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Protein

Echinoderm microtubule-associated protein-like 2

Gene

EML2

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

Functioni

Tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules.1 Publication

GO - Molecular functioni

  1. microtubule binding Source: UniProtKB
  2. tubulin binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of microtubule polymerization Source: UniProtKB
  2. regulation of microtubule nucleation Source: UniProtKB
  3. sensory perception of sound Source: ProtInc
  4. visual perception Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiO95834.

Names & Taxonomyi

Protein namesi
Recommended name:
Echinoderm microtubule-associated protein-like 2
Short name:
EMAP-2
Short name:
HuEMAP-2
Gene namesi
Name:EML2
Synonyms:EMAP2, EMAPL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:18035. EML2.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication
Note: Colocalizes with the microtubule cytoskeleton. Colocalizes with the mitotic spindle.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. microtubule Source: UniProtKB-KW
  3. microtubule associated complex Source: ProtInc
  4. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27768.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 649649Echinoderm microtubule-associated protein-like 2PRO_0000050962Add
BLAST

Proteomic databases

MaxQBiO95834.
PaxDbiO95834.
PRIDEiO95834.

PTM databases

PhosphoSiteiO95834.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiO95834.
CleanExiHS_EML2.
ExpressionAtlasiO95834. baseline and differential.
GenevestigatoriO95834.

Organism-specific databases

HPAiHPA012757.

Interactioni

Subunit structurei

Interacts with GRID2 and may also interact with GRID1 (By similarity). Binds unpolymerized tubulins via its WD repeat region.By similarity2 Publications

Protein-protein interaction databases

BioGridi117290. 8 interactions.
MINTiMINT-4527842.

Structurei

Secondary structure

1
649
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 5541Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CGBX-ray2.15A/B/C/D/E/F11-60[»]
ProteinModelPortaliO95834.
SMRiO95834. Positions 10-649.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati103 – 15250WD 1Add
BLAST
Repeati157 – 20044WD 2Add
BLAST
Repeati203 – 24240WD 3Add
BLAST
Repeati250 – 28839WD 4Add
BLAST
Repeati292 – 33140WD 5Add
BLAST
Repeati375 – 41440WD 6Add
BLAST
Repeati416 – 45540WD 7Add
BLAST
Repeati458 – 49740WD 8Add
BLAST
Repeati504 – 54340WD 9Add
BLAST
Repeati571 – 61040WD 10Add
BLAST
Repeati616 – 64833WD 11Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 649640Tandem atypical propeller in EMLsBy similarityAdd
BLAST

Domaini

Contains a tandem atypical propeller in EMLs (TAPE) domain. The N-terminal beta-propeller is formed by canonical WD repeats; in contrast, the second beta-propeller contains one blade that is formed by discontinuous parts of the polypeptide chain (By similarity).By similarity

Sequence similaritiesi

Belongs to the WD repeat EMAP family.Curated
Contains 11 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00550000074369.
HOVERGENiHBG051470.
InParanoidiO95834.
KOiK18595.
OMAiDDANDHI.
PhylomeDBiO95834.
TreeFamiTF317832.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR005108. HELP.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF03451. HELP. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
SMARTiSM00320. WD40. 11 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF50998. SSF50998. 3 hits.
PROSITEiPS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 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: O95834-1) [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
MSSFGAGKTK EVIFSVEDGS VKMFLRGRPV PMMIPDELAP TYSLDTRSEL
60 70 80 90 100
PSCRLKLEWV YGYRGRDCRA NLYLLPTGEI VYFVASVAVL YSVEEQRQRH
110 120 130 140 150
YLGHNDDIKC LAIHPDMVTI ATGQVAGTTK EGKPLPPHVR IWDSVSLSTL
160 170 180 190 200
HVLGLGVFDR AVCCVGFSKS NGGNLLCAVD ESNDHMLSVW DWAKETKVVD
210 220 230 240 250
VKCSNEAVLV ATFHPTDPTV LITCGKSHIY FWTLEGGSLS KRQGLFEKHE
260 270 280 290 300
KPKYVLCVTF LEGGDVVTGD SGGNLYVWGK GGNRITQAVL GAHDGGVFGL
310 320 330 340 350
CALRDGTLVS GGGRDRRVVL WGSDYSKLQE VEVPEDFGPV RTVAEGHGDT
360 370 380 390 400
LYVGTTRNSI LQGSVHTGFS LLVQGHVEEL WGLATHPSRA QFVTCGQDKL
410 420 430 440 450
VHLWSSDSHQ PLWSRIIEDP ARSAGFHPSG SVLAVGTVTG RWLLLDTETH
460 470 480 490 500
DLVAIHTDGN EQISVVSFSP DGAYLAVGSH DNLVYVYTVD QGGRKVSRLG
510 520 530 540 550
KCSGHSSFIT HLDWAQDSSC FVTNSGDYEI LYWDPATCKQ ITSADAVRNM
560 570 580 590 600
EWATATCVLG FGVFGIWSEG ADGTDINAVA RSHDGKLLAS ADDFGKVHLF
610 620 630 640
SYPCCQPRAL SHKYGGHSSH VTNVAFLWDD SMALTTGGKD TSVLQWRVV
Length:649
Mass (Da):70,679
Last modified:May 1, 1999 - v1
Checksum:iF356D3D974D208C9
GO
Isoform 2 (identifier: O95834-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MSSFGA → MSLDDNLSGT...SSSNCSAKKE

