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Q96JB6

- LOXL4_HUMAN

UniProt

Q96JB6 - LOXL4_HUMAN

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Protein

Lysyl oxidase homolog 4

Gene

LOXL4

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

Functioni

May modulate the formation of a collagenous extracellular matrix.

Cofactori

Copper.By similarity
Contains 1 lysine tyrosylquinone.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi611 – 6111CopperSequence Analysis
Metal bindingi613 – 6131CopperSequence Analysis
Metal bindingi615 – 6151CopperSequence Analysis

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. protein-lysine 6-oxidase activity Source: Ensembl
  3. scavenger receptor activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_150206. Crosslinking of collagen fibrils.
REACT_150366. Elastic fibre formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysyl oxidase homolog 4 (EC:1.4.3.-)
Alternative name(s):
Lysyl oxidase-like protein 4
Lysyl oxidase-related protein C
Gene namesi
Name:LOXL4
Synonyms:LOXC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:17171. LOXL4.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. membrane Source: InterPro
  3. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30431.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 756732Lysyl oxidase homolog 4PRO_0000018535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 122PROSITE-ProRule annotation
Disulfide bondi71 ↔ 132PROSITE-ProRule annotation
Disulfide bondi102 ↔ 112PROSITE-ProRule annotation
Disulfide bondi191 ↔ 276PROSITE-ProRule annotation
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi204 ↔ 286PROSITE-ProRule annotation
Disulfide bondi251 ↔ 261PROSITE-ProRule annotation
Disulfide bondi336 ↔ 400PROSITE-ProRule annotation
Disulfide bondi349 ↔ 410PROSITE-ProRule annotation
Disulfide bondi380 ↔ 390PROSITE-ProRule annotation
Disulfide bondi450 ↔ 515PROSITE-ProRule annotation
Disulfide bondi463 ↔ 528PROSITE-ProRule annotation
Disulfide bondi497 ↔ 507PROSITE-ProRule annotation
Disulfide bondi558 ↔ 564PROSITE-ProRule annotation
Disulfide bondi610 ↔ 658PROSITE-ProRule annotation
Glycosylationi629 – 6291N-linked (GlcNAc...)Sequence Analysis
Cross-linki638 ↔ 674Lysine tyrosylquinone (Lys-Tyr)By similarity
Disulfide bondi642 ↔ 648PROSITE-ProRule annotation
Disulfide bondi670 ↔ 680PROSITE-ProRule annotation
Modified residuei674 – 67412',4',5'-topaquinoneBy similarity
Disulfide bondi717 ↔ 731PROSITE-ProRule annotation

Post-translational modificationi

The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.

Keywords - PTMi

Disulfide bond, Glycoprotein, LTQ, TPQ

Proteomic databases

MaxQBiQ96JB6.
PaxDbiQ96JB6.
PRIDEiQ96JB6.

PTM databases

PhosphoSiteiQ96JB6.

Expressioni

Tissue specificityi

Expressed in many tissues, the highest levels among the tissues studied being in the skeletal muscle, testis and pancreas. Expressed in cartilage.

Gene expression databases

BgeeiQ96JB6.
CleanExiHS_LOXL4.
GenevestigatoriQ96JB6.

Organism-specific databases

HPAiCAB033876.
HPA037609.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KDM1AO603412EBI-749562,EBI-710124
PRMT6Q96LA82EBI-749562,EBI-912440
TRIP13Q156453EBI-749562,EBI-358993

Protein-protein interaction databases

BioGridi123925. 16 interactions.
IntActiQ96JB6. 11 interactions.
MINTiMINT-1448374.
STRINGi9606.ENSP00000260702.

Structurei

3D structure databases

ProteinModelPortaliQ96JB6.
SMRiQ96JB6. Positions 311-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 133102SRCR 1PROSITE-ProRule annotationAdd
BLAST
Domaini159 – 287129SRCR 2PROSITE-ProRule annotationAdd
BLAST
Domaini311 – 411101SRCR 3PROSITE-ProRule annotationAdd
BLAST
Domaini421 – 529109SRCR 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni533 – 736204Lysyl-oxidase likeAdd
BLAST

Sequence similaritiesi

Belongs to the lysyl oxidase family.Curated
Contains 4 SRCR domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG40770.
GeneTreeiENSGT00760000119251.
HOGENOMiHOG000220841.
HOVERGENiHBG052336.
InParanoidiQ96JB6.
KOiK00280.
OMAiNCLSKSA.
OrthoDBiEOG7SN8C6.
PhylomeDBiQ96JB6.
TreeFamiTF326061.

