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Q9UPQ3 (AGAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1

Short name=AGAP-1
Alternative name(s):
Centaurin-gamma-2
Short name=Cnt-g2
GTP-binding and GTPase-activating protein 1
Short name=GGAP1
Gene names
Name:AGAP1
Synonyms:CENTG2, KIAA1099
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length857 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-dependent trafficking of proteins in the endosomal-lysosomal system. Ref.1

Enzyme regulation

GAP activity stimulated by phosphatidylinositol 3,4,5-trisphosphate (PIP3) and, to a lesser extent, by phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidic acid potentiates PIP2 stimulation.

Subunit structure

Homodimer. Interacts with several subunits of the AP-3 protein complex: AP3M1, AP3S1 and AP3S2. Interacts with GUCY1A3 and GUCY1B3. Ref.8 Ref.9

Subcellular location

Cytoplasm. Note: Associates with the endocytic compartment. Ref.1 Ref.7

Tissue specificity

Widely expressed. Ref.1 Ref.7 Ref.9 Ref.10

Domain

The PH domain mediates AP-3 binding.

Post-translational modification

Phosphorylated on tyrosines. Ref.9

Sequence similarities

Belongs to the centaurin gamma-like family.

Contains 2 ANK repeats.

Contains 1 Arf-GAP domain.

Contains 1 PH domain.

Sequence caution

The sequence AAH60814.1 differs from that shown. Reason: A 4-nucleotides insertion of unknown origin disrupts the reading frame.

The sequence BAA83051.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA91862.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UPQ3-1)

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: Q9UPQ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     442-494: Missing.
Isoform 3 (identifier: Q9UPQ3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     352-405: MLLKRSGKSL...IDLLRTTVKV → LPFFVLALTA...SAQLSGAMMN
     406-857: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 857857Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1
PRO_0000074218

Regions

Domain346 – 588243PH
Domain609 – 729121Arf-GAP
Repeat768 – 79730ANK 1
Repeat801 – 83030ANK 2
Nucleotide binding78 – 858GTP Potential
Nucleotide binding122 – 1265GTP Potential
Nucleotide binding178 – 1814GTP Potential
Zinc finger624 – 64724C4-type
Region66 – 276211Small GTPase-like

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12
Modified residue8361Phosphothreonine Ref.11

Natural variations

Alternative sequence352 – 40554MLLKR…TTVKV → LPFFVLALTASTYLRPAGAR ARQSSPWPGPRGGQTSPHCA EGPQSAQLSGAMMN in isoform 3.
VSP_011181
Alternative sequence406 – 857452Missing in isoform 3.
VSP_011182
Alternative sequence442 – 49453Missing in isoform 2.
VSP_011183
Natural variant821S → G in an autistic patient. Ref.13
VAR_026446
Natural variant1481D → G. Ref.5
Corresponds to variant rs17855721 [ dbSNP | Ensembl ].
VAR_026447
Natural variant5221P → L.
Corresponds to variant rs17840725 [ dbSNP | Ensembl ].
VAR_048331
Natural variant6711V → I. Ref.1 Ref.2 Ref.3 Ref.6 Ref.13
Corresponds to variant rs2034648 [ dbSNP | Ensembl ].
VAR_026448
Natural variant7981R → G in an autistic patient. Ref.13
VAR_026449
Natural variant8291E → K.
Corresponds to variant rs15718 [ dbSNP | Ensembl ].
VAR_019550
Natural variant8541P → T in a family with an autistic patient. Ref.13
VAR_026450

Experimental info

Mutagenesis6471C → S: Loss of GAP activity. Ref.7
Mutagenesis6521R → K: Loss of GAP activity. No effect on AP-3-binding. Ref.7
Sequence conflict2881T → I in AAK56506. Ref.1
Sequence conflict2881T → I in AAL04172. Ref.2
Sequence conflict2881T → I in BAA83051. Ref.3