Note: No experimental confirmation available.

Show »
Length:796
Mass (Da):86,471
Checksum:i458459038BB78DE9
GO
Isoform 3 (identifier: O95834-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MSSFGA → MLERRALLWQ...SSSNCSAKKE

Note: No experimental confirmation available.

Show »
Length:850
Mass (Da):92,070
Checksum:i3314BC538A339D66
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti294 – 2941D → G in CAB46373 (PubMed:17974005).Curated
Sequence conflicti419 – 4279DPARSAGFH → MAAAGHGDP in AAH32630 (PubMed:17974005).Curated
Sequence conflicti582 – 5821S → F in CAB46373 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331M → V.
Corresponds to variant rs12151009 [ dbSNP | Ensembl ].
VAR_031723
Natural varianti187 – 1871L → F.
Corresponds to variant rs7252175 [ dbSNP | Ensembl ].
VAR_031724
Natural varianti235 – 2351E → D.1 Publication
Corresponds to variant rs1545040 [ dbSNP | Ensembl ].
VAR_024697
Natural varianti357 – 3571R → H.
Corresponds to variant rs3816045 [ dbSNP | Ensembl ].
VAR_022026
Natural varianti484 – 4841V → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035879

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66MSSFGA → MSLDDNLSGTSGMEVDDRVS ALEQRLQLQEDELAVLKAAL ADALRRLRACEEQGAALRAR GTPKGRAPPRLGTTASVCQL LKGLPTRTPLNGSGPPRRVG GYATSPSSPKKEATSGRSSV RRYLSPERLASVRREDPRSR TTSSSSNCSAKKE in isoform 2. 1 PublicationVSP_042541
Alternative sequencei1 – 66MSSFGA → MLERRALLWQREAGPGWGDR ARAGTGGAGGGCGGAMAERG PAFCGLYDTSSLLRYCNDDN LSGTSGMEVDDRVSALEQRL QLQEDELAVLKAALADALRR LRACEEQGAALRARGTPKGR APPRLGTTASVCQLLKGLPT RTPLNGSGPPRRVGGYATSP SSPKKEATSGRSSVRRYLSP ERLASVRREDPRSRTTSSSS NCSAKKE in isoform 3. 1 PublicationVSP_047538

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF103939 mRNA. Translation: AAD19904.1.
AL096717 mRNA. Translation: CAB46373.2.
AK295905 mRNA. Translation: BAH12218.1.
AK296258 mRNA. Translation: BAH12295.1.
AC006132 Genomic DNA. No translation available.
AC011480 Genomic DNA. No translation available.
AC098776 Genomic DNA. No translation available.
BC032630 mRNA. Translation: AAH32630.1.
AB209773 mRNA. Translation: BAD93010.1.
CCDSiCCDS12670.1. [O95834-1]
CCDS54280.1. [O95834-2]
CCDS59399.1. [O95834-3]
RefSeqiNP_001180197.1. NM_001193268.1. [O95834-3]
NP_001180198.1. NM_001193269.1. [O95834-2]
NP_036287.1. NM_012155.2. [O95834-1]
UniGeneiHs.24178.

