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P51825 (AFF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AF4/FMR2 family member 1
Alternative name(s):
ALL1-fused gene from chromosome 4 protein
Short name=Protein AF-4
Protein FEL
Proto-oncogene AF4
Gene names
Name:AFF1
Synonyms:AF4, FEL, MLLT2, PBM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1210 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Component of the super elongation complex (SEC), at least composed of EAF1, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3).

Subcellular location

Nucleus Potential.

Involvement in disease

A chromosomal aberration involving AFF1 is associated with acute leukemias. Translocation t(4;11)(q21;q23) with KMT2A/MLL1. The result is a rogue activator protein.

Sequence similarities

Belongs to the AF4 family.

Sequence caution

The sequence AAA36642.1 differs from that shown. Reason: Frameshift at positions 897, 905 and 1178.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

tatP046083EBI-2610180,EBI-6164389From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P51825-1)

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.
Isoform 2 (identifier: P51825-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MAAQS → MAFTERVNSSGN
     1096-1096: A → AR
Note: No experimental confirmation available.
Isoform 3 (identifier: P51825-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1096-1096: A → AR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12101210AF4/FMR2 family member 1
PRO_0000215910

Regions

Compositional bias483 – 49210Poly-Ser
Compositional bias835 – 8439Poly-Ser
Compositional bias866 – 8694Poly-Pro
Compositional bias871 – 8744Poly-Ser

Amino acid modifications

Modified residue2061Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
Modified residue2121Phosphoserine Ref.6 Ref.7 Ref.8
Modified residue2201Phosphothreonine Ref.7
Modified residue5881Phosphoserine Ref.8
Modified residue6811N6-acetyllysine Ref.10
Modified residue6971Phosphothreonine Ref.6 Ref.12
Modified residue7501Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue7551Phosphothreonine Ref.7

Natural variations

Alternative sequence1 – 55MAAQS → MAFTERVNSSGN in isoform 2.
VSP_046095
Alternative sequence10961A → AR in isoform 2 and isoform 3.
VSP_046096
Natural variant2091P → A.
Corresponds to variant rs3733378 [ dbSNP | Ensembl ].
VAR_020370
Natural variant12041Q → K in a breast cancer sample; somatic mutation. Ref.15
VAR_036130

Experimental info

Sequence conflict461K → R in AAA36642. Ref.2
Sequence conflict6241E → G in AAA36642. Ref.2
Sequence conflict7621M → V in BAG62103. Ref.3
Sequence conflict8201R → G in BAG62103. Ref.3
Sequence conflict899 – 9057SASSTKS → VPAVPRV in AAA36642. Ref.2
Sequence conflict928 – 9292EH → AD in AAA36642. Ref.2
Sequence conflict9991I → N in AAA36642. Ref.2
Sequence conflict11401N → I in AAA36642. Ref.2

Secondary structure

... 1210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: F0E334DF8FC2FF04

FASTA1,210131,422
        10         20         30         40         50         60 
MAAQSSLYND DRNLLRIREK ERRNQEAHQE KEAFPEKIPL FGEPYKTAKG DELSSRIQNM 

        70         80         90        100        110        120 
LGNYEEVKEF LSTKSHTHRL DASENRLGKP KYPLIPDKGS SIPSSSFHTS VHHQSIHTPA 

       130        140        150        160        170        180 
SGPLSVGNIS HNPKMAQPRT EPMPSLHAKS CGPPDSQHLT QDRLGQEGFG SSHHKKGDRR 

       190        200        210        220        230        240 
ADGDHCASVT DSAPERELSP LISLPSPVPP LSPIHSNQQT LPRTQGSSKV HGSSNNSKGY 

       250        260        270        280        290        300 
CPAKSPKDLA VKVHDKETPQ DSLVAPAQPP SQTFPPPSLP SKSVAMQQKP TAYVRPMDGQ 

       310        320        330        340        350        360 
DQAPSESPEL KPLPEDYRQQ TFEKTDLKVP AKAKLTKLKM PSQSVEQTYS NEVHCVEEIL 

       370        380        390        400        410        420 
KEMTHSWPPP LTAIHTPSTA EPSKFPFPTK DSQHVSSVTQ NQKQYDTSSK THSNSQQGTS 

       430        440        450        460        470        480 
SMLEDDLQLS DSEDSDSEQT PEKPPSSSAP PSAPQSLPEP VASAHSSSAE SESTSDSDSS 

       490        500        510        520        530        540 
SDSESESSSS DSEENEPLET PAPEPEPPTT NKWQLDNWLT KVSQPAAPPE GPRSTEPPRR 

       550        560        570        580        590        600 
HPESKGSSDS ATSQEHSESK DPPPKSSSKA PRAPPEAPHP GKRSCQKSPA QQEPPQRQTV 

       610        620        630        640        650        660 
GTKQPKKPVK ASARAGSRTS LQGEREPGLL PYGSRDQTSK DKPKVKTKGR PRAAASNEPK 

       670        680        690        700        710        720 
PAVPPSSEKK KHKSSLPAPS KALSGPEPAK DNVEDRTPEH FALVPLTESQ GPPHSGSGSR 

       730        740        750        760        770        780 
TSGCRQAVVV QEDSRKDRLP LPLRDTKLLS PLRDTPPPQS LMVKITLDLL SRIPQPPGKG 

       790        800        810        820        830        840 
SRQRKAEDKQ PPAGKKHSSE KRSSDSSSKL AKKRKGEAER DCDNKKIRLE KEIKSQSSSS 