Sequences

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

Last modified November 13, 2007. Version 4.
Checksum: BBFDB8DA0ECD55E8

FASTA85794,470
        10         20         30         40         50         60 
MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERVEEP VLQNQIREHV IAIEDAFVNS 

        70         80         90        100        110        120 
QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE IVVDGQSYLL 

       130        140        150        160        170        180 
LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI SFQTVYHYYS RMANYRNTSE IPLVLVGTQD 

       190        200        210        220        230        240 
AISSANPRVI DDARARKLSN DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI 

       250        260        270        280        290        300 
GPCKSLPNSP SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT 

       310        320        330        340        350        360 
ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ GMLLKRSGKS 

       370        380        390        400        410        420 
LNKEWKKKYV TLCDNGVLTY HPSLHDYMQN VHGKEIDLLR TTVKVPGKRP PRATSACAPI 

       430        440        450        460        470        480 
SSPKTNGLSK DMSSLHISPN SGNVTSASGS QMASGISLVS FNSRPDGMHQ RSYSVSSADQ 

       490        500        510        520        530        540 
WSEATVIANS AISSDTGLGD SVCSSPSISS TTSPKLDPPP SPHANRKKHR RKKSTSNFKA 

       550        560        570        580        590        600 
DGLSGTAEEQ EENFEFIIVS LTGQTWHFEA TTYEERDAWV QAIESQILAS LQSCESSKNK 

       610        620        630        640        650        660 
SRLTSQSEAM ALQSIRNMRG NSHCVDCETQ NPNWASLNLG ALMCIECSGI HRNLGTHLSR 

       670        680        690        700        710        720 
VRSLDLDDWP VELIKVMSSI GNELANSVWE ESSQGRTKPS VDSTREEKER WIRAKYEQKL 

       730        740        750        760        770        780 
FLAPLPCTEL SLGQHLLRAT ADEDLRTAIL LLAHGSRDEV NETCGEGDGR TALHLACRKG 

       790        800        810        820        830        840 
NVVLAQLLIW YGVDVTARDA HGNTALAYAR QASSQECIDV LLQYGCPDER FVLMATPNLS 

       850 
RRNNNRNNSS GRVPTII 

« Hide

Isoform 2 [UniParc].

Checksum: 6014F37974C24A52
Show »

FASTA80489,066
Isoform 3 [UniParc].

Checksum: 0B179759420981A9
Show »

FASTA40544,512

References

« Hide 'large scale' references
[1]"GGAPs, a new family of bifunctional GTP-binding and GTPase-activating proteins."
Xia C., Ma W., Stafford L.J., Liu C., Gong L., Martin J.F., Liu M.
Mol. Cell. Biol. 23:2476-2488(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ILE-671, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
Tissue: Heart.
[2]"Kiaa1099 as a member (centaurin gamma2) of the centaurin ArfGAP protein family."
Hong W.
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ILE-671.
[3]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ILE-671.
Tissue: Brain.
[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 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] (ISOFORMS 1 AND 3), VARIANT GLY-148.
Tissue: Placenta.
[6]"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] OF 429-857 (ISOFORM 1), VARIANT ILE-671.
Tissue: Teratocarcinoma.
[7]"AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton."
Nie Z., Stanley K.T., Stauffer S., Jacques K.M., Hirsch D.S., Takei J., Randazzo P.A.
J. Biol. Chem. 277:48965-48975(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-647 AND ARG-652.
[8]"Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1."
Nie Z., Boehm M., Boja E.S., Vass W.C., Bonifacino J.S., Fales H.M., Randazzo P.A.
Dev. Cell 5:513-521(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE AP-3 COMPLEX.
[9]"AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl cyclase."
Meurer S., Pioch S., Wagner K., Mueller-Esterl W., Gross S.
J. Biol. Chem. 279:49346-49354(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH GUCY1A3 AND GUCY1B3.
[10]"The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3."
Nie Z., Fei J., Premont R.T., Randazzo P.A.
J. Cell Sci. 118:3555-3566(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Evaluation of the chromosome 2q37.3 gene CENTG2 as an autism susceptibility gene."
Wassink T.H., Piven J., Vieland V.J., Jenkins L., Frantz R., Bartlett C.W., Goedken R., Childress D., Spence M.A., Smith M., Sheffield V.C.
Am. J. Med. Genet. B Neuropsychiatr. Genet. 136:36-44(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLY-82; ILE-671; GLY-798 AND THR-854.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY033765 mRNA. Translation: AAK56506.1.
AF413078 mRNA. Translation: AAL04172.1.
AB029022 mRNA. Translation: BAA83051.2. Different initiation.
AC012305 Genomic DNA. No translation available.
AC019047 Genomic DNA. No translation available.
AC064874 Genomic DNA. No translation available.
AC073989 Genomic DNA. No translation available.
AC079400 Genomic DNA. No translation available.
BC060814 mRNA. Translation: AAH60814.1. Sequence problems.
BC140856 mRNA. Translation: AAI40857.1.
AK001722 mRNA. Translation: BAA91862.1. Different initiation.
CCDSCCDS2514.1. [Q9UPQ3-2]
CCDS33408.1. [Q9UPQ3-1]
CCDS58756.1. [Q9UPQ3-3]
RefSeqNP_001032208.1. NM_001037131.2. [Q9UPQ3-1]
NP_001231817.1. NM_001244888.1. [Q9UPQ3-3]
NP_055729.2. NM_014914.4. [Q9UPQ3-2]
UniGeneHs.435039.

