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

Neutral cholesterol ester hydrolase 1

Gene

NCEH1

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

Functioni

Hydrolyzes 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor. May be responsible for cholesterol ester hydrolysis in macrophages, thereby contributing to the development of atherosclerosis. Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds. May contribute to cancer pathogenesis by promoting tumor cell migration.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei191 – 1911PROSITE-ProRule annotation
Active sitei348 – 3481PROSITE-ProRule annotation
Active sitei378 – 3781PROSITE-ProRule annotation

GO - Molecular functioni

  1. carboxylic ester hydrolase activity Source: InterPro

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Protein family/group databases

MEROPSiS09.992.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral cholesterol ester hydrolase 1 (EC:3.1.1.-)
Short name:
NCEH
Alternative name(s):
Arylacetamide deacetylase-like 1
Gene namesi
Name:NCEH1
Synonyms:AADACL1, KIAA1363
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:29260. NCEH1.

Subcellular locationi

Membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Microsome By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence Analysis
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini26 – 408383LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165697847.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 408408Neutral cholesterol ester hydrolase 1PRO_0000265939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi287 – 2871N-linked (GlcNAc...)1 Publication
Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ6PIU2.
PaxDbiQ6PIU2.
PRIDEiQ6PIU2.

PTM databases

PhosphoSiteiQ6PIU2.

Expressioni

Tissue specificityi

Expressed in monocyte-derived macrophages. Up-regulated in invasive melanoma and breast carcinoma cell lines.2 Publications

Gene expression databases

BgeeiQ6PIU2.
CleanExiHS_AADACL1.
ExpressionAtlasiQ6PIU2. baseline and differential.
GenevestigatoriQ6PIU2.

Organism-specific databases

HPAiHPA026888.

Interactioni

Protein-protein interaction databases

BioGridi121608. 5 interactions.
IntActiQ6PIU2. 1 interaction.
STRINGi9606.ENSP00000273512.

Structurei

3D structure databases

ProteinModelPortaliQ6PIU2.
SMRiQ6PIU2. Positions 90-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi113 – 1153Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0657.
GeneTreeiENSGT00550000074556.
HOVERGENiHBG058974.
InParanoidiQ6PIU2.
KOiK14349.
OrthoDBiEOG7HB599.
PhylomeDBiQ6PIU2.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR002168. Lipase_GDXG_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
[Graphical view]
PIRSFiPIRSF037251. Arylacetamide_deacetylase. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q6PIU2-1) [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
MRSSCVLLTA LVALAAYYVY IPLPGSVSDP WKLMLLDATF RGAQQVSNLI
60 70 80 90 100
HYLGLSHHLL ALNFIIVSFG KKSAWSSAQV KVTDTDFDGV EVRVFEGPPK
110 120 130 140 150
PEEPLKRSVV YIHGGGWALA SAKIRYYDEL CTAMAEELNA VIVSIEYRLV
160 170 180 190 200
PKVYFPEQIH DVVRATKYFL KPEVLQKYMV DPGRICISGD SAGGNLAAAL
210 220 230 240 250
GQQFTQDASL KNKLKLQALI YPVLQALDFN TPSYQQNVNT PILPRYVMVK
260 270 280 290 300
YWVDYFKGNY DFVQAMIVNN HTSLDVEEAA AVRARLNWTS LLPASFTKNY
310 320 330 340 350
KPVVQTTGNA RIVQELPQLL DARSAPLIAD QAVLQLLPKT YILTCEHDVL
360 370 380 390 400
RDDGIMYAKR LESAGVEVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRNSY

IKWLDQNL
Length:408
Mass (Da):45,808
Last modified:December 12, 2006 - v3
Checksum:iE5754850BE9805B5
GO
Isoform 2 (identifier: Q6PIU2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-123: K → SASWSPSDE

Show »
Length:416
Mass (Da):46,627
Checksum:iA315923F59D660E7
GO
Isoform 3 (identifier: Q6PIU2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Show »
Length:275
Mass (Da):31,168
Checksum:i1D5212243D62F48B
GO

Sequence cautioni

The sequence AAH28734.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH47588.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AC007919 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AC069237 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA92601.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAH13028.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAH14142.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAH14802.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161A → T in BAA92601 (PubMed:10718198).Curated
Sequence conflicti58 – 581H → R in BAH13028 (PubMed:14702039).Curated
Sequence conflicti72 – 721K → R in BAH14802 (PubMed:14702039).Curated
Sequence conflicti79 – 791Q → K in AAH47588 (PubMed:15489334).Curated
Sequence conflicti254 – 2541D → G in BAH14142 (PubMed:14702039).Curated
Sequence conflicti329 – 3291A → S in BAH14142 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191V → F.
Corresponds to variant rs35316420 [ dbSNP | Ensembl ].
VAR_047099
Natural varianti71 – 711K → Q.
Corresponds to variant rs2302815 [ dbSNP | Ensembl ].
VAR_047100
Natural varianti343 – 3431L → M.1 Publication
Corresponds to variant rs17857335 [ dbSNP | Ensembl ].
VAR_047101

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 133133Missing in isoform 3. 1 PublicationVSP_037518Add
BLAST
Alternative sequencei123 – 1231K → SASWSPSDE in isoform 2. 1 PublicationVSP_037519

