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Protein

Phosphoglucomutase-like protein 5

Gene

PGM5

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

Functioni

Component of adherens-type cell-cell and cell-matrix junctions. Lacks phosphoglucomutase activity.

Cofactori

Mg2+CuratedNote: Binds 1 Mg2+ ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281SubstrateBy similarity
Active sitei122 – 1221Phosphoserine intermediateBy similarity
Metal bindingi122 – 1221Magnesium; via phosphate groupBy similarity
Binding sitei135 – 1351SubstrateBy similarity
Metal bindingi293 – 2931MagnesiumBy similarity
Metal bindingi295 – 2951MagnesiumBy similarity
Metal bindingi297 – 2971MagnesiumBy similarity
Binding sitei394 – 3941SubstrateBy similarity
Binding sitei520 – 5201SubstrateBy similarity

GO - Molecular functioni

  1. intramolecular transferase activity, phosphotransferases Source: InterPro
  2. magnesium ion binding Source: InterPro
  3. structural molecule activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
  2. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism, Cell adhesion, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucomutase-like protein 5
Alternative name(s):
Aciculin
Phosphoglucomutase-related protein
Short name:
PGM-RP
Gene namesi
Name:PGM5
Synonyms:PGMRP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:8908. PGM5.

Subcellular locationi

Cell junctionadherens junction 1 Publication. Cytoplasmcytoskeleton 1 Publication
Note: Adherens-type cellular junctions. Concentrated in focal contacts at the ends of actin bundles, and associated with actin filaments.

GO - Cellular componenti

  1. cell-cell adherens junction Source: MGI
  2. costamere Source: UniProtKB
  3. cytoplasmic side of plasma membrane Source: UniProtKB
  4. dystrophin-associated glycoprotein complex Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. intercalated disc Source: UniProtKB
  7. sarcolemma Source: UniProtKB
  8. spot adherens junction Source: UniProtKB
  9. stress fiber Source: UniProtKB
  10. Z disc Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 567567Phosphoglucomutase-like protein 5PRO_0000147787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei122 – 1221Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15124.
PaxDbiQ15124.
PRIDEiQ15124.

PTM databases

PhosphoSiteiQ15124.

Expressioni

Tissue specificityi

Detected in smooth and cardiac muscle at high levels and in skeletal muscle at low level. Present in other tissues due to vascular or other smooth muscle component. Low levels are present in liver, kidney, skin and brain (at protein level).2 Publications

Developmental stagei

In the developing aorta, expressed at low levels in 10-12 week old fetuses. Levels increase progressively in 24 week fetus, 6 month old child and 1.5 year old child aortic smooth muscle, reaching a maximum at maturity.1 Publication

Gene expression databases

BgeeiQ15124.
CleanExiHS_PGM5.
ExpressionAtlasiQ15124. baseline and differential.
GenevestigatoriQ15124.

Organism-specific databases

HPAiCAB034397.
HPA046329.

Interactioni

Subunit structurei

Interacts with cytoskeletal proteins dystrophin and utrophin.

Protein-protein interaction databases

BioGridi111258. 3 interactions.
STRINGi9606.ENSP00000379678.

Structurei

3D structure databases

ProteinModelPortaliQ15124.
SMRiQ15124. Positions 6-567.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1232Substrate bindingBy similarity
Regioni297 – 2982Substrate bindingBy similarity
Regioni381 – 3833Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi510 – 5134Poly-Ser

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG0033.
GeneTreeiENSGT00390000011831.
HOGENOMiHOG000009550.
HOVERGENiHBG001599.
InParanoidiQ15124.
KOiK15636.
OMAiSTIRIYA.
PhylomeDBiQ15124.
TreeFamiTF300350.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q15124-1) [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
MEGSPIPVLT VPTAPYEDQR PAGGGGLRRP TGLFEGQRNY LPNFIQSVLS
60 70 80 90 100
SIDLRDRQGC TMVVGSDGRY FSRTAIEIVV QMAAANGIGR LIIGQNGILS
110 120 130 140 150
TPAVSCIIRK IKAAGGIILT ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD
160 170 180 190 200
KIYQISKTIE EYAICPDLRI DLSRLGRQEF DLENKFKPFR VEIVDPVDIY
210 220 230 240 250
LNLLRTIFDF HAIKGLLTGP SQLKIRIDAM HGVMGPYVRK VLCDELGAPA
260 270 280 290 300
NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM
310 320 330 340 350
ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSMALDRVA
360 370 380 390 400
KSMKVPVYET PAGWRFFSNL MDSGRCNLCG EESFGTGSDH LREKDGLWAV
410 420 430 440 450
LVWLSIIAAR KQSVEEIVRD HWAKFGRHYY CRFDYEGLDP KTTYYIMRDL
460 470 480 490 500
EALVTDKSFI GQQFAVGSHV YSVAKTDSFE YVDPVDGTVT KKQGLRIIFS
510 520 530 540 550
DASRLIFRLS SSSGVRATLR LYAESYERDP SGHDQEPQAV LSPLIAIALK
560
ISQIHERTGR RGPTVIT
Length:567
Mass (Da):62,225
Last modified:July 10, 2007 - v2
Checksum:i00583A442977A025
GO
Isoform 2 (identifier: Q15124-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     387-387: G → V
     388-567: Missing.

Note: No experimental confirmation available.

