPTMnetiQ8NBJ7.
PhosphoSiteiQ8NBJ7.

Miscellaneous databases

PMAP-CutDBQ8NBJ7.

Expressioni

Tissue specificityi

Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Highest levels in kidney, liver and placenta.2 Publications

Gene expression databases

BgeeiQ8NBJ7.
CleanExiHS_SUMF2.
ExpressionAtlasiQ8NBJ7. baseline and differential.
GenevisibleiQ8NBJ7. HS.

Organism-specific databases

HPAiCAB025743.
HPA024040.

Interactioni

Subunit structurei

Homodimer and heterodimer with SUMF1.2 Publications

Protein-protein interaction databases

BioGridi117386. 11 interactions.
IntActiQ8NBJ7. 6 interactions.
MINTiMINT-1196002.
STRINGi9606.ENSP00000341938.

Structurei

Secondary structure

1
301
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 334Combined sources
Beta strandi36 – 416Combined sources
Beta strandi55 – 595Combined sources
Beta strandi61 – 677Combined sources
Helixi71 – 8111Combined sources
Helixi86 – 905Combined sources
Beta strandi92 – 965Combined sources
Helixi97 – 993Combined sources
Helixi102 – 1065Combined sources
Beta strandi118 – 1225Combined sources
Helixi149 – 15810Combined sources
Helixi166 – 1749Combined sources
Beta strandi185 – 1873Combined sources
Turni200 – 2023Combined sources
Beta strandi231 – 24111Combined sources
Helixi245 – 2473Combined sources
Beta strandi250 – 2545Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi274 – 2774Combined sources
Beta strandi291 – 2933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y4JX-ray1.86A/B27-301[»]
ProteinModelPortaliQ8NBJ7.
SMRiQ8NBJ7. Positions 27-294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NBJ7.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase-modifying factor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFQ0. Eukaryota.
COG1262. LUCA.
GeneTreeiENSGT00390000008983.
HOVERGENiHBG054193.
InParanoidiQ8NBJ7.
PhylomeDBiQ8NBJ7.

Family and domain databases

Gene3Di3.90.1580.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR005532. SUMF_dom.
[Graphical view]
PfamiPF03781. FGE-sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NBJ7-1) [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
MARHGLPLLP LLSLLVGAWL KLGNGQATSM VQLQGGRFLM GTNSPDSRDG
60 70 80 90 100
DGPVREATVK PFAIDIFPVT NKDFRDFVRE KKYRTEAEMF GWSFVFEDFV
110 120 130 140 150
SDELRNKATQ PMKSVLWWLP VEKAFWRQPA GPGSGIRERL EHPVLHVSWN
160 170 180 190 200
DARAYCAWRG KRLPTEEEWE FAARGGLKGQ VYPWGNWFQP NRTNLWQGKF
210 220 230 240 250
PKGDKAEDGF HGVSPVNAFP AQNNYGLYDL LGNVWEWTAS PYQAAEQDMR
260 270 280 290 300
VLRGASWIDT ADGSANHRAR VTTRMGNTPD SASDNLGFRC AADAGRPPGE

L
Length:301
Mass (Da):33,843
Last modified:May 18, 2010 - v2
Checksum:i1E834CEA56922755
GO
Isoform 2 (identifier: Q8NBJ7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-88: Missing.

Show »
Length:213
Mass (Da):24,117
Checksum:iE8AF9A2220AEE11D
GO
Isoform 3 (identifier: Q8NBJ7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     227-301: LYDLLGNVWE...ADAGRPPGEL → WATLQIQPQT...QVFLLEAKYY

Note: No experimental confirmation available.
Show »
Length:339
Mass (Da):37,395
Checksum:i74E1DA4C9B85F276
GO
Isoform 5 (identifier: Q8NBJ7-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-197: Missing.