       850        860        870        880        890        900 
SSSHKESSKT KPSRPSSQSS KKEMLPPPPV SSSSQKPAKP ALKRSRREAD TCGQDPPKSA 

       910        920        930        940        950        960 
SSTKSNHKDS SIPKQRRVEG KGSRSSSEHK GSSGDTANPF PVPSLPNGNS KPGKPQVKFD 

       970        980        990       1000       1010       1020 
KQQADLHMRE AKKMKQKAEL MTDRVGKAFK YLEAVLSFIE CGIATESESQ SSKSAYSVYS 

      1030       1040       1050       1060       1070       1080 
ETVDLIKFIM SLKSFSDATA PTQEKIFAVL CMRCQSILNM AMFRCKKDIA IKYSRTLNKH 

      1090       1100       1110       1120       1130       1140 
FESSSKVAQA PSPCIASTGT PSPLSPMPSP ASSVGSQSSA GSVGSSGVAA TISTPVTIQN 

      1150       1160       1170       1180       1190       1200 
MTSSYVTITS HVLTAFDLWE QAEALTRKNK EFFARLSTNV CTLALNSSLV DLVHYTRQGF 

      1210 
QQLQELTKTP 

« Hide

Isoform 2 [UniParc].

Checksum: 8C9DCE41FF2EA841
Show »

FASTA1,218132,384
Isoform 3 [UniParc].

Checksum: FD08BE7A2BE38BFC
Show »

FASTA1,211131,578

References

« Hide 'large scale' references
[1]"Genes on chromosomes 4, 9, and 19 involved in 11q23 abnormalities in acute leukemia share sequence homology and/or common motifs."
Nakamura T., Alder H., Gu Y., Prasad R., Canaani O., Kamada N., Gale R.P., Lange B., Crist W.M., Nowell P.C., Croce C.M., Canaani E.
Proc. Natl. Acad. Sci. U.S.A. 90:4631-4635(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A serine/proline-rich protein is fused to HRX in t(4;11) acute leukemias."
Morrissey J., Tkachuk D.C., Milatovich A., Francke U., Link M., Cleary M.L.
Blood 81:1124-1131(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHROMOSOMAL TRANSLOCATION WITH KMT2A.
[3]"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. expand/collapse author list , 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).
Tissue: Placenta.
[4]"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. expand/collapse author list , 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].
[5]"The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene."
Gu Y., Nakamura T., Alder H., Prasad R., Canaani O., Cimino G., Croce C.M., Canaani E.
Cell 71:701-708(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH KMT2A.
[6]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212 AND THR-697, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; THR-220; SER-750 AND THR-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; SER-588 AND SER-750, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-750, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-697, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The super elongation complex (SEC) family in transcriptional control."
Luo Z., Lin C., Shilatifard A.
Nat. Rev. Mol. Cell Biol. 13:543-547(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON THE SUPER ELONGATION COMPLEX.
[14]"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding."
Leach B.I., Kuntimaddi A., Schmidt C.R., Cierpicki T., Johnson S.A., Bushweller J.H.
Structure 21:176-183(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 738-779 IN COMPLEX WITH MLLT3.
[15]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-1204.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13773 mRNA. Translation: AAA58360.1.
L25050 mRNA. Translation: AAA36642.1. Frameshift.
AK300364 mRNA. Translation: BAG62103.1.
AC092658 Genomic DNA. No translation available.
AC093779 Genomic DNA. No translation available.
AC093827 Genomic DNA. No translation available.
PIRA58198.
I39410.
RefSeqNP_001160165.1. NM_001166693.1.
NP_005926.1. NM_005935.2.
XP_005263064.1. XM_005263007.1.
XP_005263065.1. XM_005263008.2.
UniGeneHs.480190.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LM0NMR-A738-779[»]
ProteinModelPortalP51825.
SMRP51825. Positions 10-71, 738-779.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110445. 28 interactions.
DIPDIP-56407N.
IntActP51825. 15 interactions.
MINTMINT-1198004.
STRING9606.ENSP00000305689.

PTM databases

PhosphoSiteP51825.

Polymorphism databases

DMDM1703194.

Proteomic databases

PaxDbP51825.
PRIDEP51825.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307808; ENSP00000305689; ENSG00000172493. [P51825-1]
ENST00000395146; ENSP00000378578; ENSG00000172493. [P51825-2]
GeneID4299.
KEGGhsa:4299.
UCSCuc003hqj.4. human. [P51825-1]

Organism-specific databases

CTD4299.
GeneCardsGC04P087856.
HGNCHGNC:7135. AFF1.
MIM159557. gene.
neXtProtNX_P51825.
Orphanet99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBPA30851.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG120323.
HOVERGENHBG004189.
KOK15184.
OMAEPYKTAK.
OrthoDBEOG767390.
PhylomeDBP51825.
TreeFamTF326216.

Gene expression databases

ArrayExpressP51825.
BgeeP51825.
CleanExHS_AFF1.
GenevestigatorP51825.

Family and domain databases

InterProIPR007797. TF_AF4/FMR2.
[Graphical view]
PANTHERPTHR10528. PTHR10528. 1 hit.
PfamPF05110. AF-4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAFF1. human.
GeneWikiAFF1.
GenomeRNAi4299.
NextBio16923.
PROP51825.
SOURCESearch...

Entry information

Entry nameAFF1_HUMAN
AccessionPrimary (citable) accession number: P51825
Secondary accession number(s): B4DTU1, E9PBM3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM