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Q9Y316

- MEMO1_HUMAN

UniProt

Q9Y316 - MEMO1_HUMAN

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Protein

Protein MEMO1

Gene

MEMO1

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

Functioni

May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Is required for breast carcinoma cell migration.2 Publications

GO - Biological processi

  1. regulation of microtubule-based process Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Protein MEMO1
Alternative name(s):
C21orf19-like protein
Hepatitis C virus NS5A-transactivated protein 7
Short name:
HCV NS5A-transactivated protein 7
Mediator of ErbB2-driven cell motility 1
Short name:
Mediator of cell motility 1
Short name:
Memo-1
Gene namesi
Name:MEMO1
Synonyms:C2orf4, MEMO, NS5ATP7
ORF Names:CGI-27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:14014. MEMO1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161W → A: Abolishes interaction with ERBB2. 1 Publication
Mutagenesisi49 – 491H → A: Abolishes interaction with ERBB2. 1 Publication
Mutagenesisi54 – 541Y → A: Diminishes interaction with ERBB2. 1 Publication
Mutagenesisi81 – 811H → A: Abolishes interaction with ERBB2. 1 Publication
Mutagenesisi192 – 1921H → A: Abolishes interaction with ERBB2. 1 Publication
Mutagenesisi244 – 2441C → A: Abolishes interaction with ERBB2. 1 Publication

Organism-specific databases

PharmGKBiPA162395745.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297Protein MEMO1PRO_0000134394Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y316.
PaxDbiQ9Y316.
PRIDEiQ9Y316.

PTM databases

PhosphoSiteiQ9Y316.

Expressioni

Gene expression databases

BgeeiQ9Y316.
CleanExiHS_MEMO1.
ExpressionAtlasiQ9Y316. baseline.
GenevestigatoriQ9Y316.

Organism-specific databases

HPAiHPA042603.

Interactioni

Subunit structurei

Interacts with ERBB2 phosphorylated on 'Tyr-1248'.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERBB2P046266EBI-1104564,EBI-641062

Protein-protein interaction databases

BioGridi119263. 15 interactions.
IntActiQ9Y316. 4 interactions.
MINTiMINT-3085289.
STRINGi9606.ENSP00000295065.

Structurei

Secondary structure

1
297
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 155
Helixi21 – 3212
Beta strandi43 – 475
Helixi52 – 6312
Turni68 – 703
Beta strandi73 – 797
Beta strandi81 – 833
Beta strandi86 – 905
Beta strandi94 – 963
Beta strandi103 – 1053
Helixi107 – 1159
Beta strandi119 – 1213
Helixi124 – 1296
Helixi134 – 1363
Helixi137 – 1437
Helixi145 – 1473
Beta strandi152 – 1587
Helixi163 – 17715
Beta strandi182 – 1876
Beta strandi192 – 1943
Helixi195 – 1973
Helixi204 – 2063
Helixi209 – 22517
Helixi229 – 23911
Helixi246 – 26116
Beta strandi266 – 27712
Beta strandi286 – 29611

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BCZX-ray2.10A/B/C/D5-297[»]
3BD0X-ray3.01A/B/C/D5-297[»]
ProteinModelPortaliQ9Y316.
SMRiQ9Y316. Positions 5-297.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y316.

Family & Domainsi

Sequence similaritiesi

Belongs to the MEMO1 family.Curated

Phylogenomic databases

eggNOGiCOG1355.
GeneTreeiENSGT00390000006408.
HOGENOMiHOG000225260.
HOVERGENiHBG050811.
InParanoidiQ9Y316.
KOiK06990.
OMAiEHSLEMH.
OrthoDBiEOG7FFMS1.
PhylomeDBiQ9Y316.
TreeFamiTF300014.