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037784 mRNA. Translation: BAA92601.1. Different initiation.
AK294811 mRNA. Translation: BAH11890.1.
AK295641 mRNA. Translation: BAH12137.1.
AK299422 mRNA. Translation: BAH13028.1. Different initiation.
AK304253 mRNA. Translation: BAH14142.1. Different initiation.
AK316431 mRNA. Translation: BAH14802.1. Different initiation.
AC007919 Genomic DNA. No translation available.
AC069237 Genomic DNA. No translation available.
BC028734 mRNA. Translation: AAH28734.2. Different initiation.
BC047588 mRNA. Translation: AAH47588.2. Different initiation.
CCDSiCCDS54681.1. [Q6PIU2-3]
RefSeqiNP_001139748.1. NM_001146276.1.
NP_001139749.1. NM_001146277.1. [Q6PIU2-3]
NP_001139750.1. NM_001146278.1. [Q6PIU2-3]
NP_065843.3. NM_020792.4.
UniGeneiHs.444099.

Genome annotation databases

EnsembliENST00000475381; ENSP00000418571; ENSG00000144959. [Q6PIU2-1]
ENST00000543711; ENSP00000443227; ENSG00000144959. [Q6PIU2-3]
GeneIDi57552.
KEGGihsa:57552.
UCSCiuc011bpw.2. human. [Q6PIU2-1]
uc011bpx.2. human.

Polymorphism databases

DMDMi74737782.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037784 mRNA. Translation: BAA92601.1. Different initiation.
AK294811 mRNA. Translation: BAH11890.1.
AK295641 mRNA. Translation: BAH12137.1.
AK299422 mRNA. Translation: BAH13028.1. Different initiation.
AK304253 mRNA. Translation: BAH14142.1. Different initiation.
AK316431 mRNA. Translation: BAH14802.1. Different initiation.
AC007919 Genomic DNA. No translation available.
AC069237 Genomic DNA. No translation available.
BC028734 mRNA. Translation: AAH28734.2. Different initiation.
BC047588 mRNA. Translation: AAH47588.2. Different initiation.
CCDSiCCDS54681.1. [Q6PIU2-3]
RefSeqiNP_001139748.1. NM_001146276.1.
NP_001139749.1. NM_001146277.1. [Q6PIU2-3]
NP_001139750.1. NM_001146278.1. [Q6PIU2-3]
NP_065843.3. NM_020792.4.
UniGeneiHs.444099.

3D structure databases

ProteinModelPortaliQ6PIU2.
SMRiQ6PIU2. Positions 90-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121608. 5 interactions.
IntActiQ6PIU2. 1 interaction.
STRINGi9606.ENSP00000273512.

Chemistry

BindingDBiQ6PIU2.
ChEMBLiCHEMBL5048.

Protein family/group databases

MEROPSiS09.992.

PTM databases

PhosphoSiteiQ6PIU2.

Polymorphism databases

DMDMi74737782.

Proteomic databases

MaxQBiQ6PIU2.
PaxDbiQ6PIU2.
PRIDEiQ6PIU2.

Protocols and materials databases

DNASUi57552.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000475381; ENSP00000418571; ENSG00000144959. [Q6PIU2-1]
ENST00000543711; ENSP00000443227; ENSG00000144959. [Q6PIU2-3]
GeneIDi57552.
KEGGihsa:57552.
UCSCiuc011bpw.2. human. [Q6PIU2-1]
uc011bpx.2. human.

Organism-specific databases

CTDi57552.
GeneCardsiGC03M172348.
H-InvDBHIX0003864.
HIX0163448.
HGNCiHGNC:29260. NCEH1.
HPAiHPA026888.
MIMi613234. gene.
neXtProtiNX_Q6PIU2.
PharmGKBiPA165697847.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0657.
GeneTreeiENSGT00550000074556.
HOVERGENiHBG058974.
InParanoidiQ6PIU2.
KOiK14349.
OrthoDBiEOG7HB599.
PhylomeDBiQ6PIU2.

Miscellaneous databases

ChiTaRSiNCEH1. human.
GeneWikiiNCEH1.
GenomeRNAii57552.
NextBioi64018.
PROiQ6PIU2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PIU2.
CleanExiHS_AADACL1.
ExpressionAtlasiQ6PIU2. baseline and differential.
GenevestigatoriQ6PIU2.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR002168. Lipase_GDXG_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
[Graphical view]
PIRSFiPIRSF037251. Arylacetamide_deacetylase. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: 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; 2 AND 3).
    Tissue: Brain, Hippocampus, Testis, Tongue and Trachea.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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), VARIANT MET-343.
    Tissue: Brain.
  5. "Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness."
    Jessani N., Liu Y., Humphrey M., Cravatt B.F.
    Proc. Natl. Acad. Sci. U.S.A. 99:10335-10340(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION.
  6. "An enzyme that regulates ether lipid signaling pathways in cancer annotated by multidimensional profiling."
    Chiang K.P., Niessen S., Saghatelian A., Cravatt B.F.
    Chem. Biol. 13:1041-1050(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: TISSUE SPECIFICITY.
  8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-287.
    Tissue: Liver.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNCEH1_HUMAN
AccessioniPrimary (citable) accession number: Q6PIU2
Secondary accession number(s): B7Z2K4
, B7Z3A1, B7Z5U2, B7Z906, B7ZAW6, F5H7K4, Q86WZ1, Q9P2I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: March 4, 2015
This is version 98 of the entry and version 3 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 3
    Human chromosome 3: 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

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.