Show »
Length:217
Mass (Da):23,902
Checksum:i80822E9067E4E5C2
GO
Isoform 4 (identifier: Q8NBJ7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-301: SVLWWLPVEK...ADAGRPPGEL → VKFTHGGTGS...QVFLLEAKYY

Note: No experimental confirmation available.
Show »
Length:321
Mass (Da):34,187
Checksum:iA4B285CB52C41407
GO

Sequence cautioni

The sequence AAH00224.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAB43247.1 differs from that shown. Reason: Frameshift at positions 150 and 187. Curated
The sequence CAB43247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511D → E.Combined sources6 Publications
Corresponds to variant rs4245575 [ dbSNP | Ensembl ].
VAR_046951

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8888Missing in isoform 2. 2 PublicationsVSP_007878Add
BLAST
Alternative sequencei114 – 301188SVLWW…PPGEL → VKFTHGGTGSSQTAPTCGRE SSPRETKLRMASMESPQMLS PPRTTTGSMTSWGTCGSGQH HRTRLLSRTCASSGGHPGST QLMALPITGPGSPPGWATLQ IQPQTTSVSAVLQTQAGRQG SCKQPGGDKEKSLLGSLSFP GHVANSAIPSSRASASGKNF PFPVSHPSVAGASHQGRRGL SLLCFGEGAQCVLTMAGGQV FLLEAKYY in isoform 4. 1 PublicationVSP_007880Add
BLAST
Alternative sequencei114 – 19784Missing in isoform 5. CuratedVSP_040878Add
BLAST
Alternative sequencei227 – 30175LYDLL…PPGEL → WATLQIQPQTTSVSAVLQTQ AGRQGSCKQPGGDKEKSLLG SLSFPGHVANSAIPSSRASA SGKNFPFPVSHPSVAGASHQ GRRGLSLLCFGEGAQCVLTM AGGQVFLLEAKYY in isoform 3. 1 PublicationVSP_007879Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY323911 mRNA. Translation: AAP86218.1.
AY359103 mRNA. Translation: AAQ89461.1.
AK300488 mRNA. Translation: BAG62203.1.
AK301627 mRNA. Translation: BAG63112.1.
AK075477 mRNA. Translation: BAC11643.1.
AL050037 mRNA. Translation: CAB43247.1. Sequence problems.
CH471140 Genomic DNA. Translation: EAX07980.1.
BC000224 mRNA. Translation: AAH00224.1. Different initiation.
BC006159 mRNA. Translation: AAH06159.1.
BC015600 mRNA. Translation: AAH15600.2.
BC084539 mRNA. Translation: AAH84539.1.
BC111092 mRNA. Translation: AAI11093.1.
CCDSiCCDS55111.1. [Q8NBJ7-2]
PIRiT08715.
RefSeqiNP_001035934.2. NM_001042469.1.
NP_001035935.2. NM_001042470.1.
NP_001123541.1. NM_001130069.2.
NP_001139805.1. NM_001146333.1. [Q8NBJ7-2]
NP_056226.2. NM_015411.2.
UniGeneiHs.279696.

Genome annotation databases

EnsembliENST00000275607; ENSP00000275607; ENSG00000129103. [Q8NBJ7-2]
GeneIDi25870.
KEGGihsa:25870.
UCSCiuc003trt.4. human. [Q8NBJ7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY323911 mRNA. Translation: AAP86218.1.
AY359103 mRNA. Translation: AAQ89461.1.
AK300488 mRNA. Translation: BAG62203.1.
AK301627 mRNA. Translation: BAG63112.1.
AK075477 mRNA. Translation: BAC11643.1.
AL050037 mRNA. Translation: CAB43247.1. Sequence problems.
CH471140 Genomic DNA. Translation: EAX07980.1.
BC000224 mRNA. Translation: AAH00224.1. Different initiation.
BC006159 mRNA. Translation: AAH06159.1.
BC015600 mRNA. Translation: AAH15600.2.
BC084539 mRNA. Translation: AAH84539.1.
BC111092 mRNA. Translation: AAI11093.1.
CCDSiCCDS55111.1. [Q8NBJ7-2]
PIRiT08715.
RefSeqiNP_001035934.2. NM_001042469.1.
NP_001035935.2. NM_001042470.1.
NP_001123541.1. NM_001130069.2.
NP_001139805.1. NM_001146333.1. [Q8NBJ7-2]
NP_056226.2. NM_015411.2.
UniGeneiHs.279696.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y4JX-ray1.86A/B27-301[»]
ProteinModelPortaliQ8NBJ7.
SMRiQ8NBJ7. Positions 27-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117386. 11 interactions.
IntActiQ8NBJ7. 6 interactions.
MINTiMINT-1196002.
STRINGi9606.ENSP00000341938.