Show »
Length:387
Mass (Da):41,790
Checksum:i31FF5EACAFB47DC4
GO

Sequence cautioni

The sequence AAC41948.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH33073.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA73882.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221A → S in CAA73882 (PubMed:9342213).Curated
Sequence conflicti244 – 2441D → E AA sequence (PubMed:8175905).Curated
Sequence conflicti260 – 2612ED → DE AA sequence (PubMed:8175905).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei387 – 3871G → V in isoform 2. 1 PublicationVSP_030014
Alternative sequencei388 – 567180Missing in isoform 2. 1 PublicationVSP_030015Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK297108 mRNA. Translation: BAG59618.1.
AL161457, AL353608, AL353616 Genomic DNA. Translation: CAI16959.2.
AL353608, AL161457, AL353616 Genomic DNA. Translation: CAI41169.2.
AL353616, AL161457, AL353608 Genomic DNA. Translation: CAH71906.2.
AL353608, AL161457 Genomic DNA. Translation: CAO03528.1.
AL161457, AL353608 Genomic DNA. Translation: CAO03529.1.
BC033073 mRNA. Translation: AAH33073.1. Different initiation.
Y13478 Genomic DNA. Translation: CAA73882.1. Different initiation.
L40933 Genomic DNA. Translation: AAC41948.1. Different initiation.
CCDSiCCDS6622.2. [Q15124-1]
PIRiS62629.
RefSeqiNP_068800.2. NM_021965.3. [Q15124-1]
UniGeneiHs.307835.

Genome annotation databases

EnsembliENST00000396392; ENSP00000379674; ENSG00000154330. [Q15124-2]
ENST00000396396; ENSP00000379678; ENSG00000154330. [Q15124-1]
GeneIDi5239.
KEGGihsa:5239.
UCSCiuc004agr.3. human. [Q15124-1]

Polymorphism databases

DMDMi152031655.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK297108 mRNA. Translation: BAG59618.1.
AL161457, AL353608, AL353616 Genomic DNA. Translation: CAI16959.2.
AL353608, AL161457, AL353616 Genomic DNA. Translation: CAI41169.2.
AL353616, AL161457, AL353608 Genomic DNA. Translation: CAH71906.2.
AL353608, AL161457 Genomic DNA. Translation: CAO03528.1.
AL161457, AL353608 Genomic DNA. Translation: CAO03529.1.
BC033073 mRNA. Translation: AAH33073.1. Different initiation.
Y13478 Genomic DNA. Translation: CAA73882.1. Different initiation.
L40933 Genomic DNA. Translation: AAC41948.1. Different initiation.
CCDSiCCDS6622.2. [Q15124-1]
PIRiS62629.
RefSeqiNP_068800.2. NM_021965.3. [Q15124-1]
UniGeneiHs.307835.

3D structure databases

ProteinModelPortaliQ15124.
SMRiQ15124. Positions 6-567.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111258. 3 interactions.
STRINGi9606.ENSP00000379678.

PTM databases

PhosphoSiteiQ15124.

Polymorphism databases

DMDMi152031655.

Proteomic databases

MaxQBiQ15124.
PaxDbiQ15124.
PRIDEiQ15124.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396392; ENSP00000379674; ENSG00000154330. [Q15124-2]
ENST00000396396; ENSP00000379678; ENSG00000154330. [Q15124-1]
GeneIDi5239.
KEGGihsa:5239.
UCSCiuc004agr.3. human. [Q15124-1]

Organism-specific databases

CTDi5239.
GeneCardsiGC09P070971.
H-InvDBHIX0020782.
HGNCiHGNC:8908. PGM5.
HPAiCAB034397.
HPA046329.
MIMi600981. gene.
neXtProtiNX_Q15124.
PharmGKBiPA33245.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0033.
GeneTreeiENSGT00390000011831.
HOGENOMiHOG000009550.
HOVERGENiHBG001599.
InParanoidiQ15124.
KOiK15636.
OMAiSTIRIYA.
PhylomeDBiQ15124.
TreeFamiTF300350.

Miscellaneous databases

ChiTaRSiPGM5. human.
GeneWikiiPGM5.
GenomeRNAii5239.
NextBioi20240.
PROiQ15124.
SOURCEiSearch...

Gene expression databases

BgeeiQ15124.
CleanExiHS_PGM5.
ExpressionAtlasiQ15124. baseline and differential.
GenevestigatoriQ15124.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Muscle.
  4. "Characterisation of the promoter which regulates expression of a phosphoglucomutase-related protein, a component of the dystrophin/utrophin cytoskeleton predominantly expressed in smooth muscle."
    Moiseeva E.P., Critchley D.R.
    Eur. J. Biochem. 248:634-643(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-87.
  5. Parker K.
    Submitted (MAY-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 29-55; 158-169; 191-224; 227-239; 355-375; 433-492 AND 497-504, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "A novel dystrophin/utrophin-associated protein is an enzymatically inactive member of the phosphoglucomutase superfamily."
    Moiseeva E.P., Belkin A.M., Spurr N.K., Koteliansky V.E., Critchley D.R.
    Eur. J. Biochem. 235:103-113(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-567, TISSUE SPECIFICITY.
    Tissue: Uterus.
  7. "A novel phosphoglucomutase-related protein is concentrated in adherens junctions of muscle and nonmuscle cells."
    Belkin A.M., Klimanskaya I.V., Lukashev M.E., Lilley K., Critchley D.R., Koteliansky V.E.
    J. Cell Sci. 107:159-173(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 82-104; 234-262 AND 447-467, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Uterus.
  8. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPGM5_HUMAN
AccessioniPrimary (citable) accession number: Q15124
Secondary accession number(s): B1AM46
, B4DLQ6, Q5VYV3, Q8N527, Q9UDH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 10, 2007
Last modified: March 4, 2015
This is version 131 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

External Data

Dasty 3

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 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.