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Protein

SPARC-related modular calcium-binding protein 2

Gene

SMOC2

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

Functioni

Promotes matrix assembly and cell adhesiveness (By similarity). Can stimulate endothelial cell proliferation, migration, as well as angiogenesis.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi360 – 371121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi397 – 408122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
SPARC-related modular calcium-binding protein 2
Alternative name(s):
Secreted modular calcium-binding protein 2
Short name:
SMOC-2
Smooth muscle-associated protein 2
Short name:
SMAP-2
Gene namesi
Name:SMOC2
Synonyms:SMAP2
ORF Names:MSTP117
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:20323. SMOC2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Dentin dysplasia 1 (DTDP1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA dental defect in which both primary and secondary dentitions are affected. The clinical crowns of both permanent and deciduous teeth are of normal shape, form and color in most cases, although they may be slightly opalescent and blue or brown. Teeth may be very mobile and exfoliate spontaneously because of inadequate root formation. On radiographs, the roots are short and may be more pointed than normal. Pulp chambers are usually absent except for a chevron-shaped remnant in the crown. Root canals are usually absent.
See also OMIM:125400

Organism-specific databases

MalaCardsiSMOC2.
MIMi125400. phenotype.
Orphaneti314721. Atypical dentin dysplasia due to SMOC2 deficiency.
PharmGKBiPA134934590.

Polymorphism and mutation databases

BioMutaiSMOC2.
DMDMi38258648.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 446425SPARC-related modular calcium-binding protein 2PRO_0000020318Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi90 ↔ 113By similarity
Disulfide bondi124 ↔ 131By similarity
Disulfide bondi133 ↔ 153By similarity
Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence analysis
Disulfide bondi216 ↔ 240By similarity
Disulfide bondi251 ↔ 258By similarity
Disulfide bondi260 ↔ 281By similarity
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9H3U7.
PaxDbiQ9H3U7.
PeptideAtlasiQ9H3U7.
PRIDEiQ9H3U7.

PTM databases

iPTMnetiQ9H3U7.
PhosphoSiteiQ9H3U7.

Expressioni

Gene expression databases

BgeeiQ9H3U7.
CleanExiHS_SMAP2.
ExpressionAtlasiQ9H3U7. baseline and differential.
GenevisibleiQ9H3U7. HS.

Organism-specific databases

HPAiCAB033979.

Interactioni

Subunit structurei

Binds various proteins from the extracellular matrix.By similarity

Protein-protein interaction databases

BioGridi122056. 1 interaction.
STRINGi9606.ENSP00000346537.

Structurei

3D structure databases

ProteinModelPortaliQ9H3U7.
SMRiQ9H3U7. Positions 352-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 8653Kazal-likePROSITE-ProRule annotationAdd
BLAST
Domaini87 – 15367Thyroglobulin type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini213 – 28169Thyroglobulin type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini347 – 38236EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini384 – 41936EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 Kazal-like domain.PROSITE-ProRule annotation
Contains 2 thyroglobulin type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG4578. Eukaryota.
ENOG410YP7C. LUCA.
GeneTreeiENSGT00390000018436.
HOVERGENiHBG058558.
InParanoidiQ9H3U7.
OMAiPRCPGSI.
OrthoDBiEOG7KDFB1.
PhylomeDBiQ9H3U7.
TreeFamiTF320666.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
4.10.800.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002350. Kazal_dom.
IPR019577. SPARC/Testican_Ca-bd-dom.
IPR000716. Thyroglobulin_1.
[Graphical view]
PfamiPF07648. Kazal_2. 1 hit.
PF10591. SPARC_Ca_bdg. 1 hit.
PF00086. Thyroglobulin_1. 2 hits.
[Graphical view]
SMARTiSM00280. KAZAL. 1 hit.
SM00211. TY. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF57610. SSF57610. 2 hits.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51465. KAZAL_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 2 hits.
PS51162. THYROGLOBULIN_1_2. 2 hits.
[Graphical view]

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: Q9H3U7-1) [UniParc]FASTAAdd to basket