Family and domain databases

Gene3Di3.10.250.10. 4 hits.
InterProiIPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
[Graphical view]
PfamiPF01186. Lysyl_oxidase. 1 hit.
PF00530. SRCR. 4 hits.
[Graphical view]
PRINTSiPR00074. LYSYLOXIDASE.
PR00258. SPERACTRCPTR.
SMARTiSM00202. SR. 4 hits.
[Graphical view]
SUPFAMiSSF56487. SSF56487. 4 hits.
PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q96JB6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAWSPPATLF LFLLLLGQPP PSRPQSLGTT KLRLVGPESK PEEGRLEVLH
60 70 80 90 100
QGQWGTVCDD NFAIQEATVA CRQLGFEAAL TWAHSAKYGQ GEGPIWLDNV
110 120 130 140 150
RCVGTESSLD QCGSNGWGVS DCSHSEDVGV ICHPRRHRGY LSETVSNALG
160 170 180 190 200
PQGRRLEEVR LKPILASAKQ HSPVTEGAVE VKYEGHWRQV CDQGWTMNNS
210 220 230 240 250
RVVCGMLGFP SEVPVDSHYY RKVWDLKMRD PKSRLKSLTN KNSFWIHQVT
260 270 280 290 300
CLGTEPHMAN CQVQVAPARG KLRPACPGGM HAVVSCVAGP HFRPPKTKPQ
310 320 330 340 350
RKGSWAEEPR VRLRSGAQVG EGRVEVLMNR QWGTVCDHRW NLISASVVCR
360 370 380 390 400
QLGFGSAREA LFGARLGQGL GPIHLSEVRC RGYERTLSDC PALEGSQNGC
410 420 430 440 450
QHENDAAVRC NVPNMGFQNQ VRLAGGRIPE EGLLEVQVEV NGVPRWGSVC
460 470 480 490 500
SENWGLTEAM VACRQLGLGF AIHAYKETWF WSGTPRAQEV VMSGVRCSGT
510 520 530 540 550
ELALQQCQRH GPVHCSHGGG RFLAGVSCMD SAPDLVMNAQ LVQETAYLED
560 570 580 590 600
RPLSQLYCAH EENCLSKSAD HMDWPYGYRR LLRFSTQIYN LGRTDFRPKT
610 620 630 640 650
GRDSWVWHQC HRHYHSIEVF THYDLLTLNG SKVAEGHKAS FCLEDTNCPT
660 670 680 690 700
GLQRRYACAN FGEQGVTVGC WDTYRHDIDC QWVDITDVGP GNYIFQVIVN
710 720 730 740 750
PHYEVAESDF SNNMLQCRCK YDGHRVWLHN CHTGNSYPAN AELSLEQEQR

LRNNLI
Length:756
Mass (Da):84,483
Last modified:December 1, 2001 - v1
Checksum:i13051ACADB922BBC
GO

Sequence cautioni

The sequence AAH07522.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31W → R in AAH13153. (PubMed:15489334)Curated
Sequence conflicti101 – 1011R → Q in AAH13153. (PubMed:15489334)Curated
Sequence conflicti493 – 4931S → G in AAL27543. (PubMed:11691588)Curated
Sequence conflicti539 – 5391A → T in AAL27543. (PubMed:11691588)Curated
Sequence conflicti542 – 5421V → A in AAL27543. (PubMed:11691588)Curated
Sequence conflicti703 – 7031Y → H in AAL27543. (PubMed:11691588)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541R → Q.
Corresponds to variant rs33995374 [ dbSNP | Ensembl ].
VAR_050012
Natural varianti372 – 3721P → T.
Corresponds to variant rs11189525 [ dbSNP | Ensembl ].
VAR_059431
Natural varianti405 – 4051D → A.1 Publication
Corresponds to variant rs1983864 [ dbSNP | Ensembl ].
VAR_050013

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF338441 mRNA. Translation: AAK71934.1.
AY036093 mRNA. Translation: AAK64186.1.
AF395336 mRNA. Translation: AAL27543.1.
AK025542 mRNA. Translation: BAB15167.1.
AK172781 mRNA. Translation: BAD18762.1.
AL139241 Genomic DNA. Translation: CAH72819.1.
CH471066 Genomic DNA. Translation: EAW49886.1.
BC007522 mRNA. Translation: AAH07522.1. Different initiation.
BC013153 mRNA. Translation: AAH13153.1.
CCDSiCCDS7473.1.
RefSeqiNP_115587.6. NM_032211.6.
UniGeneiHs.306814.
Hs.671890.