Genome annotation databases

EnsembliENST00000245925; ENSP00000245925; ENSG00000125746. [O95834-1]
ENST00000536630; ENSP00000442365; ENSG00000125746. [O95834-2]
ENST00000587152; ENSP00000468312; ENSG00000125746. [O95834-3]
GeneIDi24139.
KEGGihsa:24139.
UCSCiuc002pcn.3. human. [O95834-1]
uc010xxl.2. human. [O95834-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF103939 mRNA. Translation: AAD19904.1.
AL096717 mRNA. Translation: CAB46373.2.
AK295905 mRNA. Translation: BAH12218.1.
AK296258 mRNA. Translation: BAH12295.1.
AC006132 Genomic DNA. No translation available.
AC011480 Genomic DNA. No translation available.
AC098776 Genomic DNA. No translation available.
BC032630 mRNA. Translation: AAH32630.1.
AB209773 mRNA. Translation: BAD93010.1.
CCDSiCCDS12670.1. [O95834-1]
CCDS54280.1. [O95834-2]
CCDS59399.1. [O95834-3]
RefSeqiNP_001180197.1. NM_001193268.1. [O95834-3]
NP_001180198.1. NM_001193269.1. [O95834-2]
NP_036287.1. NM_012155.2. [O95834-1]
UniGeneiHs.24178.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CGBX-ray2.15A/B/C/D/E/F11-60[»]
ProteinModelPortaliO95834.
SMRiO95834. Positions 10-649.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117290. 8 interactions.
MINTiMINT-4527842.

PTM databases

PhosphoSiteiO95834.

Proteomic databases

MaxQBiO95834.
PaxDbiO95834.
PRIDEiO95834.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000245925; ENSP00000245925; ENSG00000125746. [O95834-1]
ENST00000536630; ENSP00000442365; ENSG00000125746. [O95834-2]
ENST00000587152; ENSP00000468312; ENSG00000125746. [O95834-3]
GeneIDi24139.
KEGGihsa:24139.
UCSCiuc002pcn.3. human. [O95834-1]
uc010xxl.2. human. [O95834-2]

Organism-specific databases

CTDi24139.
GeneCardsiGC19M046112.
HGNCiHGNC:18035. EML2.
HPAiHPA012757.
neXtProtiNX_O95834.
PharmGKBiPA27768.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00550000074369.
HOVERGENiHBG051470.
InParanoidiO95834.
KOiK18595.
OMAiDDANDHI.
PhylomeDBiO95834.
TreeFamiTF317832.

Enzyme and pathway databases

SignaLinkiO95834.

Miscellaneous databases

ChiTaRSiEML2. human.
GenomeRNAii24139.
NextBioi46809.
PROiO95834.

Gene expression databases

BgeeiO95834.
CleanExiHS_EML2.
ExpressionAtlasiO95834. baseline and differential.
GenevestigatoriO95834.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR005108. HELP.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF03451. HELP. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
SMARTiSM00320. WD40. 11 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF50998. SSF50998. 3 hits.
PROSITEiPS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and expression patterns of a human EMAP-related protein-2 (HuEMAP-2)."
    Lepley D.M., Palange J.M., Suprenant K.A.
    Gene 237:343-349(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Placenta.
  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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-850 (ISOFORM 3).
    Tissue: Substantia nigra and Thalamus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    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] OF 1-427 (ISOFORM 1).
    Tissue: Liver.
  6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-649 (ISOFORM 1), VARIANT ASP-235.
    Tissue: Brain.
  7. "The human EMAP-like protein-70 (ELP70) is a microtubule destabilizer that localizes to the mitotic apparatus."
    Eichenmuller B., Everley P., Palange J., Lepley D., Suprenant K.A.
    J. Biol. Chem. 277:1301-1309(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TUBULIN, SUBCELLULAR LOCATION.
  8. "Crystal structure of EML1 reveals the basis for Hsp90 dependence of oncogenic EML4-ALK by disruption of an atypical ?-propeller domain."
    Richards M.W., Law E.W., Rennalls L.P., Busacca S., O'Regan L., Fry A.M., Fennell D.A., Bayliss R.
    Proc. Natl. Acad. Sci. U.S.A. 111:5195-5200(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TUBULIN.
  9. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-484.

Entry informationi

Entry nameiEMAL2_HUMAN
AccessioniPrimary (citable) accession number: O95834
Secondary accession number(s): B7Z3I2
, B7Z3Q9, K7ERL7, Q59EN8, Q8N5A2, Q9UG50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 1999
Last modified: March 4, 2015
This is version 131 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. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.