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

SPARC-related modular calcium-binding protein 1

Gene

SMOC1

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

Functioni

Plays essential roles in both eye and limb development. Probable regulator of osteoblast differentiation.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi372 – 383121Sequence analysisAdd
BLAST
Calcium bindingi409 – 420122Sequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • eye development Source: UniProtKB
  • limb development Source: UniProtKB
  • regulation of osteoblast differentiation Source: UniProtKB
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
SPARC-related modular calcium-binding protein 1
Alternative name(s):
Secreted modular calcium-binding protein 1
Short name:
SMOC-1
Gene namesi
Name:SMOC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20318. SMOC1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Ophthalmoacromelic syndrome (OAS)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare disorder presenting with ocular anomalies, ranging from mild microphthalmia to true anophthalmia, and limb anomalies. Limb malformations include fused 4th and 5th metacarpals and short 5th finger in hands, and oligodactyly in foot (four toes). Most patients have bilateral anophthalmia/ microphthalmia, but unilateral abnormality is also noted. Other malformations are rare, but venous or vertebral anomaly was recognized each in single cases.
See also OMIM:206920
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti278 – 2781R → C in OAS. 1 Publication
Corresponds to variant rs776638586 [ dbSNP | Ensembl ].
VAR_069326
Natural varianti283 – 2831T → N in OAS. 1 Publication
VAR_069327
Natural varianti286 – 2861R → H in OAS. 1 Publication
VAR_069328

Keywords - Diseasei

Disease mutation, Microphthalmia

Organism-specific databases

MalaCardsiSMOC1.
MIMi206920. phenotype.
Orphaneti1106. Microphthalmia with limb anomalies.
PharmGKBiPA134942329.

Polymorphism and mutation databases

BioMutaiSMOC1.
DMDMi38258649.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 434408SPARC-related modular calcium-binding protein 1PRO_0000020316Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi95 ↔ 118By similarity
Disulfide bondi129 ↔ 136By similarity
Disulfide bondi138 ↔ 158By similarity
Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence analysis
Disulfide bondi227 ↔ 251By similarity
Disulfide bondi262 ↔ 269By similarity
Disulfide bondi271 ↔ 292By similarity
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9H4F8.
PaxDbiQ9H4F8.
PeptideAtlasiQ9H4F8.
PRIDEiQ9H4F8.

PTM databases

iPTMnetiQ9H4F8.
PhosphoSiteiQ9H4F8.

Expressioni

Tissue specificityi

Widely expressed in many tissues with a strongest signal in ovary. No expression in spleen.1 Publication

Gene expression databases

BgeeiQ9H4F8.
CleanExiHS_SMOC1.
ExpressionAtlasiQ9H4F8. baseline and differential.
GenevisibleiQ9H4F8. HS.

Organism-specific databases

HPAiHPA004153.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Hoxa1P090222EBI-2801103,EBI-3957603From a different organism.
KRTAP10-8P604103EBI-2801103,EBI-10171774
NOTCH2NLQ7Z3S93EBI-2801103,EBI-945833
TCF4P158843EBI-2801103,EBI-533224

Protein-protein interaction databases

BioGridi122055. 24 interactions.
IntActiQ9H4F8. 5 interactions.
STRINGi9606.ENSP00000355110.