3D structure databases

ProteinModelPortalQ9UPQ3.
SMRQ9UPQ3. Positions 70-233, 344-422, 530-592, 612-854.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125550. 4 interactions.
IntActQ9UPQ3. 3 interactions.
MINTMINT-6783717.
STRING9606.ENSP00000307634.

PTM databases

PhosphoSiteQ9UPQ3.

Polymorphism databases

DMDM160332373.

Proteomic databases

MaxQBQ9UPQ3.
PaxDbQ9UPQ3.
PRIDEQ9UPQ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304032; ENSP00000307634; ENSG00000157985. [Q9UPQ3-1]
ENST00000336665; ENSP00000338378; ENSG00000157985. [Q9UPQ3-2]
ENST00000409457; ENSP00000387174; ENSG00000157985. [Q9UPQ3-3]
GeneID116987.
KEGGhsa:116987.
UCSCuc002vvs.3. human. [Q9UPQ3-1]
uc002vvt.3. human. [Q9UPQ3-2]
uc021vyp.1. human. [Q9UPQ3-3]

Organism-specific databases

CTD116987.
GeneCardsGC02P236402.
HGNCHGNC:16922. AGAP1.
HPAHPA051405.
MIM608651. gene.
neXtProtNX_Q9UPQ3.
PharmGKBPA26412.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5347.
HOGENOMHOG000007233.
HOVERGENHBG054045.
KOK12491.
OMAEVENNIS.
OrthoDBEOG72VH5V.
PhylomeDBQ9UPQ3.
TreeFamTF317762.

Gene expression databases

ArrayExpressQ9UPQ3.
BgeeQ9UPQ3.
CleanExHS_AGAP1.
GenevestigatorQ9UPQ3.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
2.30.29.30. 2 hits.
3.40.50.300. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF08477. Miro. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSPR00405. REVINTRACTNG.
SMARTSM00248. ANK. 2 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAGAP1. human.
GeneWikiCENTG2.
GenomeRNAi116987.
NextBio80074.
PROQ9UPQ3.
SOURCESearch...

Entry information

Entry nameAGAP1_HUMAN
AccessionPrimary (citable) accession number: Q9UPQ3
Secondary accession number(s): B2RTX7 expand/collapse secondary AC list , Q541S5, Q6P9D7, Q9NV93
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 146 of the entry and version 4 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

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 2

Human chromosome 2: entries, gene names and cross-references to MIM