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Protein

Chitinase domain-containing protein 1

Gene

CHID1

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

Functioni

Saccharide- and LPS-binding protein with possible roles in pathogen sensing and endotoxin neutralization. Ligand-binding specificity relates to the length of the oligosaccharides, with preference for chitotetraose (in vitro).1 Publication

GO - Molecular functioni

  • chitinase activity Source: GO_Central
  • chitin binding Source: GO_Central
  • oligosaccharide binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitinase domain-containing protein 1
Alternative name(s):
Stabilin-1-interacting chitinase-like protein
Short name:
SI-CLP
Gene namesi
Name:CHID1
ORF Names:GL008, PSEC0104, SB139
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:28474. CHID1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • late endosome Source: UniProtKB
  • lysosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi84 – 841Y → S: Significantly decreased carbohydrate binding. 1 Publication
Mutagenesisi88 – 881W → A: Significantly decreased carbohydrate binding. 1 Publication
Mutagenesisi110 – 1101W → A: Significantly decreased carbohydrate binding. 1 Publication
Mutagenesisi261 – 2611Y → S: Significantly decreased carbohydrate binding. 1 Publication
Mutagenesisi277 – 2771W → A: No noticeable effect. 1 Publication
Mutagenesisi302 – 3021Y → S: Significantly decreased carbohydrate binding. 1 Publication

Organism-specific databases

PharmGKBiPA142672118.

Polymorphism and mutation databases

BioMutaiCHID1.
DMDMi74733460.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 393374Chitinase domain-containing protein 1PRO_0000280608Add
BLAST

Proteomic databases

EPDiQ9BWS9.
MaxQBiQ9BWS9.
PRIDEiQ9BWS9.
TopDownProteomicsiQ9BWS9-2. [Q9BWS9-2]

PTM databases

iPTMnetiQ9BWS9.
PhosphoSiteiQ9BWS9.

Expressioni

Tissue specificityi

Expressed in cells of monocytic, T, B and epithelial origin.2 Publications

Inductioni

Up-regulated by IL4/interleukin-4 and dexamethasone in the macrophages. Up-regulated by glucocorticoid.2 Publications

Gene expression databases

BgeeiQ9BWS9.
CleanExiHS_CHID1.
ExpressionAtlasiQ9BWS9. baseline and differential.
GenevisibleiQ9BWS9. HS.

Organism-specific databases

HPAiHPA039374.

Interactioni

Subunit structurei

Interacts with STAB1.1 Publication

Protein-protein interaction databases

BioGridi122451. 6 interactions.
IntActiQ9BWS9. 1 interaction.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 473Combined sources
Helixi57 – 637Combined sources
Turni70 – 734Combined sources
Beta strandi81 – 866Combined sources
Helixi91 – 999Combined sources
Helixi100 – 1023Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi111 – 1177Combined sources
Beta strandi120 – 1245Combined sources
Helixi126 – 1283Combined sources
Helixi131 – 14010Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi149 – 1524Combined sources
Helixi157 – 1648Combined sources
Helixi167 – 18418Combined sources
Beta strandi188 – 1925Combined sources
Helixi194 – 1963Combined sources
Helixi202 – 21817Combined sources
Beta strandi222 – 2276Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 2383Combined sources
Helixi243 – 2497Combined sources
Turni250 – 2523Combined sources
Beta strandi254 – 2585Combined sources
Helixi275 – 28511Combined sources
Helixi292 – 2943Combined sources
Beta strandi295 – 30713Combined sources
Turni308 – 3114Combined sources
Beta strandi312 – 3165Combined sources
Helixi318 – 32811Combined sources
Beta strandi333 – 3353Combined sources
Turni336 – 3394Combined sources
Beta strandi340 – 3478Combined sources
Turni348 – 3503Combined sources
Beta strandi351 – 3566Combined sources
Helixi360 – 37314Combined sources
Beta strandi376 – 3805Combined sources
Helixi387 – 3926Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BXWX-ray2.70A/B1-393[»]
ProteinModelPortaliQ9BWS9.
SMRiQ9BWS9. Positions 33-393.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BWS9.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00390000012069.
HOVERGENiHBG055278.
InParanoidiQ9BWS9.
KOiK17525.
OMAiYSINERI.
OrthoDBiEOG75J0N4.
PhylomeDBiQ9BWS9.
TreeFamiTF319271.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BWS9-1) [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
MRTLFNLLWL ALACSPVHTT LSKSDAKKAA SKTLLEKSQF SDKPVQDRGL
60 70 80 90 100
VVTDLKAESV VLEHRSYCSA KARDRHFAGD VLGYVTPWNS HGYDVTKVFG
110 120 130 140 150
SKFTQISPVW LQLKRRGREM FEVTGLHDVD QGWMRAVRKH AKGLHIVPRL
160 170 180 190 200
LFEDWTYDDF RNVLDSEDEI EELSKTVVQV AKNQHFDGFV VEVWNQLLSQ
210 220 230 240 250
KRVGLIHMLT HLAEALHQAR LLALLVIPPA ITPGTDQLGM FTHKEFEQLA
260 270 280 290 300
PVLDGFSLMT YDYSTAHQPG PNAPLSWVRA CVQVLDPKSK WRSKILLGLN
310 320 330 340 350
FYGMDYATSK DAREPVVGAR YIQTLKDHRP RMVWDSQASE HFFEYKKSRS
360 370 380 390
GRHVVFYPTL KSLQVRLELA RELGVGVSIW ELGQGLDYFY DLL
Length:393
Mass (Da):44,941
Last modified:June 1, 2001 - v1
Checksum:iFFD5E67C20AF69B4
GO
Isoform 2 (identifier: Q9BWS9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-37: K → KVKFCSCCPGWSAMARSWLTATSATQ

Show »
Length:418
Mass (Da):47,616
Checksum:iD8591C41BF31FB5D
GO
Isoform 3 (identifier: Q9BWS9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     204-234: Missing.

Show »
Length:362
Mass (Da):41,678
Checksum:i5C0F15F14D50CFF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti335 – 3351D → G in BAB55316 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti331 – 3311R → Q.1 Publication
Corresponds to variant rs1127800 [ dbSNP | Ensembl ].
VAR_031173
Natural varianti338 – 3381A → V.3 Publications
Corresponds to variant rs6682 [ dbSNP | Ensembl ].
VAR_031174

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei37 – 371K → KVKFCSCCPGWSAMARSWLT ATSATQ in isoform 2. 1 PublicationVSP_023825
Alternative sequencei204 – 23431Missing in isoform 3. 1 PublicationVSP_023826Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BN000479 mRNA. Translation: CAF32458.1.
AF212229 mRNA. Translation: AAK14915.1.
AY037151 mRNA. Translation: AAK67632.1.
AK027711 mRNA. Translation: BAB55316.1.
AK075413 mRNA. Translation: BAC11603.1.
AK124697 mRNA. Translation: BAG54072.1.
BC000001 mRNA. Translation: AAH00001.1.
BC013642 mRNA. Translation: AAH13642.1.
BC095409 mRNA. Translation: AAH95409.1.
CCDSiCCDS44510.1. [Q9BWS9-3]
CCDS44511.1. [Q9BWS9-2]
CCDS7722.1. [Q9BWS9-1]
RefSeqiNP_001136146.1. NM_001142674.1. [Q9BWS9-1]
NP_001136147.1. NM_001142675.1. [Q9BWS9-1]
NP_001136148.1. NM_001142676.1. [Q9BWS9-2]
NP_001136149.1. NM_001142677.1. [Q9BWS9-3]
NP_076436.3. NM_023947.3. [Q9BWS9-1]
XP_005253130.1. XM_005253073.3. [Q9BWS9-3]
XP_006718345.1. XM_006718282.2. [Q9BWS9-1]
UniGeneiHs.144468.

Genome annotation databases

EnsembliENST00000323578; ENSP00000325055; ENSG00000177830. [Q9BWS9-1]
ENST00000429789; ENSP00000416034; ENSG00000177830. [Q9BWS9-3]
ENST00000436108; ENSP00000388156; ENSG00000177830. [Q9BWS9-1]
ENST00000449825; ENSP00000391255; ENSG00000177830. [Q9BWS9-1]
ENST00000454838; ENSP00000398722; ENSG00000177830. [Q9BWS9-2]
ENST00000528581; ENSP00000435503; ENSG00000177830. [Q9BWS9-2]
GeneIDi66005.
KEGGihsa:66005.
UCSCiuc001lsm.4. human. [Q9BWS9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BN000479 mRNA. Translation: CAF32458.1.
AF212229 mRNA. Translation: AAK14915.1.
AY037151 mRNA. Translation: AAK67632.1.
AK027711 mRNA. Translation: BAB55316.1.
AK075413 mRNA. Translation: BAC11603.1.
AK124697 mRNA. Translation: BAG54072.1.
BC000001 mRNA. Translation: AAH00001.1.
BC013642 mRNA. Translation: AAH13642.1.
BC095409 mRNA. Translation: AAH95409.1.
CCDSiCCDS44510.1. [Q9BWS9-3]
CCDS44511.1. [Q9BWS9-2]
CCDS7722.1. [Q9BWS9-1]
RefSeqiNP_001136146.1. NM_001142674.1. [Q9BWS9-1]
NP_001136147.1. NM_001142675.1. [Q9BWS9-1]
NP_001136148.1. NM_001142676.1. [Q9BWS9-2]
NP_001136149.1. NM_001142677.1. [Q9BWS9-3]
NP_076436.3. NM_023947.3. [Q9BWS9-1]
XP_005253130.1. XM_005253073.3. [Q9BWS9-3]
XP_006718345.1. XM_006718282.2. [Q9BWS9-1]
UniGeneiHs.144468.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BXWX-ray2.70A/B1-393[»]
ProteinModelPortaliQ9BWS9.
SMRiQ9BWS9. Positions 33-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122451. 6 interactions.
IntActiQ9BWS9. 1 interaction.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