Also known as: Smap2

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
MLLPQLCWLP LLAGLLPPVP AQKFSALTFL RVDQDKDKDC SLDCAGSPQK
60 70 80 90 100
PLCASDGRTF LSRCEFQRAK CKDPQLEIAY RGNCKDVSRC VAERKYTQEQ
110 120 130 140 150
ARKEFQQVFI PECNDDGTYS QVQCHSYTGY CWCVTPNGRP ISGTAVAHKT
160 170 180 190 200
PRCPGSVNEK LPQREGTGKT DDAAAPALET QPQGDEEDIA SRYPTLWTEQ
210 220 230 240 250
VKSRQNKTNK NSVSSCDQEH QSALEEAKQP KNDNVVIPEC AHGGLYKPVQ
260 270 280 290 300
CHPSTGYCWC VLVDTGRPIP GTSTRYEQPK CDNTARAHPA KARDLYKGRQ
310 320 330 340 350
LQGCPGAKKH EFLTSVLDAL STDMVHAASD PSSSSGRLSE PDPSHTLEER
360 370 380 390 400
VVHWYFKLLD KNSSGDIGKK EIKPFKRFLR KKSKPKKCVK KFVEYCDVNN
410 420 430 440
DKSISVQELM GCLGVAKEDG KADTKKRHTP RGHAESTSNR QPRKQG
Length:446
Mass (Da):49,674
Last modified:October 31, 2003 - v2
Checksum:iCF0D92A71C9E1006
GO
Isoform 2 (identifier: Q9H3U7-2) [UniParc]FASTAAdd to basket

Also known as: Smap2b

The sequence of this isoform differs from the canonical sequence as follows:
     170-170: T → TVSLQIFSVLNS

Show »
Length:457
Mass (Da):50,863
Checksum:iD20AE3BB82785925
GO

Sequence cautioni

The sequence AAQ13639.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1702KT → TR in CAC10353 (PubMed:12741954).Curated
Sequence conflicti212 – 2121S → P in BAB20267 (PubMed:12031507).Curated
Sequence conflicti434 – 4341A → V in AAH47583 (PubMed:15489334).Curated
Sequence conflicti439 – 4391N → Y in CAC10353 (PubMed:12741954).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei170 – 1701T → TVSLQIFSVLNS in isoform 2. 2 PublicationsVSP_008722

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014730 mRNA. Translation: BAB20267.1.
AB014737 mRNA. Translation: BAB20274.1.
AK056700 mRNA. Translation: BAG51789.1.
AL832303 mRNA. Translation: CAI46175.1.
AL138918
, AL109940, AL136099, AL442124 Genomic DNA. Translation: CAI20434.1.
AL138918
, AL109940, AL136099, AL442124 Genomic DNA. Translation: CAI20435.1.
CH471051 Genomic DNA. Translation: EAW47462.1.
BC028420 mRNA. Translation: AAH28420.1.
BC047583 mRNA. Translation: AAH47583.1.
AF173892 mRNA. Translation: AAQ13639.1. Different initiation.
AJ249902 mRNA. Translation: CAC10353.1.
CCDSiCCDS5307.1. [Q9H3U7-2]
CCDS55076.1. [Q9H3U7-1]
RefSeqiNP_001159884.1. NM_001166412.1. [Q9H3U7-1]
NP_071421.1. NM_022138.2. [Q9H3U7-2]
UniGeneiHs.487200.

Genome annotation databases

EnsembliENST00000354536; ENSP00000346537; ENSG00000112562. [Q9H3U7-2]
ENST00000356284; ENSP00000348630; ENSG00000112562. [Q9H3U7-1]
GeneIDi64094.
KEGGihsa:64094.
UCSCiuc003qwr.2. human. [Q9H3U7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014730 mRNA. Translation: BAB20267.1.
AB014737 mRNA. Translation: BAB20274.1.
AK056700 mRNA. Translation: BAG51789.1.
AL832303 mRNA. Translation: CAI46175.1.
AL138918
, AL109940, AL136099, AL442124 Genomic DNA. Translation: CAI20434.1.
AL138918
, AL109940, AL136099, AL442124 Genomic DNA. Translation: CAI20435.1.
CH471051 Genomic DNA. Translation: EAW47462.1.
BC028420 mRNA. Translation: AAH28420.1.
BC047583 mRNA. Translation: AAH47583.1.
AF173892 mRNA. Translation: AAQ13639.1. Different initiation.
AJ249902 mRNA. Translation: CAC10353.1.
CCDSiCCDS5307.1. [Q9H3U7-2]
CCDS55076.1. [Q9H3U7-1]
RefSeqiNP_001159884.1. NM_001166412.1. [Q9H3U7-1]
NP_071421.1. NM_022138.2. [Q9H3U7-2]
UniGeneiHs.487200.