Structurei

3D structure databases

ProteinModelPortaliQ9H4F8.
SMRiQ9H4F8. Positions 368-425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 8953Kazal-likePROSITE-ProRule annotationAdd
BLAST
Domaini92 – 15867Thyroglobulin type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini224 – 29269Thyroglobulin type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini359 – 39436EF-hand 1Add
BLAST
Domaini396 – 43136EF-hand 2Add
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.Curated
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.
HOGENOMiHOG000234328.
HOVERGENiHBG058558.
InParanoidiQ9H4F8.
OMAiRGHRTTG.
OrthoDBiEOG7KDFB1.
PhylomeDBiQ9H4F8.
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.
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.
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: Q9H4F8-1) [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
MLPARCARLL TPHLLLVLVQ LSPARGHRTT GPRFLISDRD PQCNLHCSRT
60 70 80 90 100
QPKPICASDG RSYESMCEYQ RAKCRDPTLG VVHRGRCKDA GQSKCRLERA
110 120 130 140 150
QALEQAKKPQ EAVFVPECGE DGSFTQVQCH TYTGYCWCVT PDGKPISGSS
160 170 180 190 200
VQNKTPVCSG SVTDKPLSQG NSGRKDDGSK PTPTMETQPV FDGDEITAPT
210 220 230 240 250
LWIKHLVIKD SKLNNTNIRN SEKVYSCDQE RQSALEEAQQ NPREGIVIPE
260 270 280 290 300
CAPGGLYKPV QCHQSTGYCW CVLVDTGRPL PGTSTRYVMP SCESDARAKT
310 320 330 340 350
TEADDPFKDR ELPGCPEGKK MEFITSLLDA LTTDMVQAIN SAAPTGGGRF
360 370 380 390 400
SEPDPSHTLE ERVVHWYFSQ LDSNSSNDIN KREMKPFKRY VKKKAKPKKC
410 420 430
ARRFTDYCDL NKDKVISLPE LKGCLGVSKE GRLV
Length:434
Mass (Da):48,163
Last modified:March 1, 2001 - v1
Checksum:i2CB639212BA42478
GO
Isoform 2 (identifier: Q9H4F8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     430-430: E → EV

Note: No experimental confirmation available.
Show »
Length:435
Mass (Da):48,262
Checksum:i3E1945054B9BA424
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821V → M.
Corresponds to variant rs10150925 [ dbSNP | Ensembl ].
VAR_034498
Natural varianti278 – 2781R → C in OAS. 1 Publication
Corresponds to variant rs776638586 [ dbSNP | Ensembl ].
VAR_069326
Natural varianti283 – 2831T → N in OAS. 1 Publication
VAR_069327
Natural varianti286 – 2861R → H in OAS. 1 Publication
VAR_069328

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei430 – 4301E → EV in isoform 2. 2 PublicationsVSP_008720

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ249900 mRNA. Translation: CAC10352.1.
AK289988 mRNA. Translation: BAF82677.1.
AK313063 mRNA. Translation: BAG35892.1.
AL135747 Genomic DNA. No translation available.
AL157789 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81013.1.
CH471061 Genomic DNA. Translation: EAW81014.1.
BC008608 mRNA. Translation: AAH08608.1.
BC011548 mRNA. Translation: AAH11548.1.
CCDSiCCDS32110.1. [Q9H4F8-2]
CCDS9798.1. [Q9H4F8-1]
RefSeqiNP_001030024.1. NM_001034852.2. [Q9H4F8-2]
NP_071420.1. NM_022137.5. [Q9H4F8-1]
UniGeneiHs.497349.

Genome annotation databases

EnsembliENST00000361956; ENSP00000355110; ENSG00000198732. [Q9H4F8-2]
ENST00000381280; ENSP00000370680; ENSG00000198732. [Q9H4F8-1]
GeneIDi64093.
KEGGihsa:64093.
UCSCiuc001xls.3. human. [Q9H4F8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ249900 mRNA. Translation: CAC10352.1.
AK289988 mRNA. Translation: BAF82677.1.
AK313063 mRNA. Translation: BAG35892.1.
AL135747 Genomic DNA. No translation available.
AL157789 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81013.1.
CH471061 Genomic DNA. Translation: EAW81014.1.
BC008608 mRNA. Translation: AAH08608.1.
BC011548 mRNA. Translation: AAH11548.1.
CCDSiCCDS32110.1. [Q9H4F8-2]
CCDS9798.1. [Q9H4F8-1]
RefSeqiNP_001030024.1. NM_001034852.2. [Q9H4F8-2]
NP_071420.1. NM_022137.5. [Q9H4F8-1]
UniGeneiHs.497349.