PTM databases

iPTMnetiQ8NBJ7.
PhosphoSiteiQ8NBJ7.

Polymorphism and mutation databases

BioMutaiSUMF2.
DMDMi296452916.

2D gel databases

REPRODUCTION-2DPAGEIPI00171412.

Proteomic databases

EPDiQ8NBJ7.
MaxQBiQ8NBJ7.
PaxDbiQ8NBJ7.
PRIDEiQ8NBJ7.

Protocols and materials databases

DNASUi25870.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000275607; ENSP00000275607; ENSG00000129103. [Q8NBJ7-2]
GeneIDi25870.
KEGGihsa:25870.
UCSCiuc003trt.4. human. [Q8NBJ7-1]

Organism-specific databases

CTDi25870.
GeneCardsiSUMF2.
HGNCiHGNC:20415. SUMF2.
HPAiCAB025743.
HPA024040.
MIMi607940. gene.
neXtProtiNX_Q8NBJ7.
PharmGKBiPA134921869.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFQ0. Eukaryota.
COG1262. LUCA.
GeneTreeiENSGT00390000008983.
HOVERGENiHBG054193.
InParanoidiQ8NBJ7.
PhylomeDBiQ8NBJ7.

Enzyme and pathway databases

ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-1663150. The activation of arylsulfatases.

Miscellaneous databases

EvolutionaryTraceiQ8NBJ7.
GeneWikiiSUMF2.
GenomeRNAii25870.
PMAP-CutDBQ8NBJ7.
PROiQ8NBJ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NBJ7.
CleanExiHS_SUMF2.
ExpressionAtlasiQ8NBJ7. baseline and differential.
GenevisibleiQ8NBJ7. HS.

Family and domain databases

Gene3Di3.90.1580.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR005532. SUMF_dom.
[Graphical view]
PfamiPF03781. FGE-sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases."
    Cosma M.P., Pepe S., Annunziata I., Newbold R.F., Grompe M., Parenti G., Ballabio A.
    Cell 113:445-456(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT GLU-51.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-51.
  3. "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] (ISOFORM 2), VARIANT GLU-51.
    Tissue: Colon and Prostate.
  4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-51.
    Tissue: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT GLU-51.
    Tissue: Fetal kidney.
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORMS 1; 2 AND 3), VARIANT GLU-51.
    Tissue: Eye, Ovary and Placenta.
  9. "Expression, localization, structural, and functional characterization of pFGE, the paralog of the Calpha-formylglycine-generating enzyme."
    Mariappan M., Preusser-Kunze A., Balleininger M., Eiselt N., Schmidt B., Gande S.L., Wenzel D., Dierks T., von Figura K.
    J. Biol. Chem. 280:15173-15179(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, GLYCOSYLATION, TISSUE SPECIFICITY.
  10. "Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2."
    Zito E., Fraldi A., Pepe S., Annunziata I., Kobinger G., Di Natale P., Ballabio A., Cosma M.P.
    EMBO Rep. 6:655-660(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-156 AND CYS-290.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme."
    Dickmanns A., Schmidt B., Rudolph M.G., Mariappan M., Dierks T., von Figura K., Ficner R.
    J. Biol. Chem. 280:15180-15187(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 27-301 IN COMPLEX WITH CALCIUM IONS, GLYCOSYLATION AT ASN-191, DISULFIDE BONDS.
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSUMF2_HUMAN
AccessioniPrimary (citable) accession number: Q8NBJ7
Secondary accession number(s): B4DU41
, B4DWQ0, Q14DW5, Q53ZE3, Q96BH2, Q9BRN3, Q9BWI1, Q9Y405
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: May 18, 2010
Last modified: June 8, 2016
This is version 144 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.