Family and domain databases

HAMAPiMF_00055. MEMO1.
InterProiIPR002737. MEMO1_fam.
[Graphical view]
PANTHERiPTHR11060. PTHR11060. 1 hit.
PfamiPF01875. Memo. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04336. AmmeMemoSam_B. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y316-1) [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
MSNRVVCREA SHAGSWYTAS GPQLNAQLEG WLSQVQSTKR PARAIIAPHA
60 70 80 90 100
GYTYCGSCAA HAYKQVDPSI TRRIFILGPS HHVPLSRCAL SSVDIYRTPL
110 120 130 140 150
YDLRIDQKIY GELWKTGMFE RMSLQTDEDE HSIEMHLPYT AKAMESHKDE
160 170 180 190 200
FTIIPVLVGA LSESKEQEFG KLFSKYLADP SNLFVVSSDF CHWGQRFRYS
210 220 230 240 250
YYDESQGEIY RSIEHLDKMG MSIIEQLDPV SFSNYLKKYH NTICGRHPIG
260 270 280 290
VLLNAITELQ KNGMNMSFSF LNYAQSSQCR NWQDSSVSYA AGALTVH
Length:297
Mass (Da):33,733
Last modified:November 1, 1999 - v1
Checksum:iE315FD5587776211
GO
Isoform 2 (identifier: Q9Y316-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     49-71: Missing.

Show »
Length:274
Mass (Da):31,307
Checksum:i1BE5B4A07A5D44D8
GO
Isoform 3 (identifier: Q9Y316-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MSNRVVCREASHAGSWYTAS → MPLWRADKCQDVQSASWRPRRAD

Show »
Length:300
Mass (Da):34,294
Checksum:i0778186B7CCA0ADA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231Q → H in AAH70046. (PubMed:15489334)Curated
Sequence conflicti172 – 1721L → P in BAG59632. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020MSNRV…WYTAS → MPLWRADKCQDVQSASWRPR RAD in isoform 3. 1 PublicationVSP_047693Add
BLAST
Alternative sequencei49 – 7123Missing in isoform 2. 1 PublicationVSP_041092Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF363446 mRNA. Translation: AAL34462.1.
AB041018 mRNA. Translation: BAD74066.1.
AB041019 mRNA. Translation: BAD74067.1.
AF529368 mRNA. Translation: AAQ09602.1.
AF132961 mRNA. Translation: AAD27736.1.
AK297128 mRNA. Translation: BAG59632.1.
AL121652 Genomic DNA. No translation available.
AL121655 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00467.1.
CH471053 Genomic DNA. Translation: EAX00469.1.
CH471053 Genomic DNA. Translation: EAX00470.1.
CH471053 Genomic DNA. Translation: EAX00472.1.
BC018733 mRNA. Translation: AAH18733.1.
BC070046 mRNA. Translation: AAH70046.1.
BC094681 mRNA. Translation: AAH94681.1.
CCDSiCCDS1776.1. [Q9Y316-1]
CCDS46255.1. [Q9Y316-2]
RefSeqiNP_001131074.1. NM_001137602.1. [Q9Y316-2]
NP_057039.1. NM_015955.2. [Q9Y316-1]
XP_005264408.1. XM_005264351.1. [Q9Y316-1]
UniGeneiHs.444969.

Genome annotation databases

EnsembliENST00000295065; ENSP00000295065; ENSG00000162959. [Q9Y316-1]
ENST00000379383; ENSP00000368691; ENSG00000162959. [Q9Y316-3]
ENST00000404530; ENSP00000385557; ENSG00000162959. [Q9Y316-1]
ENST00000426310; ENSP00000400795; ENSG00000162959. [Q9Y316-2]
GeneIDi51072.
KEGGihsa:51072.
UCSCiuc002rnx.3. human. [Q9Y316-1]
uc010ymu.2. human. [Q9Y316-2]