PTM databases

iPTMnetiQ9BWS9.
PhosphoSiteiQ9BWS9.

Polymorphism and mutation databases

BioMutaiCHID1.
DMDMi74733460.

Proteomic databases

EPDiQ9BWS9.
MaxQBiQ9BWS9.
PRIDEiQ9BWS9.
TopDownProteomicsiQ9BWS9-2. [Q9BWS9-2]

Protocols and materials databases

DNASUi66005.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323578; ENSP00000325055; ENSG00000177830. [Q9BWS9-1]
ENST00000429789; ENSP00000416034; ENSG00000177830. [Q9BWS9-3]
ENST00000436108; ENSP00000388156; ENSG00000177830. [Q9BWS9-1]
ENST00000449825; ENSP00000391255; ENSG00000177830. [Q9BWS9-1]
ENST00000454838; ENSP00000398722; ENSG00000177830. [Q9BWS9-2]
ENST00000528581; ENSP00000435503; ENSG00000177830. [Q9BWS9-2]
GeneIDi66005.
KEGGihsa:66005.
UCSCiuc001lsm.4. human. [Q9BWS9-1]

Organism-specific databases

CTDi66005.
GeneCardsiCHID1.
HGNCiHGNC:28474. CHID1.
HPAiHPA039374.
MIMi615692. gene.
neXtProtiNX_Q9BWS9.
PharmGKBiPA142672118.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000012069.
HOVERGENiHBG055278.
InParanoidiQ9BWS9.
KOiK17525.
OMAiYSINERI.
OrthoDBiEOG75J0N4.
PhylomeDBiQ9BWS9.
TreeFamiTF319271.

Miscellaneous databases

ChiTaRSiCHID1. human.
EvolutionaryTraceiQ9BWS9.
GenomeRNAii66005.
PROiQ9BWS9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BWS9.
CleanExiHS_CHID1.
ExpressionAtlasiQ9BWS9. baseline and differential.
GenevisibleiQ9BWS9. HS.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel stabilin-1 interacting chitinase-like protein (SI-CLP) is up-regulated in alternatively activated macrophages and secreted via lysosomal pathway."
    Kzhyshkowska J., Mamidi S., Gratchev A., Kremmer E., Schmuttermaier C., Krusell L., Haus G., Utikal J., Schledzewski K., Scholtze J., Goerdt S.
    Blood 107:3221-3228(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAB1, TISSUE SPECIFICITY.
  2. "A novel gene expressed in human liver non-tumor tissues."
    Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-338.
    Tissue: Liver.
  3. Li N., Wan T., Zhang W., Cao X.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  4. "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), VARIANT VAL-338.
    Tissue: Amygdala.
  5. "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 2).
    Tissue: Teratocarcinoma.
  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), VARIANTS GLN-331 AND VAL-338.
    Tissue: Brain and Placenta.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Structure of human stabilin-1 interacting chitinase-like protein (SI-CLP) reveals a saccharide-binding cleft with lower sugar-binding selectivity."
    Meng G., Zhao Y., Bai X., Liu Y., Green T.J., Luo M., Zheng X.
    J. Biol. Chem. 285:39898-39904(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF TYR-84; TRP-88; TRP-110; TYR-261; TRP-277 AND TYR-302, FUNCTION.

Entry informationi

Entry nameiCHID1_HUMAN
AccessioniPrimary (citable) accession number: Q9BWS9
Secondary accession number(s): B3KWB0
, Q8NBM9, Q96CZ3, Q96S93, Q96SK0, Q9BY52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 117 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.