3D structure databases

ProteinModelPortaliQ9H3U7.
SMRiQ9H3U7. Positions 352-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122056. 1 interaction.
STRINGi9606.ENSP00000346537.

PTM databases

iPTMnetiQ9H3U7.
PhosphoSiteiQ9H3U7.

Polymorphism and mutation databases

BioMutaiSMOC2.
DMDMi38258648.

Proteomic databases

EPDiQ9H3U7.
PaxDbiQ9H3U7.
PeptideAtlasiQ9H3U7.
PRIDEiQ9H3U7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354536; ENSP00000346537; ENSG00000112562. [Q9H3U7-2]
ENST00000356284; ENSP00000348630; ENSG00000112562. [Q9H3U7-1]
GeneIDi64094.
KEGGihsa:64094.
UCSCiuc003qwr.2. human. [Q9H3U7-1]

Organism-specific databases

CTDi64094.
GeneCardsiSMOC2.
HGNCiHGNC:20323. SMOC2.
HPAiCAB033979.
MalaCardsiSMOC2.
MIMi125400. phenotype.
607223. gene.
neXtProtiNX_Q9H3U7.
Orphaneti314721. Atypical dentin dysplasia due to SMOC2 deficiency.
PharmGKBiPA134934590.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4578. Eukaryota.
ENOG410YP7C. LUCA.
GeneTreeiENSGT00390000018436.
HOVERGENiHBG058558.
InParanoidiQ9H3U7.
OMAiPRCPGSI.
OrthoDBiEOG7KDFB1.
PhylomeDBiQ9H3U7.
TreeFamiTF320666.

Miscellaneous databases

ChiTaRSiSMOC2. human.
GeneWikiiSMOC2.
GenomeRNAii64094.
PROiQ9H3U7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H3U7.
CleanExiHS_SMAP2.
ExpressionAtlasiQ9H3U7. baseline and differential.
GenevisibleiQ9H3U7. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
4.10.800.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002350. Kazal_dom.
IPR019577. SPARC/Testican_Ca-bd-dom.
IPR000716. Thyroglobulin_1.
[Graphical view]
PfamiPF07648. Kazal_2. 1 hit.
PF10591. SPARC_Ca_bdg. 1 hit.
PF00086. Thyroglobulin_1. 2 hits.
[Graphical view]
SMARTiSM00280. KAZAL. 1 hit.
SM00211. TY. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF57610. SSF57610. 2 hits.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51465. KAZAL_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 2 hits.
PS51162. THYROGLOBULIN_1_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel smooth muscle associated protein, smap2, upregulated during neointima formation in a rat carotid endarterectomy model."
    Nishimoto S., Hamajima Y., Toda Y., Toyoda H., Kitamura K., Komurasaki T.
    Biochim. Biophys. Acta 1576:225-230(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Heart.
  2. "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 1).
    Tissue: Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lymph node.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
    Tissue: Testis.
  7. Liu Y.Q., Liu B., Wang X.Y., Sheng H., Qin B.M., Zhang Q., Zheng W.Y., Hui R.T.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-446 (ISOFORM 1).
    Tissue: Aorta.
  8. "Characterization of SMOC-2, a modular extracellular calcium-binding protein."
    Vannahme C., Goesling S., Paulsson M., Maurer P., Hartmann U.
    Biochem. J. 373:805-814(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 168-446.
    Tissue: Fetal brain.
  9. "The novel SPARC family member SMOC-2 potentiates angiogenic growth factor activity."
    Rocnik E.F., Liu P., Sato K., Walsh K., Vaziri C.
    J. Biol. Chem. 281:22855-22864(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Homozygosity mapping and candidate prioritization identify mutations, missed by whole-exome sequencing, in SMOC2, causing major dental developmental defects."
    Bloch-Zupan A., Jamet X., Etard C., Laugel V., Muller J., Geoffroy V., Strauss J.P., Pelletier V., Marion V., Poch O., Strahle U., Stoetzel C., Dollfus H.
    Am. J. Hum. Genet. 89:773-781(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN DTDP1.

Entry informationi

Entry nameiSMOC2_HUMAN
AccessioniPrimary (citable) accession number: Q9H3U7
Secondary accession number(s): B3KPS7
, Q4G169, Q5TAT7, Q5TAT8, Q86VV9, Q96SF3, Q9H1L3, Q9H1L4, Q9H3U0, Q9H4F7, Q9HCV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 31, 2003
Last modified: July 6, 2016
This is version 139 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.