3D structure databases

ProteinModelPortaliQ9H4F8.
SMRiQ9H4F8. Positions 368-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122055. 24 interactions.
IntActiQ9H4F8. 5 interactions.
STRINGi9606.ENSP00000355110.

PTM databases

iPTMnetiQ9H4F8.
PhosphoSiteiQ9H4F8.

Polymorphism and mutation databases

BioMutaiSMOC1.
DMDMi38258649.

Proteomic databases

MaxQBiQ9H4F8.
PaxDbiQ9H4F8.
PeptideAtlasiQ9H4F8.
PRIDEiQ9H4F8.

Protocols and materials databases

DNASUi64093.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361956; ENSP00000355110; ENSG00000198732. [Q9H4F8-2]
ENST00000381280; ENSP00000370680; ENSG00000198732. [Q9H4F8-1]
GeneIDi64093.
KEGGihsa:64093.
UCSCiuc001xls.3. human. [Q9H4F8-1]

Organism-specific databases

CTDi64093.
GeneCardsiSMOC1.
HGNCiHGNC:20318. SMOC1.
HPAiHPA004153.
MalaCardsiSMOC1.
MIMi206920. phenotype.
608488. gene.
neXtProtiNX_Q9H4F8.
Orphaneti1106. Microphthalmia with limb anomalies.
PharmGKBiPA134942329.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4578. Eukaryota.
ENOG410YP7C. LUCA.
GeneTreeiENSGT00390000018436.
HOGENOMiHOG000234328.
HOVERGENiHBG058558.
InParanoidiQ9H4F8.
OMAiRGHRTTG.
OrthoDBiEOG7KDFB1.
PhylomeDBiQ9H4F8.
TreeFamiTF320666.

Miscellaneous databases

ChiTaRSiSMOC1. human.
GenomeRNAii64093.
PROiQ9H4F8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4F8.
CleanExiHS_SMOC1.
ExpressionAtlasiQ9H4F8. baseline and differential.
GenevisibleiQ9H4F8. 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.
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.
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. "Characterization of SMOC-1, a novel modular calcium-binding protein in basement membranes."
    Vannahme C., Smyth N., Miosge N., Goesling S., Frie C., Paulsson M., Maurer P., Hartmann U.
    J. Biol. Chem. 277:37977-37986(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
    Tissue: Fetal brain.
  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] (ISOFORMS 1 AND 2).
    Tissue: Caudate nucleus.
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
    Tissue: Brain and Lung.
  6. "Secretome analysis of human BMSCs and identification of SMOC1 as an important ECM protein in osteoblast differentiation."
    Choi Y.A., Lim J., Kim K.M., Acharya B., Cho J.Y., Bae Y.C., Shin H.I., Kim S.Y., Park E.K.
    J. Proteome Res. 9:2946-2956(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS REGULATOR OF OSTEOBLAST DIFFERENTIATION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  7. Cited for: FUNCTION, INVOLVEMENT IN OAS.
  8. "Mutations in the SPARC-related modular calcium-binding protein 1 gene, SMOC1, cause waardenburg anophthalmia syndrome."
    Abouzeid H., Boisset G., Favez T., Youssef M., Marzouk I., Shakankiry N., Bayoumi N., Descombes P., Agosti C., Munier F.L., Schorderet D.F.
    Am. J. Hum. Genet. 88:92-98(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INVOLVEMENT IN OAS.
  9. Cited for: VARIANTS OAS CYS-278 AND ASN-283.
  10. Cited for: VARIANT OAS HIS-286.

Entry informationi

Entry nameiSMOC1_HUMAN
AccessioniPrimary (citable) accession number: Q9H4F8
Secondary accession number(s): A8K1S3, B2R7P5, Q96F78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 139 of the entry and version 1 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 14
    Human chromosome 14: 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. 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.