Genome annotation databases

EnsembliENST00000260702; ENSP00000260702; ENSG00000138131.
GeneIDi84171.
KEGGihsa:84171.
UCSCiuc001kpa.1. human.

Polymorphism databases

DMDMi20177960.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF338441 mRNA. Translation: AAK71934.1 .
AY036093 mRNA. Translation: AAK64186.1 .
AF395336 mRNA. Translation: AAL27543.1 .
AK025542 mRNA. Translation: BAB15167.1 .
AK172781 mRNA. Translation: BAD18762.1 .
AL139241 Genomic DNA. Translation: CAH72819.1 .
CH471066 Genomic DNA. Translation: EAW49886.1 .
BC007522 mRNA. Translation: AAH07522.1 . Different initiation.
BC013153 mRNA. Translation: AAH13153.1 .
CCDSi CCDS7473.1.
RefSeqi NP_115587.6. NM_032211.6.
UniGenei Hs.306814.
Hs.671890.

3D structure databases

ProteinModelPortali Q96JB6.
SMRi Q96JB6. Positions 311-410.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123925. 16 interactions.
IntActi Q96JB6. 11 interactions.
MINTi MINT-1448374.
STRINGi 9606.ENSP00000260702.

PTM databases

PhosphoSitei Q96JB6.

Polymorphism databases

DMDMi 20177960.

Proteomic databases

MaxQBi Q96JB6.
PaxDbi Q96JB6.
PRIDEi Q96JB6.

Protocols and materials databases

DNASUi 84171.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260702 ; ENSP00000260702 ; ENSG00000138131 .
GeneIDi 84171.
KEGGi hsa:84171.
UCSCi uc001kpa.1. human.

Organism-specific databases

CTDi 84171.
GeneCardsi GC10M099997.
HGNCi HGNC:17171. LOXL4.
HPAi CAB033876.
HPA037609.
MIMi 607318. gene.
neXtProti NX_Q96JB6.
PharmGKBi PA30431.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40770.
GeneTreei ENSGT00760000119251.
HOGENOMi HOG000220841.
HOVERGENi HBG052336.
InParanoidi Q96JB6.
KOi K00280.
OMAi NCLSKSA.
OrthoDBi EOG7SN8C6.
PhylomeDBi Q96JB6.
TreeFami TF326061.

Enzyme and pathway databases

Reactomei REACT_150206. Crosslinking of collagen fibrils.
REACT_150366. Elastic fibre formation.

Miscellaneous databases

ChiTaRSi LOXL4. human.
GeneWikii LOXL4.
GenomeRNAii 84171.
NextBioi 73532.
PROi Q96JB6.
SOURCEi Search...

Gene expression databases

Bgeei Q96JB6.
CleanExi HS_LOXL4.
Genevestigatori Q96JB6.

Family and domain databases

Gene3Di 3.10.250.10. 4 hits.
InterProi IPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
[Graphical view ]
Pfami PF01186. Lysyl_oxidase. 1 hit.
PF00530. SRCR. 4 hits.
[Graphical view ]
PRINTSi PR00074. LYSYLOXIDASE.
PR00258. SPERACTRCPTR.
SMARTi SM00202. SR. 4 hits.
[Graphical view ]
SUPFAMi SSF56487. SSF56487. 4 hits.
PROSITEi PS00926. LYSYL_OXIDASE. 1 hit.
PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and biological activity of a novel lysyl oxidase-related gene expressed in cartilage."
    Ito H., Akiyama H., Iguchi H., Iyama K., Miyamoto M., Ohsawa K., Nakamura T.
    J. Biol. Chem. 276:24023-24029(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  2. "Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains."
    Maeki J.M., Tikkanen H., Kivirikko K.I.
    Matrix Biol. 20:493-496(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an altered scavenger receptor cysteine rich domain."
    Asuncion L., Fogelgren B., Fong K.S.K., Fong S.F.T., Kim Y., Csiszar K.
    Matrix Biol. 20:487-491(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  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].
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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], VARIANT ALA-405.
    Tissue: Eye.

Entry informationi

Entry nameiLOXL4_HUMAN
AccessioniPrimary (citable) accession number: Q96JB6
Secondary accession number(s): Q5W0B3
, Q96DY1, Q96PC0, Q9H6T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 128 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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