Polymorphism databases

DMDMi7388490.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF363446 mRNA. Translation: AAL34462.1 .
AB041018 mRNA. Translation: BAD74066.1 .
AB041019 mRNA. Translation: BAD74067.1 .
AF529368 mRNA. Translation: AAQ09602.1 .
AF132961 mRNA. Translation: AAD27736.1 .
AK297128 mRNA. Translation: BAG59632.1 .
AL121652 Genomic DNA. No translation available.
AL121655 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00467.1 .
CH471053 Genomic DNA. Translation: EAX00469.1 .
CH471053 Genomic DNA. Translation: EAX00470.1 .
CH471053 Genomic DNA. Translation: EAX00472.1 .
BC018733 mRNA. Translation: AAH18733.1 .
BC070046 mRNA. Translation: AAH70046.1 .
BC094681 mRNA. Translation: AAH94681.1 .
CCDSi CCDS1776.1. [Q9Y316-1 ]
CCDS46255.1. [Q9Y316-2 ]
RefSeqi NP_001131074.1. NM_001137602.1. [Q9Y316-2 ]
NP_057039.1. NM_015955.2. [Q9Y316-1 ]
XP_005264408.1. XM_005264351.1. [Q9Y316-1 ]
UniGenei Hs.444969.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BCZ X-ray 2.10 A/B/C/D 5-297 [» ]
3BD0 X-ray 3.01 A/B/C/D 5-297 [» ]
ProteinModelPortali Q9Y316.
SMRi Q9Y316. Positions 5-297.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119263. 15 interactions.
IntActi Q9Y316. 4 interactions.
MINTi MINT-3085289.
STRINGi 9606.ENSP00000295065.

PTM databases

PhosphoSitei Q9Y316.

Polymorphism databases

DMDMi 7388490.

Proteomic databases

MaxQBi Q9Y316.
PaxDbi Q9Y316.
PRIDEi Q9Y316.

Protocols and materials databases

DNASUi 51072.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295065 ; ENSP00000295065 ; ENSG00000162959 . [Q9Y316-1 ]
ENST00000379383 ; ENSP00000368691 ; ENSG00000162959 . [Q9Y316-3 ]
ENST00000404530 ; ENSP00000385557 ; ENSG00000162959 . [Q9Y316-1 ]
ENST00000426310 ; ENSP00000400795 ; ENSG00000162959 . [Q9Y316-2 ]
GeneIDi 51072.
KEGGi hsa:51072.
UCSCi uc002rnx.3. human. [Q9Y316-1 ]
uc010ymu.2. human. [Q9Y316-2 ]

Organism-specific databases

GeneCardsi GC02M032092.
HGNCi HGNC:14014. MEMO1.
HPAi HPA042603.
MIMi 611786. gene.
neXtProti NX_Q9Y316.
PharmGKBi PA162395745.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1355.
GeneTreei ENSGT00390000006408.
HOGENOMi HOG000225260.
HOVERGENi HBG050811.
InParanoidi Q9Y316.
KOi K06990.
OMAi EHSLEMH.
OrthoDBi EOG7FFMS1.
PhylomeDBi Q9Y316.
TreeFami TF300014.

Miscellaneous databases

ChiTaRSi MEMO1. human.
EvolutionaryTracei Q9Y316.
GenomeRNAii 51072.
NextBioi 53687.
PROi Q9Y316.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y316.
CleanExi HS_MEMO1.
ExpressionAtlasi Q9Y316. baseline.
Genevestigatori Q9Y316.

Family and domain databases

HAMAPi MF_00055. MEMO1.
InterProi IPR002737. MEMO1_fam.
[Graphical view ]
PANTHERi PTHR11060. PTHR11060. 1 hit.
Pfami PF01875. Memo. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR04336. AmmeMemoSam_B. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "From PREDs and open reading frames to cDNA isolation: revisiting the human chromosome 21 transcription map."
    Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S., Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.
    Genomics 78:46-54(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning of two isoforms of C2orf4 gene."
    Shibuya K., Kudoh J., Shimizu N.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
    Tissue: Heart and Skeletal muscle.
  3. "Cloning and identification of human gene 7 transactivated by hepatitis C virus NS5A protein."
    Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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).
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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).
    Tissue: B-cell, PNS and Testis.
  9. Cited for: FUNCTION, INTERACTION WITH ERBB2.
  10. "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
    Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
    Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-derived phosphopeptide in its vestigial active site."
    Qiu C., Lienhard S., Hynes N.E., Badache A., Leahy D.J.
    J. Biol. Chem. 283:2734-2740(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 5-297, INTERACTION WITH ERBB2, MUTAGENESIS OF TRP-16; HIS-49; TYR-54; HIS-81; HIS-192 AND CYS-244.

Entry informationi

Entry nameiMEMO1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y316
Secondary accession number(s): B4DLS0
, D6W575, Q5R2V8, Q5R2V9, Q6NSL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 122 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 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

External Data

Dasty 3